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Volumn 9, Issue 22, 2003, Pages 1771-1787

Bioorganic approaches towards HIV vaccine design

Author keywords

AIDS; Carbohydrate antigen; Conformations; Envelope glycoproteins; Epitopes; Gp120; Gp41; HIV; Neutralizing antibodies; Peptide antigen; Vaccine; Viral neutralization

Indexed keywords

ANTIRETROVIRUS AGENT; CD4 ANTIGEN; CHEMOKINE RECEPTOR CCR5; CHEMOKINE RECEPTOR CXCR4; CYANOVIRIN N; GLYCOPROTEIN GP 120; GLYCOPROTEIN GP 160; GLYCOPROTEIN GP 41; HUMAN IMMUNODEFICIENCY VIRUS VACCINE; MONOCLONAL ANTIBODY; NEUTRALIZING ANTIBODY; PROTEINASE INHIBITOR; RECOMBINANT PROTEIN; RNA DIRECTED DNA POLYMERASE INHIBITOR; VIRUS ENVELOPE PROTEIN;

EID: 0041488801     PISSN: 13816128     EISSN: None     Source Type: Journal    
DOI: 10.2174/1381612033454432     Document Type: Review
Times cited : (18)

References (185)
  • 1
    • 12444301993 scopus 로고    scopus 로고
    • AIDS epidemic update: December Geneva, 2002
    • Unaids
    • UNAIDS. AIDS epidemic update: December 2002. World Health Organization, Geneva, 2002.
    • (2002) World Health Organization
  • 3
    • 0035912249 scopus 로고    scopus 로고
    • HIV chemotherapy
    • Richman DD. HIV chemotherapy. Nature 2001; 410: 995-1001.
    • (2001) Nature , vol.410 , pp. 995-1001
    • Richman, D.D.1
  • 4
    • 0031773241 scopus 로고    scopus 로고
    • The myth of the medical breakthrough: Smallpox, vaccination, and Jenner reconsidered
    • Gross CP, Sepkowitz KA. The myth of the medical breakthrough: smallpox, vaccination, and Jenner reconsidered. Int J Infect Dis 1998; 3: 54-60.
    • (1998) Int. J. Infect. Dis. , vol.3 , pp. 54-60
    • Gross, C.P.1    Sepkowitz, K.A.2
  • 5
    • 0033979937 scopus 로고    scopus 로고
    • Vaccines in historic evolution and perspective: A narrative of vaccine discoveries
    • Hilleman MR. Vaccines in historic evolution and perspective: a narrative of vaccine discoveries. Vaccine 2000; 18: 1436-47.
    • (2000) Vaccine , vol.18 , pp. 1436-1447
    • Hilleman, M.R.1
  • 6
    • 0030057969 scopus 로고    scopus 로고
    • Current status of poliovirus infections
    • Melnick JL. Current status of poliovirus infections. Clin Microbiol Rev 1996; 9: 293-300.
    • (1996) Clin. Microbiol. Rev. , vol.9 , pp. 293-300
    • Melnick, J.L.1
  • 7
    • 0035065285 scopus 로고    scopus 로고
    • Poliomyelitis eradication: Progress, challenges for the end game, and preparation for the post-eradication era
    • Sutter RW, Tangermann RH, Aylward RB, Cochi SL. Poliomyelitis eradication: progress, challenges for the end game, and preparation for the post-eradication era. Infect Dis Clin North Am 2001; 15: 41-64.
    • (2001) Infect. Dis. Clin. North Am. , vol.15 , pp. 41-64
    • Sutter, R.W.1    Tangermann, R.H.2    Aylward, R.B.3    Cochi, S.L.4
  • 8
    • 0036719574 scopus 로고    scopus 로고
    • Antibodies, viruses and vaccines
    • Burton DR. Antibodies, viruses and vaccines. Nat Rev Immunol 2002; 2: 706-13.
    • (2002) Nat. Rev. Immunol. , vol.2 , pp. 706-713
    • Burton, D.R.1
  • 9
    • 0032960601 scopus 로고    scopus 로고
    • HIV-1 neutralizing antibodies: How full is the bottle?
    • Moore JP, Burton DR. HIV-1 neutralizing antibodies: how full is the bottle? Nat Med 1999; 5: 142-4.
    • (1999) Nat. Med. , vol.5 , pp. 142-144
    • Moore, J.P.1    Burton, D.R.2
  • 10
    • 0035912222 scopus 로고    scopus 로고
    • Cellular immune responses to HIV
    • McMichael AJ, Rowland-Jones SL. Cellular immune responses to HIV. Nature 2001; 410: 980-7.
    • (2001) Nature , vol.410 , pp. 980-987
    • McMichael, A.J.1    Rowland-Jones, S.L.2
  • 11
    • 0033766645 scopus 로고    scopus 로고
    • Control of viremia and prevention of clinical AIDS in rhesus monkeys by cytokine-augmented DNA vaccination
    • Barouch DH, Santra S, Schmitz JE, Kuroda MJ, Fu TM, Wagner W, et al. Control of viremia and prevention of clinical AIDS in rhesus monkeys by cytokine-augmented DNA vaccination. Science 2000; 290: 486-92.
    • (2000) Science , vol.290 , pp. 486-492
    • Barouch, D.H.1    Santra, S.2    Schmitz, J.E.3    Kuroda, M.J.4    Fu, T.M.5    Wagner, W.6
  • 12
    • 0033951746 scopus 로고    scopus 로고
    • Protection of macaques against vaginal transmission of a pathogenic HIV- 1/SIV chimeric virus by passive infusion of neutralizing antibodies
    • Mascola JR, Stiegler G, VanCott TC, Katinger H, Carpenter CB, Hanson CE, et al. Protection of macaques against vaginal transmission of a pathogenic HIV- 1/SIV chimeric virus by passive infusion of neutralizing antibodies. Nat Med 2000; 6: 207-10.
    • (2000) Nat. Med. , vol.6 , pp. 207-210
    • Mascola, J.R.1    Stiegler, G.2    VanCott, T.C.3    Katinger, H.4    Carpenter, C.B.5    Hanson, C.E.6
  • 13
    • 0033952103 scopus 로고    scopus 로고
    • Human neutralizing monoclonal antibodies of the IgGI subtype protect against mucosal simian-human immunodeficiency virus infection
    • Baba TW, Liska V, Hofmann-Lehmann R, Vlasak J, Xu W, Ayehunie S, et al. Human neutralizing monoclonal antibodies of the IgGI subtype protect against mucosal simian-human immunodeficiency virus infection. Nat Med 2000; 6: 200-6.
    • (2000) Nat. Med. , vol.6 , pp. 200-206
    • Baba, T.W.1    Liska, V.2    Hofmann-Lehmann, R.3    Vlasak, J.4    Xu, W.5    Ayehunie, S.6
  • 14
    • 0020596551 scopus 로고
    • Isolation of a T-lymphotropic retrovirus from a patient at risk for acquired immune deficiency syndrome (AIDS)
    • Barre-Sinoussi F, Chermann JC, Rey F, Nugeyre MT, Chamaret S, Gruest J, et al. Isolation of a T-lymphotropic retrovirus from a patient at risk for acquired immune deficiency syndrome (AIDS). Science 1983; 220: 868-71.
    • (1983) Science , vol.220 , pp. 868-871
    • Barre-Sinoussi, F.1    Chermann, J.C.2    Rey, F.3    Nugeyre, M.T.4    Chamaret, S.5    Gruest, J.6
  • 15
    • 0037195627 scopus 로고    scopus 로고
    • A history of HIV discovery
    • Montagnier L. A history of HIV discovery. Science 2002; 298: 1727-8.
    • (2002) Science , vol.298 , pp. 1727-1728
    • Montagnier, L.1
  • 16
    • 0021237243 scopus 로고
    • Detection, isolation, and continuous production of cytopathic retroviruses (HTLV-III) from patients with AIDS and pre-AIDS
    • Popovic M, Sarngadharan MG, Read E, Gallo RC. Detection, isolation, and continuous production of cytopathic retroviruses (HTLV-III) from patients with AIDS and pre-AIDS. Science 1984; 224: 497-500.
    • (1984) Science , vol.224 , pp. 497-500
    • Popovic, M.1    Sarngadharan, M.G.2    Read, E.3    Gallo, R.C.4
  • 17
    • 0021261510 scopus 로고
    • Frequent detection and isolation of cytopathic retroviruses (HTLV-III) from patients with AIDS and at risk for AIDS
    • Gallo RC, Salahuddin SZ, Popovic M, Shearer GM, Kaplan M, Haynes BF, et al. Frequent detection and isolation of cytopathic retroviruses (HTLV-III) from patients with AIDS and at risk for AIDS. Science 1984; 224: 500-3.
    • (1984) Science , vol.224 , pp. 500-503
    • Gallo, R.C.1    Salahuddin, S.Z.2    Popovic, M.3    Shearer, G.M.4    Kaplan, M.5    Haynes, B.F.6
  • 18
    • 0021281132 scopus 로고
    • Serological analysis of a subgroup of human T-lymphotropic retroviruses (HTLV-III) associated with AIDS
    • Schupbach J, Popovic M, Gilden RV, Gonda MA, Sarngadharan MG, Gallo RC. Serological analysis of a subgroup of human T-lymphotropic retroviruses (HTLV-III) associated with AIDS. Science 1984; 224: 503-5.
    • (1984) Science , vol.224 , pp. 503-505
    • Schupbach, J.1    Popovic, M.2    Gilden, R.V.3    Gonda, M.A.4    Sarngadharan, M.G.5    Gallo, R.C.6
  • 19
    • 0021234845 scopus 로고
    • Antibodies reactive with human T-lymphotropic retroviruses (HTLV-III) in the serum of patients with AIDS
    • Sarngadharan MG, Popovic M, Bruch L, Schupbach J, Gallo RC. Antibodies reactive with human T-lymphotropic retroviruses (HTLV-III) in the serum of patients with AIDS. Science 1984; 224: 506-8.
    • (1984) Science , vol.224 , pp. 506-508
    • Sarngadharan, M.G.1    Popovic, M.2    Bruch, L.3    Schupbach, J.4    Gallo, R.C.5
  • 20
    • 0037195631 scopus 로고    scopus 로고
    • The early years of HIV/AIDS
    • Gallo RC. The early years of HIV/AIDS. Science 2002; 298: 1728-30.
    • (2002) Science , vol.298 , pp. 1728-1730
    • Gallo, R.C.1
  • 21
    • 0035912191 scopus 로고    scopus 로고
    • Challenges and opportunities for development of an AIDS vaccine
    • Nabel GJ. Challenges and opportunities for development of an AIDS vaccine. Nature 2001; 410: 1002-7.
    • (2001) Nature , vol.410 , pp. 1002-1007
    • Nabel, G.J.1
  • 22
    • 0037195632 scopus 로고    scopus 로고
    • Prospects for the future
    • Gallo RC. Montagnier L. Prospects for the future. Science 2002; 298: 1730-1.
    • (2002) Science , vol.298 , pp. 1730-1731
    • Gallo, R.C.1    Montagnier, L.2
  • 23
    • 0037178778 scopus 로고    scopus 로고
    • The HIV-1 vaccine race
    • Ho DD, Huang Y. The HIV-1 vaccine race. Cell 2002; 110: 135-8.
    • (2002) Cell , vol.110 , pp. 135-138
    • Ho, D.D.1    Huang, Y.2
  • 24
    • 0036007204 scopus 로고    scopus 로고
    • The past, present and future of HIV-vaccine development: A critical view
    • Bojak A, Deml L, Wagner R. The past, present and future of HIV-vaccine development: a critical view. Drug Discov Today 2002; 7: 36-46.
    • (2002) Drug Discov. Today , vol.7 , pp. 36-46
    • Bojak, A.1    Deml, L.2    Wagner, R.3
  • 25
    • 0036377510 scopus 로고    scopus 로고
    • Development of vaccination strategies that elicit broadly neutralizing antibodies against human immunodeficiency virus type 1 in both the mucosal and systemic immune compartments
    • Hone DM, DeVico AL, Fouts TR, Onyabe DY, Agwale SM, Wambebe CO, et al. Development of vaccination strategies that elicit broadly neutralizing antibodies against human immunodeficiency virus type 1 in both the mucosal and systemic immune compartments. J Hum Virol 2002; 5: 17-23.
    • (2002) J. Hum. Virol. , vol.5 , pp. 17-23
    • Hone, D.M.1    DeVico, A.L.2    Fouts, T.R.3    Onyabe, D.Y.4    Agwale, S.M.5    Wambebe, C.O.6
  • 26
    • 0033960675 scopus 로고    scopus 로고
    • Vaccines and the induction of functional antibodies: Time to look beyond the molecules of natural infection?
