메뉴 건너뛰기




Volumn 65, Issue 7, 2005, Pages 879-904

The appealing story of HIV entry inhibitors: From discovery of biological mechanisms to drug development

Author keywords

[No Author keywords available]

Indexed keywords

1 ACETYL N [3 [4 (4 CARBAMOYLBENZYL) 1 PIPERIDINYL]PROPYL] N (3 CHLORO 4 METHYLPHENYL) 4 PIPERIDINECARBOXAMIDE; 1 BENZOYL 4 [(4,7 DIMETHOXY 1H PYRROLO[2,3 C]PYRIDIN 3 YL)OXOACETYL]PIPERAZINE; AMD 070; AMD 887; ANTI HUMAN IMMUNODEFICIENCY VIRUS AGENT; ANTIRETROVIRUS AGENT; APLAVIROC; CD4 IMMUNOGLOBULIN G2; CHEMOKINE RECEPTOR CCR5; CHEMOKINE RECEPTOR CXCR4; DEXTRIN; DEXTRIN 2 SULFATE; ENFUVIRTIDE; GLYCOPROTEIN GP 120 INHIBITOR; HUMAN IMMUNODEFICIENCY VIRUS ENTRY INHIBITOR; INDINAVIR; KRH 2731; MARAVIROC; NEVIRAPINE; PRO 140; RITONAVIR; RNA DIRECTED DNA POLYMERASE INHIBITOR; SAQUINAVIR; T 1249; TENOFOVIR; TIFUVIRTIDE; TNX 355; UNCLASSIFIED DRUG; VICRIVIROC; ZIDOVUDINE;

EID: 18644369147     PISSN: 00126667     EISSN: None     Source Type: Journal    
DOI: 10.2165/00003495-200565070-00001     Document Type: Review
Times cited : (65)

References (200)
  • 1
    • 0344760902 scopus 로고    scopus 로고
    • March 23. Developed by the Panel on Clinical Practices of HIV infection convened by the Department of Health and Human Services (DHHS), USA [online]. Available from URL
    • Guidelines for the use of antiretroviral agents in HIV-1-infected adults and adolescents. March 23, 2004. Developed by the Panel on Clinical Practices of HIV infection convened by the Department of Health and Human Services (DHHS), USA [online]. Available from URL: http://www.hopkins-aids.edu/guidelines/ guidelines.html [Accessed 2005 Mar 17]
    • (2004) Guidelines for the Use of Antiretroviral Agents in HIV-1-Infected Adults and Adolescents
  • 2
    • 0141814730 scopus 로고    scopus 로고
    • The entry of entry inhibitors: A fusion of science and medicine
    • Moore JP, Doms RW. The entry of entry inhibitors: a fusion of science and medicine. Proc Natl Acad Sci U S A 2003; 100: 10598-602
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 10598-10602
    • Moore, J.P.1    Doms, R.W.2
  • 3
    • 4444346813 scopus 로고    scopus 로고
    • New antiretroviral agents for the treatment of HIV infection
    • Marks K, Gulick RM. New antiretroviral agents for the treatment of HIV infection. Curr Infect Dis Rep 2004; 6: 333-9
    • (2004) Curr Infect Dis Rep , vol.6 , pp. 333-339
    • Marks, K.1    Gulick, R.M.2
  • 4
    • 4644242776 scopus 로고    scopus 로고
    • The brightening future of HIV therapeutics
    • Greene WC. The brightening future of HIV therapeutics. Nat Immunol 2004; 5: 867-71
    • (2004) Nat Immunol , vol.5 , pp. 867-871
    • Greene, W.C.1
  • 5
    • 0021833513 scopus 로고
    • Characterization of envelope and core structural gene products of HTLV-III with sera from AIDS patients
    • Robey WG, Safai B, Oroszlan S, et al. Characterization of envelope and core structural gene products of HTLV-III with sera from AIDS patients. Science 1985; 228: 593-5
    • (1985) Science , vol.228 , pp. 593-595
    • Robey, W.G.1    Safai, B.2    Oroszlan, S.3
  • 6
    • 0021997051 scopus 로고
    • Major glycoproteins antigens that induce antibodies in AIDS patients are encoded by HTLV-III
    • Allan JS, Coligan JE, Barin F, et al. Major glycoproteins antigens that induce antibodies in AIDS patients are encoded by HTLV-III. Science 1985; 228: 1091-4
    • (1985) Science , vol.228 , pp. 1091-1094
    • Allan, J.S.1    Coligan, J.E.2    Barin, F.3
  • 7
    • 0022539126 scopus 로고
    • Expression of the HTLV-III envelope gene by recombinant vaccinia virus
    • Chakrabarti S, Robert-Guroff M, Wong-Staal F, et al. Expression of the HTLV-III envelope gene by recombinant vaccinia virus. Nature 1986; 320: 535-8
    • (1986) Nature , vol.320 , pp. 535-538
    • Chakrabarti, S.1    Robert-Guroff, M.2    Wong-Staal, F.3
  • 8
    • 0022352075 scopus 로고
    • Characterization of gp41 as the transmembrane protein coded by the HTLV-III/LAV envelope gene
    • Veronese FD, DeVico AL, Copeland TD, et al. Characterization of gp41 as the transmembrane protein coded by the HTLV-III/LAV envelope gene. Science 1985; 229: 1402-5
    • (1985) Science , vol.229 , pp. 1402-1405
    • Veronese, F.D.1    DeVico, A.L.2    Copeland, T.D.3
  • 9
    • 0023669119 scopus 로고
    • Detection of a fusion peptide sequence in the transmembrane protein of human immunodeficiency virus
    • Gallaher WR. Detection of a fusion peptide sequence in the transmembrane protein of human immunodeficiency virus. Cell 1987; 50: 327-8
    • (1987) Cell , vol.50 , pp. 327-328
    • Gallaher, W.R.1
  • 10
    • 0024399763 scopus 로고
    • Identification of the fusion peptide of primate immunodeficiency viruses
    • Bosch ML, Earl PL, Fargnoli K, et al. Identification of the fusion peptide of primate immunodeficiency viruses. Science 1989; 244: 694-7
    • (1989) Science , vol.244 , pp. 694-697
    • Bosch, M.L.1    Earl, P.L.2    Fargnoli, K.3
  • 11
    • 0022587282 scopus 로고
    • Binding of the HTLVIII/LAV to T4+ T cells by a complex of the 100 K viral protein and the T4 molecule
    • McDougal JS, Kennedy M, Sligh J, et al. Binding of the HTLVIII/LAV to T4+ T cells by a complex of the 100 K viral protein and