    • Burton DR, Parren PW. Vaccines and the induction of functional antibodies: time to look beyond the molecules of natural infection? Nat Med 2000; 6: 123-5.
    • (2000) Nat. Med. , vol.6 , pp. 123-125
    • Burton, D.R.1    Parren, P.W.2
  • 27
    • 0036181247 scopus 로고    scopus 로고
    • Clinical trials of HIV vaccines
    • Graham BS. Clinical trials of HIV vaccines. Annu Rev Med 2002; 53: 207-21.
    • (2002) Annu. Rev. Med. , vol.53 , pp. 207-221
    • Graham, B.S.1
  • 29
    • 0033019853 scopus 로고    scopus 로고
    • The implications of antigenic diversity for vaccine development
    • Zolla-Pazner S, Gomy MK, Nyambi PN. The implications of antigenic diversity for vaccine development. Immunol Lett 1999; 66: 159-64.
    • (1999) Immunol. Lett. , vol.66 , pp. 159-164
    • Zolla-Pazner, S.1    Gomy, M.K.2    Nyambi, P.N.3
  • 30
    • 0030885594 scopus 로고    scopus 로고
    • A vaccine for HIV type 1: The antibody perspective
    • Burton DR. A vaccine for HIV type 1: the antibody perspective. Proc Natl Acad Sci U S A 1997; 94: 10018-23.
    • (1997) Proc. Natl. Acad. Sci. U S A , vol.94 , pp. 10018-10023
    • Burton, D.R.1
  • 32
    • 0025095635 scopus 로고
    • Oligomeric structure of the human immunodeficiency virus type 1 envelope glycoprotein
    • Earl PL, Doms RW, Moss B. Oligomeric structure of the human immunodeficiency virus type 1 envelope glycoprotein. Proc Natl Acad Sci U S A 1990; 87: 648-52.
    • (1990) Proc. Natl. Acad. Sci. U S A , vol.87 , pp. 648-652
    • Earl, P.L.1    Doms, R.W.2    Moss, B.3
  • 35
    • 0028834461 scopus 로고
    • A trimeric structural domain of the HIV-1 transmembrane glycoprotein
    • Lu M, Blacklow SC, Kim PS. A trimeric structural domain of the HIV-1 transmembrane glycoprotein. Nat Struct Biol 1995; 2: 1075-82.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 1075-1082
    • Lu, M.1    Blacklow, S.C.2    Kim, P.S.3
  • 36
    • 0031441562 scopus 로고    scopus 로고
    • A trimeric structural subdomain of the HIV-1 transmembrane glycoprotein
    • Lu M, Kim PS. A trimeric structural subdomain of the HIV-1 transmembrane glycoprotein. J. Biomol. Struct. Dyn. 1997; 15: 465-71.
    • (1997) J. Biomol. Struct. Dyn. , vol.15 , pp. 465-471
    • Lu, M.1    Kim, P.S.2
  • 37
    • 0028107685 scopus 로고
    • Probing the structure of the human immunodeficiency virus surface glycoprotein gp120 with a panel of monoclonal antibodies
    • Moore JP, Sattentau QJ, Wyatt R, Sodroski J. Probing the structure of the human immunodeficiency virus surface glycoprotein gp120 with a panel of monoclonal antibodies. J Virol 1994; 68: 469-84.
    • (1994) J. Virol , vol.68 , pp. 469-484
    • Moore, J.P.1    Sattentau, Q.J.2    Wyatt, R.3    Sodroski, J.4
  • 39
    • 0030746535 scopus 로고    scopus 로고
    • Relevance of the antibody response against human immunodeficiency virus type 1 envelope to vaccine design
    • Parren PW, Gauduin MC, Koup RA, Poignard P, Fisicaro P, Burton DR, et al. Relevance of the antibody response against human immunodeficiency virus type 1 envelope to vaccine design. Immunol Lett 1997; 57: 105-12.
    • (1997) Immunol. Lett. , vol.57 , pp. 105-112
    • Parren, P.W.1    Gauduin, M.C.2    Koup, R.A.3    Poignard, P.4    Fisicaro, P.5    Burton, D.R.6
  • 40
    • 0025292252 scopus 로고
    • Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells
    • Leonard CK, Spellman MW, Riddle L, Harris RJ, Thomas JN, Gregory TJ. Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells. J Biol Chem 1990; 265: 10373-82.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10373-10382
    • Leonard, C.K.1    Spellman, M.W.2    Riddle, L.3    Harris, R.J.4    Thomas, J.N.5    Gregory, T.J.6
  • 41
    • 0025374887 scopus 로고
    • Diversity of oligosaccharide structures on the envelope glycoprotein gp 120 of human immunodeficiency virus 1 from the lymphoblastoid cell line H9. Presence of complex-type oligosaccharides with bisecting N- acetylglucosamine residues
    • Mizuochi T, Matthews TJ, Kato M, Hamako J, Titani K, Solomon J, et al. Diversity of oligosaccharide structures on the envelope glycoprotein gp 120 of human immunodeficiency virus 1 from the lymphoblastoid cell line H9. Presence of complex-type oligosaccharides with bisecting N- acetylglucosamine residues. J Biol Chem 1990; 265: 8519-24.
    • (1990) J. Biol. Chem. , vol.265 , pp. 8519-8524
    • Mizuochi, T.1    Matthews, T.J.2    Kato, M.3    Hamako, J.4    Titani, K.5    Solomon, J.6
  • 42
    • 0023811767 scopus 로고
    • Carbohydrates of human immunodeficiency virus. Structures of oligosaccharides linked to the envelope glycoprotein 120
    • Geyer H, Holschbach C, Hunsmann G, Schneider J. Carbohydrates of human immunodeficiency virus. Structures of oligosaccharides linked to the envelope glycoprotein 120. J Biol Chem 1988; 263: 11760-7.
    • (1988) J. Biol. Chem. , vol.263 , pp. 11760-11867
    • Geyer, H.1    Holschbach, C.2    Hunsmann, G.3    Schneider, J.4
  • 43
    • 0034687168 scopus 로고    scopus 로고
    • Mass spectrometric characterization of the glycosylation pattern of HIV- gp120 expressed in CHO cells
    • Zhu X, Borchers C, Bienstock RJ, Tomer KB. Mass spectrometric characterization of the glycosylation pattern of HIV- gp120 expressed in CHO cells. Biochemistry 2000: 39: 11194-204.
    • (2000) Biochemistry , vol.39 , pp. 11194-11204
    • Zhu, X.1    Borchers, C.2    Bienstock, R.J.3    Tomer, K.B.4
  • 45
    • 0032546844 scopus 로고    scopus 로고
    • The HIV-1 envelope glycoproteins: Fusogens, antigens, and immunogens
    • Wyatt R, Sodroski J. The HIV-1 envelope glycoproteins: fusogens, antigens, and immunogens. Science 1998; 280: 1884-8.
    • (1998) Science , vol.280 , pp. 1884-1888
    • Wyatt, R.1    Sodroski, J.2
  • 46
    • 0036229473 scopus 로고    scopus 로고
    • Role of N-linked glycans in a human immunodeficiency virus envelope glycoprotein: Effects on protein function and the neutralizing antibody response
    • Quinones-Kochs MI, Buonocore L, Rose JK. Role of N-linked glycans in a human immunodeficiency virus envelope glycoprotein: effects on protein function and the neutralizing antibody response. J Virol 2002; 76: 4199-211.
    • (2002) J. Virol. , vol.76 , pp. 4199-4211
    • Quinones-Kochs, M.I.1    Buonocore, L.2    Rose, J.K.3
  • 47
    • 0031749469 scopus 로고    scopus 로고
    • A role for carbohydrates in immune evasion in AIDS
    • Reitter JN, Means RE, Desrosiers RC. A role for carbohydrates in immune evasion in AIDS. Nat Med 1998; 4: 679-84.
    • (1998) Nat. Med. , vol.4 , pp. 679-684
    • Reitter, J.N.1    Means, R.E.2    Desrosiers, R.C.3
  • 48
    • 9044241681 scopus 로고    scopus 로고
    • Human monoclonal antibody 2G12 defines a distinctive neutralization epitope on the gp120 glycoprotein of human immunodeficiency virus type 1
    • Trkola A, Purtscher M, Muster T, Ballaun C, Buchacher A, Sullivan N, et al. Human monoclonal antibody 2G12 defines a distinctive neutralization epitope on the gp120 glycoprotein of human immunodeficiency virus type 1. J Virol 1996; 70: 1100-8.
    • (1996) J. Virol. , vol.70 , pp. 1100-1108
    • Trkola, A.1    Purtscher, M.2    Muster, T.3    Ballaun, C.4    Buchacher, A.5    Sullivan, N.6
  • 49
    • 0028969021 scopus 로고
    • Sequence diversity of V1 and V2 domains of gp120 from human immunodeficiency virus type 1: Lack of correlation with viral phenotype
    • Wang N, Zhu T, Ho DD. Sequence diversity of V1 and V2 domains of gp120 from human immunodeficiency virus type 1: lack of correlation with viral phenotype. J Virol 1995; 69: 2708-15.
    • (1995) J. Virol. , vol.69 , pp. 2708-2715
    • Wang, N.1    Zhu, T.2    Ho, D.D.3
  • 50
    • 0030725907 scopus 로고    scopus 로고
    • Effect of natural HIV-1 envelope V1-V2 sequence diversity on the binding of V3-specific and non-V3-specific antibodies
    • Rencher SD, Hurwitz JL. Effect of natural HIV-1 envelope V1-V2 sequence diversity on the binding of V3-specific and non-V3-specific antibodies. J Acquir Immune Defic Syndr Hum Retrovirol 1997; 16: 69-73.
    • (1997) J. Acquir. Immune Defic. Syndr. Hum. Retrovirol , vol.16 , pp. 69-73
    • Rencher, S.D.1    Hurwitz, J.L.2
  • 51
    • 0032577550 scopus 로고    scopus 로고
    • HIV entry and its inhibition
    • Chan DC, Kim PS. HIV entry and its inhibition. Cell 1998; 93: 681-4.
    • (1998) Cell , vol.93 , pp. 681-684
    • Chan, D.C.1    Kim, P.S.2
  • 52
    • 16144365650 scopus 로고    scopus 로고
    • CD4-induced interaction of primary HIV-1 gp120 glycoproteins with the chemokine receptor CCR-5
    • Wu L, Gerard NP, Wyatt R, Choe H, Parolin C, Ruffing N, et al. CD4-induced interaction of primary HIV-1 gp120 glycoproteins with the chemokine receptor CCR-5. Nature 1996; 384: 179-83.
    • (1996) Nature , vol.384 , pp. 179-183
    • Wu, L.1    Gerard, N.P.2    Wyatt, R.3    Choe, H.4    Parolin, C.5    Ruffing, N.6
  • 53
    • 0034675998 scopus 로고    scopus 로고
    • HIV-1 membrane fusion: Targets of opportunity
    • Doms RW, Moore JP. HIV-1 membrane fusion: targets of opportunity. J Cell Biol 2000; 151: F9-14.
    • (2000) J. Cell Biol. , vol.151
    • Doms, R.W.1    Moore, J.P.2
  • 54
    • 0036889127 scopus 로고    scopus 로고
    • Antigenic properties of the human immunodeficiency virus transmembrane glycoprotein during cell-cell fusion
    • Finnegan CM, Berg W, Lewis GK, DeVico AL. Antigenic properties of the human immunodeficiency virus transmembrane glycoprotein during cell-cell fusion. J Virol 2002; 76: 12123-34.
    • (2002) J. Virol , vol.76 , pp. 12123-12134
    • Finnegan, C.M.1    Berg, W.2    Lewis, G.K.3    DeVico, A.L.4
  • 55
    • 0037069682 scopus 로고    scopus 로고
    • HIV-1 evades anti body-mediated neutralization through conformational masking of receptor-binding sites
    • Kwong PD, Doyle ML, Casper DJ, Cicala C, Leavitt SA, Majeed S, et al. HIV-1 evades anti body-mediated neutralization through conformational masking of receptor-binding sites. Nature 2002; 420: 678-82.
    • (2002) Nature , vol.420 , pp. 678-682
    • Kwong, P.D.1    Doyle, M.L.2    Casper, D.J.3    Cicala, C.4    Leavitt, S.A.5    Majeed, S.6
  • 57
    • 0032509888 scopus 로고    scopus 로고
    • HIV vaccines. Viral envelope fails to deliver?
    • Bolognesi DP, Matthews TJ. HIV vaccines. Viral envelope fails to deliver? Nature 1998; 391: 638-9.
    • (1998) Nature , vol.391 , pp. 638-639
    • Bolognesi, D.P.1    Matthews, T.J.2
  • 58
    • 0035698345 scopus 로고    scopus 로고
    • An HIV vaccine: How and when?
    • Esparza J. An HIV vaccine: how and when? Bull World Health Organ 2001; 79: 1133-7.
    • (2001) Bull World Health Organ , vol.79 , pp. 1133-1137
    • Esparza, J.1
  • 60
    • 0037165309 scopus 로고    scopus 로고
    • AIDS vaccines: On the trail of two trials
    • Moore JP. AIDS vaccines: on the trail of two trials. Nature 2002; 415: 365-6.
    • (2002) Nature , vol.415 , pp. 365-366
    • Moore, J.P.1
  • 61
    • 0032543307 scopus 로고    scopus 로고
    • Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
    • Kwong PD, Wyatt R. Robinson J, Sweet RW, Sodroski J, Hendrickson WA. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 1998; 393: 648-59.
    • (1998) Nature , vol.393 , pp. 648-659
    • Kwong, P.D.1    Wyatt, R.2    Robinson, J.3    Sweet, R.W.4    Sodroski, J.5    Hendrickson, W.A.6
  • 62
    • 0030911709 scopus 로고    scopus 로고
    • Dimeric association and segmental variability in the structure of human CD4
    • Wu H, Kwong PD, Hendrickson WA. Dimeric association and segmental variability in the structure of human CD4. Nature 1997; 387: 527-30.
    • (1997) Nature , vol.387 , pp. 527-530
    • Wu, H.1    Kwong, P.D.2    Hendrickson, W.A.3
  • 63
    • 0026001658 scopus 로고
    • An IgG human monoclonal antibody that reacts with HIV-1/GP120, inhibits virus binding to cells, and neutralizes infection
    • Posner MR, Hideshima T, Cannon T, Mukherjee M, Mayer KH, Byrn RA. An IgG human monoclonal antibody that reacts with HIV-1/GP120, inhibits virus binding to cells, and neutralizes infection. J Immunol 1991; 146: 4325-32.
    • (1991) J. Immunol. , vol.146 , pp. 4325-4332
    • Posner, M.R.1    Hideshima, T.2    Cannon, T.3    Mukherjee, M.4    Mayer, K.H.5    Byrn, R.A.6
  • 64
    • 0025958022 scopus 로고
    • Conformational epitope on gp120 important in CD4 binding and human immunodeficiency virus type 1 neutralization identified by a human monoclonal antibody
    • Ho DD, McKeating JA, Li XL, Moudgil T, Daar ES, Sun NC, et al. Conformational epitope on gp120 important in CD4 binding and human immunodeficiency virus type 1 neutralization identified by a human monoclonal antibody. J Virol 1991; 65: 489-93.
    • (1991) J. Virol , vol.65 , pp. 489-493
    • Ho, D.D.1    McKeating, J.A.2    Li, X.L.3    Moudgil, T.4    Daar, E.S.5    Sun, N.C.6
  • 65
    • 0026801056 scopus 로고
    • Discontinuous, conserved neutralization epitopes overlapping the CD4- binding region of human immunodeficiency virus type 1 gp120 envelope glycoprotein
    • Thali M, Furman C, Ho DD, Robinson J, Tilley S, Pinter A, et al. Discontinuous, conserved neutralization epitopes overlapping the CD4- binding region of human immunodeficiency virus type 1 gp120 envelope glycoprotein. J Virol 1992; 66: 5635-41.
    • (1992) J. Virol , vol.66 , pp. 5635-5641
    • Thali, M.1    Furman, C.2    Ho, D.D.3    Robinson, J.4    Tilley, S.5    Pinter, A.6
  • 66
    • 0025775863 scopus 로고
    • Evidence for non-V3-specific neutralizing antibodies that interfere with gp120/CD4 binding in human immunodeficiency virus 1-infected humans
    • Kang CY, Nara P, Chamat S, Caralli V, Ryskamp T, Haigwood N, et al. Evidence for non-V3-specific neutralizing antibodies that interfere with gp120/CD4 binding in human immunodeficiency virus 1-infected humans. Proc Natl Acad Sci U S A 1991; 88: 6171-5.
    • (1991) Proc. Natl. Acad. Sci. U S A , vol.88 , pp. 6171-6175
    • Kang, C.Y.1    Nara, P.2    Chamat, S.3    Caralli, V.4    Ryskamp, T.5    Haigwood, N.6
  • 67
    • 0026044947 scopus 로고
    • Neutralization of divergent HIV-1 isolates by conformation-dependent human antibodies to Gp120
    • Steimer KS, Scandella CJ, Skiles PV, Haigwood NL. Neutralization of divergent HIV-1 isolates by conformation-dependent human antibodies to Gp120. Science 1991; 254: 105-8.
    • (1991) Science , vol.254 , pp. 105-108
    • Steimer, K.S.1    Scandella, C.J.2    Skiles, P.V.3    Haigwood, N.L.4
  • 68
    • 0027397052 scopus 로고
    • Antibodies to discontinuous or conformationally sensitive epitopes on the gp120 glycoprotein of human immunodeficiency virus type 1 are highly prevalent in sera of infected humans
    • Moore JP, Ho DD. Antibodies to discontinuous or conformationally sensitive epitopes on the gp120 glycoprotein of human immunodeficiency virus type 1 are highly prevalent in sera of infected humans. J Virol 1993; 67: 863-75.
    • (1993) J. Virol , vol.67 , pp. 863-875
    • Moore, J.P.1    Ho, D.D.2
  • 69
    • 0030694769 scopus 로고    scopus 로고
    • The V1/V2 region of human immunodeficiency virus type 1 modulates the sensitivity to neutralization by soluble CD4 and cellular tropism
    • Morikita T, Maeda Y, Fujii S, Matsushita S, Obaru K, Takatsuki K. The V1/V2 region of human immunodeficiency virus type 1 modulates the sensitivity to neutralization by soluble CD4 and cellular tropism. AIDS Res Hum Retroviruses 1997; 13: 1291-9.
    • (1997) AIDS Res. Hum. Retroviruses , vol.13 , pp. 1291-1299
    • Morikita, T.1    Maeda, Y.2    Fujii, S.3    Matsushita, S.4    Obaru, K.5    Takatsuki, K.6
  • 70
    • 0031878761 scopus 로고    scopus 로고
    • Determinants of human immunodeficiency virus type 1 envelope glycoprotein activation by soluble CD4 and monoclonal antibodies
    • Sullivan N, Sun Y, Binley J, Lee J, Barbas CF, 3rd, Parren PW, et al. Determinants of human immunodeficiency virus type 1 envelope glycoprotein activation by soluble CD4 and monoclonal antibodies. J Virol 1998; 72: 6332-8.
    • (1998) J. Virol. , vol.72 , pp. 6332-6338
    • Sullivan, N.1    Sun, Y.2    Binley, J.3    Lee, J.4    Barbas, C.F.5    Parren, P.W.6
  • 71
    • 0028801450 scopus 로고
    • Epitope exposure on functional, oligomeric HIV-1 gp41 molecules
    • Sattentau QJ, Zolla-Pazner S, Poignard P. Epitope exposure on functional, oligomeric HIV-1 gp41 molecules. Virology 1995; 206: 713-7.
    • (1995) Virology , vol.206 , pp. 713-717
    • Sattentau, Q.J.1    Zolla-Pazner, S.2    Poignard, P.3
  • 72
    • 0005000433 scopus 로고
    • HIV-1 neutralization: The consequences of viral adaptation to growth on transformed T cells
    • Moore JP, Ho DD. HIV-1 neutralization: the consequences of viral adaptation to growth on transformed T cells. Aids 1995; 9: S117-36.
    • (1995) Aids , vol.9
    • Moore, J.P.1    Ho, D.D.2
  • 73
    • 0030897825 scopus 로고    scopus 로고
    • Neutralization of the human immunodeficiency virus type 1 primary isolate JR-FL by human monoclonal antibodies correlates with antibody binding to the oligomeric form of the envelope glycoprotein complex
    • Fouts TR, Binley JM, Trkola A, Robinson JE, Moore JP. Neutralization of the human immunodeficiency virus type 1 primary isolate JR-FL by human monoclonal antibodies correlates with antibody binding to the oligomeric form of the envelope glycoprotein complex. J Virol 1997; 71: 2779-85.
    • (1997) J. Virol , vol.71 , pp. 2779-2785
    • Fouts, T.R.1    Binley, J.M.2    Trkola, A.3    Robinson, J.E.4    Moore, J.P.5
  • 74
    • 0030812563 scopus 로고    scopus 로고
    • Replication and neutralization of human immunodeficiency virus type 1 lacking the V1 and V2 variable loops of the gp120 envelope glycoprotein
    • Cao J. Sullivan N, Desjardin E, Parolin C, Robinson J, Wyatt R, et al. Replication and neutralization of human immunodeficiency virus type 1 lacking the V1 and V2 variable loops of the gp120 envelope glycoprotein. J Virol 1997; 71: 9808-12.
    • (1997) J. Virol , vol.71 , pp. 9808-9812
    • Cao, J.1    Sullivan, N.2    Desjardin, E.3    Parolin, C.4    Robinson, J.5    Wyatt, R.6
  • 75
    • 0029119783 scopus 로고
    • Involvement of the V1/V2 variable loop structure in the exposure of human immunodeficiency virus type 1 gp120 epitopes induced by receptor binding
    • Wyatt R, Moore J, Accola M, Desjardin E, Robinson J, Sodroski J. Involvement of the V1/V2 variable loop structure in the exposure of human immunodeficiency virus type 1 gp120 epitopes induced by receptor binding. J Virol 1995; 69: 5723-33.
    • (1995) J. Virol. , vol.69 , pp. 5723-5733
    • Wyatt, R.1    Moore, J.2    Accola, M.3    Desjardin, E.4    Robinson, J.5    Sodroski, J.6
  • 76
    • 0032169831 scopus 로고    scopus 로고
    • Interactions among HIV gp120, CD4, and CXCR4: Dependence on CD4 expression level, gp120 viral origin, conservation of the gp120 COOH- and NH2-termini and V1/V2 and V3 loops, and sensitivity to neutralizing antibodies
    • Mondor I, Moulard M, Ugolini S, Klasse PJ, Hoxie J, Amara A, et al. Interactions among HIV gp120, CD4, and CXCR4: dependence on CD4 expression level, gp120 viral origin, conservation of the gp120 COOH- and NH2-termini and V1/V2 and V3 loops, and sensitivity to neutralizing antibodies. Virology 1998; 248: 394-405.
    • (1998) Virology , vol.248 , pp. 394-405
    • Mondor, I.1    Moulard, M.2    Ugolini, S.3    Klasse, P.J.4    Hoxie, J.5    Amara, A.6
  • 77
    • 0029969919 scopus 로고    scopus 로고
    • Antigenicity of truncated forms of the human immunodeficiency virus type 1 envelope glycoprotein
    • Jeffs SA, McKeating J, Lewis S, Craft H, Biram D, Stephens PE, et al. Antigenicity of truncated forms of the human immunodeficiency virus type 1 envelope glycoprotein. J Gen Virol 1996; 77: 1403-10.
    • (1996) J. Gen. Virol , vol.77 , pp. 1403-1410
    • Jeffs, S.A.1    McKeating, J.2    Lewis, S.3    Craft, H.4    Biram, D.5    Stephens, P.E.6
  • 78
    • 18244414668 scopus 로고    scopus 로고
    • Immunogenicity of full length and truncated forms of the human immunodeficiency virus type I envelope glycoprotein
    • McKeating JA, Shotton C, Jeffs S, Palmer C, Hammond A, Lewis J, et al. Immunogenicity of full length and truncated forms of the human immunodeficiency virus type I envelope glycoprotein. Immunol Lett 1996; 51: 101-5.
    • (1996) Immunol. Lett. , vol.51 , pp. 101-105
    • McKeating, J.A.1    Shotton, C.2    Jeffs, S.3    Palmer, C.4    Hammond, A.5    Lewis, J.6
  • 79
    • 0036167956 scopus 로고    scopus 로고
    • A replication-competent, neutralization-sensitive variant of simian immunodeficiency virus lacking 100 amino acids of envelope
    • Johnson WE, Morgan J, Reitter J, Puffer BA, Czajak S, Doms RW, et al. A replication-competent, neutralization-sensitive variant of simian immunodeficiency virus lacking 100 amino acids of envelope. J Virol 2002; 76: 2075-86.
    • (2002) J. Virol. , vol.76 , pp. 2075-2086
    • Johnson, W.E.1    Morgan, J.2    Reitter, J.3    Puffer, B.A.4    Czajak, S.5    Doms, R.W.6
  • 80
    • 0036842961 scopus 로고    scopus 로고
    • Truncated gp120 envelope glycoprotein of human immunodeficiency virus 1 elicits a broadly reactive neutralizing immune response
    • Jeffs SA, Shotton C, Balfe P, McKeating JA. Truncated gp120 envelope glycoprotein of human immunodeficiency virus 1 elicits a broadly reactive neutralizing immune response. J Gen Virol 2002; 83: 2723-32.
    • (2002) J. Gen. Virol , vol.83 , pp. 2723-2732
    • Jeffs, S.A.1    Shotton, C.2    Balfe, P.3    McKeating, J.A.4
  • 81
    • 0028244285 scopus 로고
    • An N-glycan within the human immunodeficiency virus type 1 gp120 V3 loop affects virus neutralization
    • Back NK, Smit L, De Jong JJ, Keulen W, Schutten M, Goudsmit J, et al. An N-glycan within the human immunodeficiency virus type 1 gp120 V3 loop affects virus neutralization. Virology 1994; 199: 431-8.
    • (1994) Virology , vol.199 , pp. 431-438
    • Back, N.K.1    Smit, L.2    De Jong, J.J.3    Keulen, W.4    Schutten, M.5    Goudsmit, J.6
  • 82
    • 0030842609 scopus 로고    scopus 로고
    • Specific N-linked and O-linked glycosylation modifications in the envelope V1 domain of simian immunodeficiency virus variants that evolve in the host alter recognition by neutralizing antibodies
    • Chackerian B, Rudensey LM, Overbaugh J. Specific N-linked and O-linked glycosylation modifications in the envelope V1 domain of simian immunodeficiency virus variants that evolve in the host alter recognition by neutralizing antibodies. J Virol 1997; 71: 7719-27.
    • (1997) J. Virol , vol.71 , pp. 7719-7727
    • Chackerian, B.1    Rudensey, L.M.2    Overbaugh, J.3
  • 83
    • 0036096976 scopus 로고    scopus 로고
    • Modifications of the human immunodeficiency virus envelope glycoprotein enhance immunogenicity for genetic immunization
    • Chakrabarti BK, Kong WP, Wu BY, Yang ZY, Friborg J, Ling X, et al. Modifications of the human immunodeficiency virus envelope glycoprotein enhance immunogenicity for genetic immunization. J Virol 2002; 76: 5357-68.
    • (2002) J. Virol , vol.76 , pp. 5357-5368
    • Chakrabarti, B.K.1    Kong, W.P.2    Wu, B.Y.3    Yang, Z.Y.4    Friborg, J.5    Ling, X.6
  • 84
    • 0029091404 scopus 로고
    • Lack of induction of antibodies specific for conserved, discontinuous epitopes of HIV-1 envelope glycoprotein by candidate AIDS vaccines
    • VanCott TC, Bethke FR, Burke DS, Redfield RR, Birx DL. Lack of induction of antibodies specific for conserved, discontinuous epitopes of HIV-1 envelope glycoprotein by candidate AIDS vaccines. J Immunol 1995; 155: 4100-10.
    • (1995) J. Immunol , vol.155 , pp. 4100-4110
    • VanCott, T.C.1    Bethke, F.R.2    Burke, D.S.3    Redfield, R.R.4    Birx, D.L.5
  • 85
    • 0030975067 scopus 로고    scopus 로고
    • Antibodies with specificity to native gp120 and neutralization activity against primary human immunodeficiency virus type 1 isolates elicited by immunization with oligomeric gp160
    • VanCott TC, Mascola JR, Kaminski RW, Kalyanaraman V, Hallberg PL, Burnett PR, et al. Antibodies with specificity to native gp120 and neutralization activity against primary human immunodeficiency virus type 1 isolates elicited by immunization with oligomeric gp160. J Virol 1997; 71: 4319-30.
    • (1997) J. Virol , vol.71 , pp. 4319-4330
    • VanCott, T.C.1    Mascola, J.R.2    Kaminski, R.W.3    Kalyanaraman, V.4    Hallberg, P.L.5    Burnett, P.R.6
  • 86
    • 19144365910 scopus 로고    scopus 로고
    • Immunization with envelope subunit vaccine products elicits neutralizing antibodies against laboratory-adapted but not primary isolates of human immunodeficiency virus type 1
    • Mascola JR, Snyder SW, Weislow OS, Belay SM, Belshe RB, Schwartz DH, et al. Immunization with envelope subunit vaccine products elicits neutralizing antibodies against laboratory-adapted but not primary isolates of human immunodeficiency virus type 1. J Infect Dis 1996; 173: 340-8.
    • (1996) J. Infect. Dis. , vol.173 , pp. 340-348
    • Mascola, J.R.1    Snyder, S.W.2    Weislow, O.S.3    Belay, S.M.4    Belshe, R.B.5    Schwartz, D.H.6
  • 87
    • 0034087050 scopus 로고    scopus 로고
    • Characterization of stable, soluble trimers containing complete ectodomains of human immunodeficiency virus type 1 envelope glycoproteins
    • Yang X, Farzan M, Wyatt R, Sodroski J. Characterization of stable, soluble trimers containing complete ectodomains of human immunodeficiency virus type 1 envelope glycoproteins. J. Virol. 2000; 74: 5716-25,
    • (2000) J. Virol. , vol.74 , pp. 5716-5725
    • Yang, X.1    Farzan, M.2    Wyatt, R.3    Sodroski, J.4
  • 88
    • 0034004321 scopus 로고    scopus 로고
    • Modifications that stabilize human immunodeficiency virus envelope glycoprotein trimers in solution
    • Yang X, Florin L, Farzan M, Kolchinsky P, Kwong PD, Sodroski J, et al. Modifications that stabilize human immunodeficiency virus envelope glycoprotein trimers in solution. J. Virol. 2000; 74: 4746-54.
    • (2000) J. Virol. , vol.74 , pp. 4746-4754
    • Yang, X.1    Florin, L.2    Farzan, M.3    Kolchinsky, P.4    Kwong, P.D.5    Sodroski, J.6
  • 89
    • 0035155850 scopus 로고    scopus 로고
    • Improved elicitation of neutralizing antibodies against primary human immunodeficiency viruses by soluble stabilized envelope glycoprotein trimers
    • Yang X, Wyatt R, Sodroski J. Improved elicitation of neutralizing antibodies against primary human immunodeficiency viruses by soluble stabilized envelope glycoprotein trimers. J Virol 2001; 75: 1165-71.
    • (2001) J. Virol. , vol.75 , pp. 1165-1171
    • Yang, X.1    Wyatt, R.2    Sodroski, J.3
  • 90
    • 0036231093 scopus 로고    scopus 로고
    • Highly stable trimers formed by human immunodeficiency virus type 1 envelope glycoproteins fused with the trimeric motif of T4 bacteriophage fibritin
    • Yang X, Lee J, Mahony EM, Kwong PD, Wyatt R, Sodroski J. Highly stable trimers formed by human immunodeficiency virus type 1 envelope glycoproteins fused with the trimeric motif of T4 bacteriophage fibritin. J Virol 2002; 76: 4634-42.
    • (2002) J. Virol. , vol.76 , pp. 4634-4642
    • Yang, X.1    Lee, J.2    Mahony, E.M.3    Kwong, P.D.4    Wyatt, R.5    Sodroski, J.6
  • 91
    • 0027985431 scopus 로고
    • Efficient neutralization of primary isolates of HIV-1 by a recombinant human monoclonal antibody
    • Burton DR, Pyati J, Koduri R, Sharp SJ, Thornton GB, Parren PW, et al. Efficient neutralization of primary isolates of HIV-1 by a recombinant human monoclonal antibody. Science 1994; 266: 1024-7.
    • (1994) Science , vol.266 , pp. 1024-1027
    • Burton, D.R.1    Pyati, J.2    Koduri, R.3    Sharp, S.J.4    Thornton, G.B.5    Parren, P.W.6
  • 92
    • 17944380435 scopus 로고    scopus 로고
    • Crystal structure of a neutralizing human IGG against HIV-1: A template for vaccine design
    • Saphire EO, Parren PW, Pantophlet R, Zwick MB, Morris GM, Rudd PM, et al. Crystal structure of a neutralizing human IGG against HIV-1: a template for vaccine design. Science 2001; 293: 1155-9.
    • (2001) Science , vol.293 , pp. 1155-1159
    • Saphire, E.O.1    Parren, P.W.2    Pantophlet, R.3    Zwick, M.B.4    Morris, G.M.5    Rudd, P.M.6
  • 93
    • 0037213247 scopus 로고    scopus 로고
    • Fine mapping of the interaction of neutralizing and nonneutralizing monoclonal antibodies with the CD4 binding site of human immunodeficiency virus type 1 gp120
    • Pantophlet R, Ollmann Saphire E, Poignard P, Parren PW, Wilson IA, Burton DR. Fine mapping of the interaction of neutralizing and nonneutralizing monoclonal antibodies with the CD4 binding site of human immunodeficiency virus type 1 gp120. J Virol 2003; 77: 642-58.
    • (2003) J. Virol , vol.77 , pp. 642-658
    • Pantophlet, R.1    Ollmann Saphire, E.2    Poignard, P.3    Parren, P.W.4    Wilson, I.A.5    Burton, D.R.6
  • 94
    • 0037223708 scopus 로고    scopus 로고
    • Nonneutralizing antibodies to the CD4-binding site on the gp120 subunit of human immunodeficiency virus type 1 do not interfere with the activity of a neutralizing antibody against the same site
    • Herrera C, Spenlehauer C, Fung MS, Burton DR, Beddows S, Moore JP. Nonneutralizing antibodies to the CD4-binding site on the gp120 subunit of human immunodeficiency virus type 1 do not interfere with the activity of a neutralizing antibody against the same site. J Virol 2003; 77: 1084-91.
    • (2003) J. Virol , vol.77 , pp. 1084-1091
    • Herrera, C.1    Spenlehauer, C.2    Fung, M.S.3    Burton, D.R.4    Beddows, S.5    Moore, J.P.6
  • 95
    • 16044364731 scopus 로고    scopus 로고
    • HIV-1 subtype and second-receptor use
    • Zhang L, Huang Y, He T, Cao Y, Ho DD. HIV-1 subtype and second-receptor use. Nature 1996; 383: 768.
    • (1996) Nature , vol.383 , pp. 768
    • Zhang, L.1    Huang, Y.2    He, T.3    Cao, Y.4    Ho, D.D.5
  • 96
    • 15844419153 scopus 로고    scopus 로고
    • Identification of a major co-receptor for primary isolates of HIV-1
    • Deng H, Liu R, Ellmeier W, Choe S, Unutmaz D, Burkhart M, et al. Identification of a major co-receptor for primary isolates of HIV-1. Nature 1996; 381: 661-6.
    • (1996) Nature , vol.381 , pp. 661-666
    • Deng, H.1    Liu, R.2    Ellmeier, W.3    Choe, S.4    Unutmaz, D.5    Burkhart, M.6
  • 97
    • 0031575431 scopus 로고    scopus 로고
    • Change in coreceptor use correlates with disease progression in HIV-1-infected individuals
    • Connor RI, Sheridan KE, Ceradini D, Choe S, Landau NR. Change in coreceptor use correlates with disease progression in HIV-1--infected individuals. J. Exp. Med. 1997; 185: 621-8.
    • (1997) J. Exp. Med. , vol.185 , pp. 621-628
    • Connor, R.I.1    Sheridan, K.E.2    Ceradini, D.3    Choe, S.4    Landau, N.R.5
  • 98
    • 15844388931 scopus 로고    scopus 로고
    • Homozygous defect in HIV-1 coreceptor accounts for resistance of some multiply-exposed individuals to HIV-1 infection
    • Liu R, Paxton WA, Choe S. Ceradini D, Martin SR, Horuk R, et al. Homozygous defect in HIV-1 coreceptor accounts for resistance of some multiply-exposed individuals to HIV-1 infection. Cell 1996; 86: 367-77.
    • (1996) Cell , vol.86 , pp. 367-377
    • Liu, R.1    Paxton, W.A.2    Choe, S.3    Ceradini, D.4    Martin, S.R.5    Horuk, R.6
  • 99
    • 16044373004 scopus 로고    scopus 로고
    • Resistance to HIV-1 infection in caucasian individuals bearing mutant alleles of the CCR-5 chemokine receptor gene
    • Samson M, Libert F, Doranz BJ, Rucker J, Liesnard C, Farber CM, et al. Resistance to HIV-1 infection in caucasian individuals bearing mutant alleles of the CCR-5 chemokine receptor gene. Nature 1996; 382: 722-5.
    • (1996) Nature , vol.382 , pp. 722-725
    • Samson, M.1    Libert, F.2    Doranz, B.J.3    Rucker, J.4    Liesnard, C.5    Farber, C.M.6
  • 100
    • 0032103577 scopus 로고    scopus 로고
    • Chemokine receptor allelic polymorphisms: Relationships to HIV resistance and disease progression
    • Paxton WA, Kang S. Chemokine receptor allelic polymorphisms: relationships to HIV resistance and disease progression. Semin Immunol 1998; 10: 187-94.
    • (1998) Semin. Immunol. , vol.10 , pp. 187-194
    • Paxton, W.A.1    Kang, S.2
  • 101
    • 0027256814 scopus 로고
    • Characterization of conserved human immunodeficiency virus type 1 gp120 neutralization epitopes exposed upon gp120-CD4 binding
    • Thali M, Moore JP, Furman C, Charles M, Ho DD, Robinson J, et al. Characterization of conserved human immunodeficiency virus type 1 gp120 neutralization epitopes exposed upon gp120-CD4 binding. J Virol 1993; 67: 3978-88.
    • (1993) J. Virol , vol.67 , pp. 3978-3988
    • Thali, M.1    Moore, J.P.2    Furman, C.3    Charles, M.4    Ho, D.D.5    Robinson, J.6
  • 103
    • 16144365317 scopus 로고    scopus 로고
    • CD4-dependent, antibody-sensitive interactions between HIV-1 and its co- receptor CCR-5
    • Trkola A, Dragic T, Arthos J, Binley JM, Olson WC, Allaway GP, et al. CD4-dependent, antibody-sensitive interactions between HIV-1 and its co- receptor CCR-5. Nature 1996; 384: 184-7.
    • (1996) Nature , vol.384 , pp. 184-187
    • Trkola, A.1    Dragic, T.2    Arthos, J.3    Binley, J.M.4    Olson, W.C.5    Allaway, G.P.6
  • 104
    • 0033012398 scopus 로고    scopus 로고
    • Chemokine receptors as HIV-1 coreceptors: Roles in viral entry, tropism, and disease
    • Berger EA, Murphy PM, Farber JM. Chemokine receptors as HIV-1 coreceptors: roles in viral entry, tropism, and disease. Annu Rev Immunol 1999; 17: 657-700.
    • (1999) Annu. Rev. Immunol. , vol.17 , pp. 657-700
    • Berger, E.A.1    Murphy, P.M.2    Farber, J.M.3
  • 105
    • 0025016461 scopus 로고
    • Antibody raised against soluble CD4-rgp120 complex recognizes the CD4 moiety and blocks membrane fusion without inhibiting CD4-gp120 binding
    • Celada F, Cambiaggi C, Maccari J, Burastero S, Gregory T, Patzer E, et al. Antibody raised against soluble CD4-rgp120 complex recognizes the CD4 moiety and blocks membrane fusion without inhibiting CD4-gp120 binding. J Exp Med 1990; 172: 1143-50.
    • (1990) J. Exp. Med. , vol.172 , pp. 1143-1150
    • Celada, F.1    Cambiaggi, C.2    Maccari, J.3    Burastero, S.4    Gregory, T.5    Patzer, E.6
  • 106
    • 0028111660 scopus 로고
    • Immunization with a soluble CD4-gp120 complex preferentially induces neutralizing anti-human immunodeficiency virus type 1 antibodies directed to conformation-dependent epitopes of gp120
    • Kang CY, Hariharan K, Nara PL, Sodroski J, Moore JP. Immunization with a soluble CD4-gp120 complex preferentially induces neutralizing anti-human immunodeficiency virus type 1 antibodies directed to conformation-dependent epitopes of gp120. J. Virol 1994; 68: 5854-62.
    • (1994) J. Virol , vol.68 , pp. 5854-5862
    • Kang, C.Y.1    Hariharan, K.2    Nara, P.L.3    Sodroski, J.4    Moore, J.P.5
  • 107
    • 0027324106 scopus 로고
    • HIV binding to its receptor creates specific epitopes for the CD4/gp120 complex
    • Gershoni JM, Denisova G, Raviv D, Smorodinsky NI, Buyaner D. HIV binding to its receptor creates specific epitopes for the CD4/gp120 complex. Faseb J 1993; 7: 1185-7.
    • (1993) Faseb. J. , vol.7 , pp. 1185-1187
    • Gershoni, J.M.1    Denisova, G.2    Raviv, D.3    Smorodinsky, N.I.4    Buyaner, D.5
  • 109
    • 0031065252 scopus 로고    scopus 로고
    • Conformational transitions in CD4 due to complexation with HIV envelope glycoprotein gp120
    • Denisova G, Raviv D, Mondor I, Sattentau QJ, Gershoni JM. Conformational transitions in CD4 due to complexation with HIV envelope glycoprotein gp120. J Immunol 1997; 158: 1157-64.
    • (1997) J. Immunol. , vol.158 , pp. 1157-1164
    • Denisova, G.1    Raviv, D.2    Mondor, I.3    Sattentau, Q.J.4    Gershoni, J.M.5
  • 110
    • 0029927680 scopus 로고    scopus 로고
    • Covalently crosslinked complexes of human immunodeficiency virus type 1 (HIV-1) gp120 and CD4 receptor elicit a neutralizing immune response that includes antibodies selective for primary virus isolates
    • DeVico A, Silver A, Thronton AM, Sarngadharan MG, Pal R. Covalently crosslinked complexes of human immunodeficiency virus type 1 (HIV-1) gp120 and CD4 receptor elicit a neutralizing immune response that includes antibodies selective for primary virus isolates. Virology 1996; 218: 258-63.
    • (1996) Virology , vol.218 , pp. 258-263
    • DeVico, A.1    Silver, A.2    Thronton, A.M.3    Sarngadharan, M.G.4    Pal, R.5
  • 111
    • 0037015043 scopus 로고    scopus 로고
    • Crosslinked HIV-1 envelope-CD4 receptor complexes elicit broadly cross- reactive neutralizing antibodies in rhesus macaques
    • Fouts T, Godfrey K, Bobb K, Montefiori D, Hanson CV, Kalyanaraman VS, et al. Crosslinked HIV-1 envelope-CD4 receptor complexes elicit broadly cross- reactive neutralizing antibodies in rhesus macaques. Proc Natl Acad Sci U S A 2002; 99: 11842-7.
    • (2002) Proc. Natl. Acad. Sci. U S A , vol.99 , pp. 11842-11847
    • Fouts, T.1    Godfrey, K.2    Bobb, K.3    Montefiori, D.4    Hanson, C.V.5    Kalyanaraman, V.S.6
  • 112
    • 0034467954 scopus 로고    scopus 로고
    • Expression and characterization of a single-chain polypeptide analogue of the human immunodeficiency virus type 1 gp120-CD4 receptor complex
    • Fouts TR, Tuskan R, Godfrey K, Reitz M, Hone D, Lewis GK, et al. Expression and characterization of a single-chain polypeptide analogue of the human immunodeficiency virus type 1 gp120-CD4 receptor complex. J Virol 2000; 74: 11427-36.
    • (2000) J. Virol , vol.74 , pp. 11427-11436
    • Fouts, T.R.1    Tuskan, R.2    Godfrey, K.3    Reitz, M.4    Hone, D.5    Lewis, G.K.6
  • 113
    • 0037076265 scopus 로고    scopus 로고
    • Broadly cross-reactive HIV-1-neutralizing human monoclonal Fab selected for binding to gp120-CD4-CCR5 complexes
    • Moulard M, Phogat SK, Shu Y, Labrijn AF, Xiao X, Binley JM, et al. Broadly cross-reactive HIV-1-neutralizing human monoclonal Fab selected for binding to gp120-CD4-CCR5 complexes. Proc Natl Acad Sci U S A 2002; 99: 6913-8.
    • (2002) Proc. Natl. Acad. Sci. U S A , vol.99 , pp. 6913-6918
    • Moulard, M.1    Phogat, S.K.2    Shu, Y.3    Labrijn, A.F.4    Xiao, X.5    Binley, J.M.6
  • 114
    • 0037018921 scopus 로고    scopus 로고
    • Conserved structures exposed in HIV-1 envelope glycoproteins stabilized by flexible linkers as potent entry inhibitors and potential immunogens
    • Chow YH, Wei OL, Phogat S, Sidorov IA, Fouts TR, Broder CC, et al. Conserved structures exposed in HIV-1 envelope glycoproteins stabilized by flexible linkers as potent entry inhibitors and potential immunogens. Biochemistry 2002; 41: 7176-82.
    • (2002) Biochemistry , vol.41 , pp. 7176-7182
    • Chow, Y.H.1    Wei, O.L.2    Phogat, S.3    Sidorov, I.A.4    Fouts, T.R.5    Broder, C.C.6
  • 115
    • 12244281787 scopus 로고    scopus 로고
    • Rational design of a CD4 mimic that inhibits HIV-1 entry and exposes cryptic neutralization epitopes
    • Martin L, Stricher F, Misse D, Sironi F, Pugniere M, Barthe P, et al. Rational design of a CD4 mimic that inhibits HIV-1 entry and exposes cryptic neutralization epitopes. Nat Biotechnol 2003; 21: 71-6.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 71-76
    • Martin, L.1    Stricher, F.2    Misse, D.3    Sironi, F.4    Pugniere, M.5    Barthe, P.6
  • 116
    • 0028865465 scopus 로고
    • Cross-clade neutralization of primary isolates of human immunodeficiency virus type 1 by human monoclonal antibodies and tetrameric CD4-IgG
    • Trkola A, Pomales AB, Yuan H, Korber B, Maddon PJ, Allaway GP, et al. Cross-clade neutralization of primary isolates of human immunodeficiency virus type 1 by human monoclonal antibodies and tetrameric CD4-IgG. J Virol 1995; 69: 6609-17.
    • (1995) J. Virol , vol.69 , pp. 6609-6617
    • Trkola, A.1    Pomales, A.B.2    Yuan, H.3    Korber, B.4    Maddon, P.J.5    Allaway, G.P.6
  • 117
    • 0036637385 scopus 로고    scopus 로고
    • The mannose-dependent epitope for neutralizing antibody 2G12 on human immunodeficiency virus type 1 glycoprotein gp120
    • Sanders RW, Venturi M, Schiffner L, Kalyanaraman R, Katinger H, Lloyd KO, et al. The mannose-dependent epitope for neutralizing antibody 2G12 on human immunodeficiency virus type 1 glycoprotein gp120. J Virol 2002; 76: 7293-305.
    • (2002) J. Virol , vol.76 , pp. 7293-7305
    • Sanders, R.W.1    Venturi, M.2    Schiffner, L.3    Kalyanaraman, R.4    Katinger, H.5    Lloyd, K.O.6
  • 118
    • 18244422922 scopus 로고    scopus 로고
    • The broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2G12 recognizes a cluster of alphal-->2 mannose residues on the outer face of gp120
    • Scanlan CN, Pantophlet R, Wormald MR, Ollmann Saphire E, Stanfield R, Wilson IA, et al. The broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2G12 recognizes a cluster of alphal-->2 mannose residues on the outer face of gp120. J Virol 2002; 76: 7306-21.
    • (2002) J. Virol , vol.76 , pp. 7306-7321
    • Scanlan, C.N.1    Pantophlet, R.2    Wormald, M.R.3    Ollmann Saphire, E.4    Stanfield, R.5    Wilson, I.A.6
  • 119
    • 0032080696 scopus 로고    scopus 로고
    • Natural IgM antibodies in baby rabbit serum bind high-mannose glycans on HIV type 1 glycoprotein 120/160 and activate classic complement pathway
    • Gerencer M, Barrett PN, Kistner O, Mitterer A, Dorner F. Natural IgM antibodies in baby rabbit serum bind high-mannose glycans on HIV type 1 glycoprotein 120/160 and activate classic complement pathway. AIDS Res Hum Retroviruses 1998; 14: 599-605.
    • (1998) AIDS Res. Hum. Retroviruses , vol.14 , pp. 599-605
    • Gerencer, M.1    Barrett, P.N.2    Kistner, O.3    Mitterer, A.4    Dorner, F.5
  • 120
    • 0027229359 scopus 로고
    • Neutralizing antibody response during human immunodeficiency virus type 1 infection: Type and group specificity and viral escape
    • Arendrup M, Sonnerborg A, Svennerholm B, Akerblom L, Nielsen C, Clausen H, et al. Neutralizing antibody response during human immunodeficiency virus type 1 infection: type and group specificity and viral escape. J Gen Virol 1993; 74: 855-63.
    • (1993) J. Gen. Virol , vol.74 , pp. 855-863
    • Arendrup, M.1    Sonnerborg, A.2    Svennerholm, B.3    Akerblom, L.4    Nielsen, C.5    Clausen, H.6
  • 121
    • 0025997687 scopus 로고
    • Effect of anti-carbohydrate antibodies on HIV infection in a monocytic cell line (U937)
    • Hansen JE, Nielsen C, Clausen H, Mathiesen LR, Nielsen JO. Effect of anti-carbohydrate antibodies on HIV infection in a monocytic cell line (U937). Antiviral Res 1991; 16: 233-42.
    • (1991) Antiviral. Res , vol.16 , pp. 233-242
    • Hansen, J.E.1    Nielsen, C.2    Clausen, H.3    Mathiesen, L.R.4    Nielsen, J.O.5
  • 122
    • 0025834187 scopus 로고
    • Recognition of human immunodeficiency virus glycopróteins by natural anti-carbohydrate antibodies in human serum
    • Tomiyama T, Lake D, Masuho Y, Hersh EM. Recognition of human immunodeficiency virus glycopróteins by natural anti-carbohydrate antibodies in human serum. Biochem Biophys Res Commun 1991; 177: 279-85.
    • (1991) Biochem. Biophys. Res. Commun. , vol.177 , pp. 279-285
    • Tomiyama, T.1    Lake, D.2    Masuho, Y.3    Hersh, E.M.4
  • 123
    • 0034598905 scopus 로고    scopus 로고
    • DC-SIGN, a dendritic cell-specific HIV-1-binding protein that enhances transinfection of T cells
    • Geijtenbeek TB, Kwon DS, Torensma R, van Vliet SJ, van Duijnhoven GC, Middel J, et al. DC-SIGN, a dendritic cell-specific HIV-1-binding protein that enhances transinfection of T cells. Cell 2000; 100: 587-97.
    • (2000) Cell , vol.100 , pp. 587-597
    • Geijtenbeek, T.B.1    Kwon, D.S.2    Torensma, R.3    van Vliet, S.J.4    van Duijnhoven, G.C.5    Middel, J.6
  • 124
    • 0034598934 scopus 로고    scopus 로고
    • Identification of DC-SIGN, a novel dendritic cell-specific ICAM-3 receptor that supports primary immune responses
    • Geijtenbeek TB, Torensma R, van Vliet SJ, van Duijnhoven GC, Adema GJ, van Kooyk Y, et al. Identification of DC-SIGN, a novel dendritic cell-specific ICAM-3 receptor that supports primary immune responses. Cell 2000; 100: 575-85.
    • (2000) Cell , vol.100 , pp. 575-585
    • Geijtenbeek, T.B.1    Torensma, R.2    van Vliet, S.J.3    van Duijnhoven, G.C.4    Adema, G.J.5    van Kooyk, Y.6
  • 125
    • 0035956986 scopus 로고    scopus 로고
    • DC-SIGNR, a DC-SIGN homologue expressed in endothelial cells, binds to human and simian immunodeficiency viruses and activates infection in trans
    • Pohlmann S, Soilleux EJ, Baribaud F, Leslie GJ, Morris LS, Trowsdale J, et al. DC-SIGNR, a DC-SIGN homologue expressed in endothelial cells, binds to human and simian immunodeficiency viruses and activates infection in trans. Proc Natl Acad Sci U S A 2001; 98: 2670-5.
    • (2001) Proc. Natl. Acad. Sci. U S A , vol.98 , pp. 2670-2675
    • Pohlmann, S.1    Soilleux, E.J.2    Baribaud, F.3    Leslie, G.J.4    Morris, L.S.5    Trowsdale, J.6
  • 126
    • 0035800757 scopus 로고    scopus 로고
    • A novel mechanism of carbohydrate recognition by the C-type lectins DC-SIGN and DC-SIGNR. Subunit organization and binding to multivalent ligands
    • Mitchell DA, Fadden AJ, Drickamer K. A novel mechanism of carbohydrate recognition by the C-type lectins DC-SIGN and DC-SIGNR. Subunit organization and binding to multivalent ligands. J Biol Chem 2001; 276: 28939-45.
    • (2001) J. Biol. Chem. , vol.276 , pp. 28939-28945
    • Mitchell, D.A.1    Fadden, A.J.2    Drickamer, K.3
  • 127
    • 0035824446 scopus 로고    scopus 로고
    • Structural basis for selective recognition of oligosaccharides by DC-SIGN and DC-SIGNR
    • Feinberg H, Mitchell DA, Drickamer K, Weis WI. Structural basis for selective recognition of oligosaccharides by DC-SIGN and DC-SIGNR. Science 2001; 294: 2163-6.
    • (2001) Science , vol.294 , pp. 2163-2166
    • Feinberg, H.1    Mitchell, D.A.2    Drickamer, K.3    Weis, W.I.4
  • 128
    • 0036892624 scopus 로고    scopus 로고
    • Human immunodeficiency virus envelope (gp120) binding to DC-SIGN and primary dendritic cells is carbohydrate dependent but does not involve 2G12 or cyanovirin binding sites: Implications for structural analyses of gp120-DC-SIGN binding
    • Hong PW, Flummerfelt KB, de Parseval A, Gurney K, Elder JH, Lee B. Human immunodeficiency virus envelope (gp120) binding to DC-SIGN and primary dendritic cells is carbohydrate dependent but does not involve 2G12 or cyanovirin binding sites: implications for structural analyses of gp120-DC-SIGN binding. J Virol 2002; 76: 12855-65.
    • (2002) J. Virol , vol.76 , pp. 12855-12865
    • Hong, P.W.1    Flummerfelt, K.B.2    de Parseval, A.3    Gurney, K.4    Elder, J.H.5    Lee, B.6
  • 129
    • 0024584844 scopus 로고
    • A human serum mannose-binding protein inhibits in vitro infection by the human immunodeficiency virus
    • Ezekowitz RA, Kuhlman M, Groopman JE, Byrn RA. A human serum mannose-binding protein inhibits in vitro infection by the human immunodeficiency virus. J Exp Med 1989; 169: 185-96.
    • (1989) J. Exp. Med. , vol.169 , pp. 185-196
    • Ezekowitz, R.A.1    Kuhlman, M.2    Groopman, J.E.3    Byrn, R.A.4
  • 130
    • 0024346777 scopus 로고
    • Correlation between carbohydrate structures on the envelope glycoprotein gp120 of HIV-1 and HIV-2 and syncytium inhibition with lectins
    • Hansen JE, Nielsen CM, Nielsen C, Heegaard P, Mathiesen LR, Nielsen JO. Correlation between carbohydrate structures on the envelope glycoprotein gp120 of HIV-1 and HIV-2 and syncytium inhibition with lectins. AIDS 1989; 3: 635-41.
    • (1989) AIDS , vol.3 , pp. 635-641
    • Hansen, J.E.1    Nielsen, C.M.2    Nielsen, C.3    Heegaard, P.4    Mathiesen, L.R.5    Nielsen, J.O.6
  • 131
    • 0026020005 scopus 로고
    • Alpha-(1-3)- and alpha-(1-6)-D-mannose-specific plant lectins are markedly inhibitory to human immunodeficiency virus and cytomegalovirus infections in vitro
    • Balzarini J, Schols D, Neyts J, Van Damme E, Peumans W, De Clercq E. Alpha-(1-3)- and alpha-(1-6)-D-mannose-specific plant lectins are markedly inhibitory to human immunodeficiency virus and cytomegalovirus infections in vitro. Antimicrob Agents Chemother 1991; 35: 410-6.
    • (1991) Antimicrob. Agents Chemother. , vol.35 , pp. 410-416
    • Balzarini, J.1    Schols, D.2    Neyts, J.3    Van Damme, E.4    Peumans, W.5    De Clercq, E.6
  • 134
    • 0034028110 scopus 로고    scopus 로고
    • Interaction of mannose-binding lectin with primary isolates of human immunodeficiency virus type 1
    • Saifuddin M, Hart ML, Gewurz H, Zhang Y, Spear GT. Interaction of mannose-binding lectin with primary isolates of human immunodeficiency virus type 1. J Gen Virol 2000; 81: 949-55.
    • (2000) J. Gen. Virol , vol.81 , pp. 949-955
    • Saifuddin, M.1    Hart, M.L.2    Gewurz, H.3    Zhang, Y.4    Spear, G.T.5
  • 135
    • 0030790094 scopus 로고    scopus 로고
    • Discovery of cyanovirin-N, a novel human immunodeficiency virus- inactivating protein that binds viral surface envelope glycoprotein gp120: Potential applications to microbicide development
    • Boyd MR, Gustafson KR, McMahon JB, Shoemaker RH, O'Keefe BR, Mori T, et al. Discovery of cyanovirin-N, a novel human immunodeficiency virus- inactivating protein that binds viral surface envelope glycoprotein gp120: potential applications to microbicide development. Antimicrob Agents Chemother 1997; 41: 1521-30.
    • (1997) Antimicrob. Agents Chemother , vol.41 , pp. 1521-1530
    • Boyd, M.R.1    Gustafson, K.R.2    McMahon, J.B.3    Shoemaker, R.H.4    O'Keefe, B.R.5    Mori, T.6
  • 136
    • 0033997468 scopus 로고    scopus 로고
    • Multiple antiviral activities of cyanovirin-N: Blocking of human immunodeficiency virus type 1 gp120 interaction with CD4 and coreceptor and inhibition of diverse enveloped viruses
    • Dey B, Lerner DL, Lusso P, Boyd MR, Elder JH Berger EA. Multiple antiviral activities of cyanovirin-N: blocking of human immunodeficiency virus type 1 gp120 interaction with CD4 and coreceptor and inhibition of diverse enveloped viruses. J Virol 2000; 74: 4562-9.
    • (2000) J. Virol , vol.74 , pp. 4562-4569
    • Dey, B.1    Lerner, D.L.2    Lusso, P.3    Boyd, M.R.4    Elder, J.H.5    Berger, E.A.6
  • 137
    • 0034791996 scopus 로고    scopus 로고
    • Solution structure of a cyanovirin-N:Man alpha 1-2Man alpha complex: Structural basis for high-affinity carbohydrate-mediated binding to gp120
    • Bewley CA. Solution structure of a cyanovirin-N:Man alpha 1-2Man alpha complex: structural basis for high-affinity carbohydrate-mediated binding to gp120. Structure (Camb) 2001; 9: 931-40.
    • (2001) Structure (Camb) , vol.9 , pp. 931-940
    • Bewley, C.A.1
  • 138
    • 0034799906 scopus 로고    scopus 로고
    • The potent anti-HIV protein cyanovirin-N contains two novel carbohydrate binding sites that selectively bind to Man(8) D1D3 and Man(9) with nanomolar affinity: Implications for binding to the HIV envelope protein gp120
    • Bewley CA, Otero-Quintero S. The potent anti-HIV protein cyanovirin-N contains two novel carbohydrate binding sites that selectively bind to Man(8) D1D3 and Man(9) with nanomolar affinity: implications for binding to the HIV envelope protein gp120. J Am Chem Soc 2001; 123: 3892-902.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 3892-3902
    • Bewley, C.A.1    Otero-Quintero, S.2
  • 139
    • 0035028207 scopus 로고    scopus 로고
    • Cyanovirin-N defines a new class of antiviral agent targeting N-linked, high-mannose glycans in an oligosaccharide-specific manner
    • Bolmstedt AJ, O'Keefe BR. Shenoy SR, McMahon JB, Boyd MR. Cyanovirin-N defines a new class of antiviral agent targeting N-linked, high-mannose glycans in an oligosaccharide-specific manner. Mol Pharmacol 2001; 59: 949-54.
    • (2001) Mol. Pharmacol. , vol.59 , pp. 949-954
    • Bolmstedt, A.J.1    O'Keefe, B.R.2    Shenoy, S.R.3    McMahon, J.B.4    Boyd, M.R.5
  • 140
    • 0037325513 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of high-mannose type HIV-1 gp120 glycopeptides
    • Singh S, Ni J, Wang LX. Chemoenzymatic synthesis of high-mannose type HIV-1 gp120 glycopeptides. Bioorg Med Chem Lett 2003; 13: 327-30.
    • (2003) Bioorg. Med. Chem. Lett. , vol.13 , pp. 327-330
    • Singh, S.1    Ni, J.2    Wang, L.X.3
  • 142
    • 0037169214 scopus 로고    scopus 로고
    • A phase I trial with two human monoclonal antibodies (hMAb 2F5, 2G12) against HIV-1
    • Armbruster C, Stiegler GM, Vcelar BA, Jager W, Michael NL, Vetter N, et al. A phase I trial with two human monoclonal antibodies (hMAb 2F5, 2G12) against HIV-1 Aids 2002; 16: 227-33.
    • (2002) Aids , vol.16 , pp. 227-233
    • Armbruster, C.1    Stiegler, G.M.2    Vcelar, B.A.3    Jager, W.4    Michael, N.L.5    Vetter, N.6
  • 143
    • 0036051788 scopus 로고    scopus 로고
    • Considerations and development of topical microbicides to inhibit the sexual transmission of HIV
    • Turpin JA. Considerations and development of topical microbicides to inhibit the sexual transmission of HIV. Expert Opin Investig Drugs 2002; 11: 1077-97.
    • (2002) Expert. Opin. Investig. Drugs , vol.11 , pp. 1077-1097
    • Turpin, J.A.1
  • 144
    • 0033615735 scopus 로고    scopus 로고
    • HIV-1 entry inhibitors in the side pocket
    • Sodroski JG. HIV-1 entry inhibitors in the side pocket. Cell 1999; 99: 243-6.
    • (1999) Cell , vol.99 , pp. 243-246
    • Sodroski, J.G.1
  • 145
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan DC, Fass D, Berger JM, Kim PS. Core structure of gp41 from the HIV envelope glycoprotein. Cell 1997; 89: 263-73.
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 147
    • 0031959601 scopus 로고    scopus 로고
    • Capture of an early fusion-active conformation of HIV-1 gp41
    • published erratum appears in Nat Struct Biol 1998 Jul;5(7):612
    • Furuta RA, Wild CT, Weng Y, Weiss CD. Capture of an early fusion-active conformation of HIV-1 gp41 [published erratum appears in Nat Struct Biol 1998 Jul;5(7):612]. Nat Struct Biol 1998; 5: 276-9.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 276-279
    • Furuta, R.A.1    Wild, C.T.2    Weng, Y.3    Weiss, C.D.4
  • 148
    • 0035900003 scopus 로고    scopus 로고
    • HIV-1 gp41 six-helix bundle formation occurs rapidly after the engagement of gp120 by CXCR4 in the HIV-1 Env-mediated fusion process
    • Gallo SA, Puri A, Blumenthal R. HIV-1 gp41 six-helix bundle formation occurs rapidly after the engagement of gp120 by CXCR4 in the HIV-1 Env-mediated fusion process. Biochemistry 2001; 40: 12231-6.
    • (2001) Biochemistry , vol.40 , pp. 12231-12236
    • Gallo, S.A.1    Puri, A.2    Blumenthal, R.3
  • 149
    • 0036278546 scopus 로고    scopus 로고
    • Dissection of human immunodeficiency virus type 1 entry with neutralizing antibodies to gp41 fusion intermediates
    • Golding H, Zaitseva M, de Rosny E, King LR, Manischewitz J, Sidorov I, et al. Dissection of human immunodeficiency virus type 1 entry with neutralizing antibodies to gp41 fusion intermediates. J Virol 2002; 76: 6780-90.
    • (2002) J. Virol , vol.76 , pp. 6780-6790
    • Golding, H.1    Zaitseva, M.2    de Rosny, E.3    King, L.R.4    Manischewitz, J.5    Sidorov, I.6
  • 150
    • 0034675886 scopus 로고    scopus 로고
    • Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion
    • Melikyan GB, Markosyan RM, Hemmati H, Delmedico MK, Lambert DM, Cohen FS. Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion. J. Cell. Biol. 2000; 151: 413-23.
    • (2000) J. Cell. Biol. , vol.151 , pp. 413-423
    • Melikyan, G.B.1    Markosyan, R.M.2    Hemmati, H.3    Delmedico, M.K.4    Lambert, D.M.5    Cohen, F.S.6
  • 151
    • 0038065763 scopus 로고    scopus 로고
    • Dilation of the human immunodeficiency virus-1 envelope glycoprotein fusion pore revealed by the inhibitory action of a synthetic peptide from gp41
    • Munoz-Barroso I, Durell S, Sakaguchi K, Appella E, Blumenthal R. Dilation of the human immunodeficiency virus-1 envelope glycoprotein fusion pore revealed by the inhibitory action of a synthetic peptide from gp41. J Cell Biol 1998; 140: 315-23.
    • (1998) J. Cell Biol. , vol.140 , pp. 315-323
    • Munoz-Barroso, I.1    Durell, S.2    Sakaguchi, K.3    Appella, E.4    Blumenthal, R.5
  • 152
    • 0028208268 scopus 로고
    • Neutralization of divergent human immunodeficiency virus type 1 variants and primary isolates by IAM-41-2F5, an anti-gp41 human monoclonal antibody
    • Conley AJ, Kessler JA, 2nd, Boots LJ, Tung JS, Arnold BA, Keller PM, et al. Neutralization of divergent human immunodeficiency virus type 1 variants and primary isolates by IAM-41-2F5, an anti-gp41 human monoclonal antibody. Proc Natl Acad Sci U S A 1994; 91: 3348-52.
    • (1994) Proc. Natl. Acad. Sci. U S A , vol.91 , pp. 3348-3352
    • Conley, A.J.1    Kessler J.A. II2    Boots, L.J.3    Tung, J.S.4    Arnold, B.A.5    Keller, P.M.6
  • 153
  • 154
    • 9344268284 scopus 로고    scopus 로고
    • Restricted antigenic variability of the epitope recognized by the neutralizing gp41 antibody 2F5
    • Purtscher M, Trkola A, Grassauer A, Schulz PM, Klima A. Dopper S, et al. Restricted antigenic variability of the epitope recognized by the neutralizing gp41 antibody 2F5. Aids 1996; 10: 587-93.
    • (1996) Aids , vol.10 , pp. 587-593
    • Purtscher, M.1    Trkola, A.2    Grassauer, A.3    Schulz, P.M.4    Klima, A.5    Dopper, S.6
  • 155
    • 0034759882 scopus 로고    scopus 로고
    • Broadly neutralizing antibodies targeted to the membrane-proximal external region of human immunodeficiency virus type 1 glycoprotein gp41
    • Zwick MB, Labrijn AF, Wang M, Spenlehauer C, Saphire EO, Binley JM, et al. Broadly neutralizing antibodies targeted to the membrane-proximal external region of human immunodeficiency virus type 1 glycoprotein gp41. J Virol 2001; 75: 10892-905.
    • (2001) J. Virol , vol.75 , pp. 10892-10905
    • Zwick, M.B.1    Labrijn, A.F.2    Wang, M.3    Spenlehauer, C.4    Saphire, E.O.5    Binley, J.M.6
  • 156
    • 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
    • Stiegler G, Kunert R, Purtscher M, Wolbank S, Voglauer R, Steindl F, et al. A potent cross-clade neutralizing human monoclonal antibody against a novel epitope on gp41 of human immunodeficiency virus type 1. AIDS Res Hum Retroviruses 2001; 17: 1757-65.
    • (2001) AIDS Res. Hum. Retroviruses , vol.17 , pp. 1757-1765
    • Stiegler, G.1    Kunert, R.2    Purtscher, M.3    Wolbank, S.4    Voglauer, R.5    Steindl, F.6
  • 157
    • 0034971817 scopus 로고    scopus 로고
    • Potent neutralization of primary human immunodeficiency virus clade C isolates with a synergistic combination of human monoclonal antibodies raised against clade B
    • Xu W, Smith-Franklin BA, Li PL, Wood C, He J, Du Q, et al. Potent neutralization of primary human immunodeficiency virus clade C isolates with a synergistic combination of human monoclonal antibodies raised against clade B. J Hum Virol 2001; 4: 55-61.
    • (2001) J. Hum. Virol , vol.4 , pp. 55-61
    • Xu, W.1    Smith-Franklin, B.A.2    Li, P.L.3    Wood, C.4    He, J.5    Du, Q.6
  • 158
    • 0032947286 scopus 로고    scopus 로고
    • Protection of Macaques against pathogenic simian/human immunodeficiency virus 89.6PD by passive transfer of neutralizing antibodies
    • Mascola JR, Lewis MG, Stiegler G, Harris D, VanCott TC, Hayes D, et al. Protection of Macaques against pathogenic simian/human immunodeficiency virus 89.6PD by passive transfer of neutralizing antibodies. J Virol 1999; 73: 4009-18.
    • (1999) J. Virol , vol.73 , pp. 4009-4018
    • Mascola, J.R.1    Lewis, M.G.2    Stiegler, G.3    Harris, D.4    VanCott, T.C.5    Hayes, D.6
  • 159
    • 0034904087 scopus 로고    scopus 로고
    • Postnatal passive immunization of neonatal macaques with a triple combination of human monoclonal antibodies against oral simian-human immunodeficiency virus challenge
    • Hoffmann-Lehmann R, Vlasak J, Rasmussen RA, Smith BA, Baba TW, Liska V, et al. Postnatal passive immunization of neonatal macaques with a triple combination of human monoclonal antibodies against oral simian-human immunodeficiency virus challenge. J Virol 2001; 75: 7470-80
    • (2001) J. Virol , vol.75 , pp. 7470-7480
    • Hoffmann-Lehmann, R.1    Vlasak, J.2    Rasmussen, R.A.3    Smith, B.A.4    Baba, T.W.5    Liska, V.6
  • 160
    • 0027378573 scopus 로고
    • A conserved neutralizing epitope on gp41 of human immunodeficiency virus type 1
    • Muster T, Steindl F, Purtscher M, Trkola A, Klima A, Himmler G, et al. A conserved neutralizing epitope on gp41 of human immunodeficiency virus type 1. J. Virol. 1993; 67: 6642-7.
    • (1993) J. Virol. , vol.67 , pp. 6642-6647
    • Muster, T.1    Steindl, F.2    Purtscher, M.3    Trkola, A.4    Klima, A.5    Himmler, G.6
  • 161
    • 0034755554 scopus 로고    scopus 로고
    • Fine definition of the epitope on the gp41-glycoprotein of human immunodeficiency virus type 1 for the neutralizing monoclonal antibody 2F5
    • Parker CE, Deterding LJ, Hager-Braun C, Binley JM, Schulke N, Katinger H, et al. Fine definition of the epitope on the gp41-glycoprotein of human immunodeficiency virus type 1 for the neutralizing monoclonal antibody 2F5. J Virol 2001; 75: 10906-11.
    • (2001) J. Virol , vol.75 , pp. 10906-10911
    • Parker, C.E.1    Deterding, L.J.2    Hager-Braun, C.3    Binley, J.M.4    Schulke, N.5    Katinger, H.6
  • 162
    • 0027959493 scopus 로고
    • Peptides corresponding to a predictive alphahefical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection
    • Wild CT, Shugars DC, Greenwell TK, McDanal CB, Matthews TJ. Peptides corresponding to a predictive alphahefical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection. Proc. Natl. Acad. Sci. U. S. A. 1994; 91: 9770-4.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 9770-9774
    • Wild, C.T.1    Shugars, D.C.2    Greenwell, T.K.3    McDanal, C.B.4    Matthews, T.J.5
  • 163
    • 0031729823 scopus 로고    scopus 로고
    • Potent suppression of HIV-1 replication in humans by T-20, a peptide inhibitor of gp41-mediated virus entry
    • Kilby JM, Hopkins S, Venetta TM, DiMassimo B, Cloud GA, Lee JY, et al. Potent suppression of HIV-1 replication in humans by T-20, a peptide inhibitor of gp41-mediated virus entry. Nat. Med. 1998; 4: 1302-7.
    • (1998) Nat. Med. , vol.4 , pp. 1302-1307
    • Kilby, J.M.1    Hopkins, S.2    Venetta, T.M.3    DiMassimo, B.4    Cloud, G.A.5    Lee, J.Y.6
  • 164
    • 0032750956 scopus 로고    scopus 로고
    • Prolonged therapy with the fusion inhibitor T-20 in combination with oral antiretroviral agents in an HIV-infected individual
    • [letter]
    • Pilcher CD, Eron JJ, Jr., Ngo L, Dusek A, Sista P, Gleavy J, et al. Prolonged therapy with the fusion inhibitor T-20 in combination with oral antiretroviral agents in an HIV-infected individual [letter]. Aids 1999; 13: 2171-3.
    • (1999) Aids , vol.13 , pp. 2171-2173
    • Pilcher, C.D.1    Eron J.J., Jr.2    Ngo, L.3    Dusek, A.4    Sista, P.5    Gleavy, J.6
  • 165
    • 0034645796 scopus 로고    scopus 로고
    • Inhibition of HIV-1 entry before gp41 folds into its fusion-active conformation
    • Kliger Y, Shai Y. Inhibition of HIV-1 entry before gp41 folds into its fusion-active conformation. J. Mol. Biol. 2000: 295: 163-8.
    • (2000) J. Mol. Biol. , vol.295 , pp. 163-168
    • Kliger, Y.1    Shai, Y.2
  • 166
    • 0036223198 scopus 로고    scopus 로고
    • Peptide and non-peptide HIV fusion inhibitors
    • Jiang S, Zhao Q, Debnath AK. Peptide and non-peptide HIV fusion inhibitors. Curr Pharm Des 2002; 8: 563-80.
    • (2002) Curr. Pharm. Des. , vol.8 , pp. 563-580
    • Jiang, S.1    Zhao, Q.2    Debnath, A.K.3
  • 167
    • 0034057007 scopus 로고    scopus 로고
    • Induction of high level of specific antibody response to the neutralizing epitope ELDKWA on HIV-1 gp41 by peptide-vaccine
    • Liao M, Lu Y, Xiao Y, Dierich MP, Chen Y. Induction of high level of specific antibody response to the neutralizing epitope ELDKWA on HIV-1 gp41 by peptide-vaccine. Peptides 2000; 21: 463-8.
    • (2000) Peptides , vol.21 , pp. 463-468
    • Liao, M.1    Lu, Y.2    Xiao, Y.3    Dierich, M.P.4    Chen, Y.5
  • 168
    • 0033962568 scopus 로고    scopus 로고
    • Epitope-vaccines: A new strategy to induce high levels of neutralizing antibodies against HIV-1
    • Xiao Y, Liao M, Lu Y, Dierich MP, Chen YH. Epitope-vaccines: a new strategy to induce high levels of neutralizing antibodies against HIV-1. Immunobiology 2000; 201: 323-31.
    • (2000) Immunobiology , vol.201 , pp. 323-331
    • Xiao, Y.1    Liao, M.2    Lu, Y.3    Dierich, M.P.4    Chen, Y.H.5
  • 169
    • 0034892978 scopus 로고    scopus 로고
    • Peptides corresponding to the heptad repeat motifs in the transmembrane protein (gp41) of human immunodeficiency virus type 1 elicit antibodies to receptor-activated conformations of the envelope glycoprotein
    • de Rosny E, Vassell R, Wingfield PT, Wild CT, Weiss CD. Peptides corresponding to the heptad repeat motifs in the transmembrane protein (gp41) of human immunodeficiency virus type 1 elicit antibodies to receptor-activated conformations of the envelope glycoprotein. J Virol 2001; 75: 8859-63.
    • (2001) J. Virol , vol.75 , pp. 8859-8863
    • de Rosny, E.1    Vassell, R.2    Wingfield, P.T.3    Wild, C.T.4    Weiss, C.D.5
  • 170
    • 0034703835 scopus 로고    scopus 로고
    • Antigenicity and immunogenicity of the HIV-1 gp41 epitope ELDKWA inserted into permissive sites of the MalE protein
    • Coeffier E, Clement JM, Cussac V, Khodaei-Boorane N, Jehanno M, Rojas M, et al. Antigenicity and immunogenicity of the HIV-1 gp41 epitope ELDKWA inserted into permissive sites of the MalE protein. Vaccine 2001; 19: 684-93.
    • (2001) Vaccine , vol.19 , pp. 684-693
    • Coeffier, E.1    Clement, J.M.2    Cussac, V.3    Khodaei-Boorane, N.4    Jehanno, M.5    Rojas, M.6
  • 171
    • 0029812316 scopus 로고    scopus 로고
    • Immunogenic presentation of a conserved gp41 epitope of human immunodeficiency virus type 1 on recombinant surface antigen of hepatitis B virus
    • Eckhart L, Raffelsberger W, Ferko B, Klima A, Purtscher M, Katinger H, et al. Immunogenic presentation of a conserved gp41 epitope of human immunodeficiency virus type 1 on recombinant surface antigen of hepatitis B virus. J. Gen. Virol. 1996; 77: 2001-8.
    • (1996) J. Gen. Virol. , vol.77 , pp. 2001-2008
    • Eckhart, L.1    Raffelsberger, W.2    Ferko, B.3    Klima, A.4    Purtscher, M.5    Katinger, H.6
  • 172
    • 0033575483 scopus 로고    scopus 로고
    • Epitope insertion into variable loops of HIV-1 gp120 as a potential means to improve immunogenicity of viral envelope protein
    • Liang X, Munshi S, Shendure J, Mark G, 3rd, Davies ME, Freed DC, et al. Epitope insertion into variable loops of HIV-1 gp120 as a potential means to improve immunogenicity of viral envelope protein. Vaccine 1999: 17: 2862-72.
    • (1999) Vaccine , vol.17 , pp. 2862-2872
    • Liang, X.1    Munshi, S.2    Shendure, J.3    Mark G. III4    Davies, M.E.5    Freed, D.C.6
  • 173
    • 0037081391 scopus 로고    scopus 로고
    • Construction of recombinant targeting immunogens incorporating an HIV-1 neutralizing epitope into sites of differing conformational constraint
    • Ho J, MacDonald KS, Barber BH. Construction of recombinant targeting immunogens incorporating an HIV-1 neutralizing epitope into sites of differing conformational constraint. Vaccine 2002; 20: 1169-80.
    • (2002) Vaccine , vol.20 , pp. 1169-1180
    • Ho, J.1    MacDonald, K.S.2    Barber, B.H.3
  • 174
    • 0008273311 scopus 로고    scopus 로고
    • Fab'-epitope complex from the HIV-1-cross-neutralizing monoclonal antibody 2F5
    • Switzerland: World Intellectural Property Organization, WO-00/61618
    • Pai EF, Klein MH, Chong P, Pedyczak A. Fab'-epitope complex from the HIV-1-cross-neutralizing monoclonal antibody 2F5. World Intellectural Property Organization. Switzerland: World Intellectural Property Organization, WO-00/61618, 2000
    • (2000) World Intellectural Property Organization
    • Pai, E.F.1    Klein, M.H.2    Chong, P.3    Pedyczak, A.4
  • 175
    • 0036001491 scopus 로고    scopus 로고
    • Structure-affinity relationships in the gp41 ELDKWA epitope for the HIV-1 neutralizing monoclonal antibody 2F5: Effects of side-chain and backbone modifications and conformational constraints
    • Tian Y, Ramesh CV, Ma X, Naqvi S, Patel T, Cenizal T, et al. Structure-affinity relationships in the gp41 ELDKWA epitope for the HIV-1 neutralizing monoclonal antibody 2F5: effects of side-chain and backbone modifications and conformational constraints. J Pept Res 2002; 59: 264-76.
    • (2002) J. Pept. Res. , vol.59 , pp. 264-276
    • Tian, Y.1    Ramesh, C.V.2    Ma, X.3    Naqvi, S.4    Patel, T.5    Cenizal, T.6
  • 176
    • 0037195784 scopus 로고    scopus 로고
    • Enhancement of alpha -Helicity in the HIV-1 Inhibitory Peptide DP178 Leads to an Increased Affinity for Human Monoclonal Antibody 2F5 but Does Not Elicit Neutralizing Responses in Vitro. IMPLICATIONS FOR VACCINE DESIGN
    • Joyce JG, Hurni WM, Bogusky MJ, Garsky VM, Liang X, Citron MP, et al. Enhancement of alpha -Helicity in the HIV-1 Inhibitory Peptide DP178 Leads to an Increased Affinity for Human Monoclonal Antibody 2F5 but Does Not Elicit Neutralizing Responses in Vitro. IMPLICATIONS FOR VACCINE DESIGN. J Biol Chem 2002; 277: 45811-20.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45811-45820
    • Joyce, J.G.1    Hurni, W.M.2    Bogusky, M.J.3    Garsky, V.M.4    Liang, X.5    Citron, M.P.6
  • 178
    • 0027203897 scopus 로고
    • Inhibition of HIV-1 infection by a fusion domain binding peptide from the HIV-1 envelope glycoprotein GP41
    • Jiang S, Lin K, Strick N, Neurath AR. Inhibition of HIV-1 infection by a fusion domain binding peptide from the HIV-1 envelope glycoprotein GP41. Biochem Biophys Res Commun 1993; 195: 533-8.
    • (1993) Biochem. Biophys. Res. Commun. , vol.195 , pp. 533-538
    • Jiang, S.1    Lin, K.2    Strick, N.3    Neurath, A.R.4
  • 179
    • 0031743949 scopus 로고    scopus 로고
    • A conformation-specific monoclonal antibody reacting with fusion-active gp41 from the human immunodeficiency virus type 1 envelope glycoprotein
    • Jiang S, Lin K, Lu M. A conformation-specific monoclonal antibody reacting with fusion-active gp41 from the human immunodeficiency virus type 1 envelope glycoprotein. J Virol 1998; 72: 10213-7.
    • (1998) J. Virol , vol.72 , pp. 10213-10217
    • Jiang, S.1    Lin, K.2    Lu, M.3
  • 180
    • 0035793406 scopus 로고    scopus 로고
    • Protein Design of an HIV-1 Entry Inhibitor
    • Root MJ, Kay MS, Kim PS. Protein Design of an HIV-1 Entry Inhibitor. Science 200; 291: 884-8.
    • (2000) Science , vol.291 , pp. 884-888
    • Root, M.J.1    Kay, M.S.2    Kim, P.S.3
  • 181
    • 0037470227 scopus 로고    scopus 로고
    • The prefusogenic intermediate of HIV-1 gp41 contains exposed C-peptide regions
    • Koshiba T, Chan DC. The prefusogenic intermediate of HIV-1 gp41 contains exposed C-peptide regions. J Biol Chem 2003; 278: 7573-9.
    • (2003) J. Biol. Chem. , vol.278 , pp. 7573-7579
    • Koshiba, T.1    Chan, D.C.2
  • 182
    • 0037413342 scopus 로고    scopus 로고
    • Carbohydrate-centered maleimide cluster as a new type of templates for multivalent peptide assembling: Synthesis of multivalent HIV-1 gp41 peptides
    • Wang LX, Ni J, Singh S. Carbohydrate-centered maleimide cluster as a new type of templates for multivalent peptide assembling: Synthesis of multivalent HIV-1 gp41 peptides. Bioorg. Med. Chem. 2003; 11: 129-36.
    • (2003) Bioorg. Med. Chem. , vol.11 , pp. 129-136
    • Wang, L.X.1    Ni, J.2    Singh, S.3
  • 183
    • 0034947038 scopus 로고    scopus 로고
    • Cytokine and chemokine based control of HIV infection and replication
    • Alfano M, Poli G. Cytokine and chemokine based control of HIV infection and replication. Curr Pharm Des 2001; 7(11): 993-1013.
    • (2001) Curr. Pharm. Des. , vol.7 , Issue.11 , pp. 993-1013
    • Alfano, M.1    Poli, G.2
  • 184
    • 0036223198 scopus 로고    scopus 로고
    • Peptide and non-peptide HIV fusion inhibitors
    • Jiang S, Zhao Q, Debnath AK. Peptide and non-peptide HIV fusion inhibitors. Curr Pharm Des 2002; 8(8): 563-80.
    • (2002) Curr. Pharm. Des. , vol.8 , Issue.8 , pp. 563-580
    • Jiang, S.1    Zhao, Q.2    Debnath, A.K.3
  • 185
    • 0034938813 scopus 로고    scopus 로고
    • The hunt for new tuberculosis vaccines: Anti-TB immunity and rational design of vaccines
    • Xing Z. The hunt for new tuberculosis vaccines: anti-TB immunity and rational design of vaccines. Curr Pharm Des 2001; 7(11): 1015-37.
    • (2001) Curr. Pharm. Des. , vol.7 , Issue.11 , pp. 1015-1037
    • Xing, Z.1


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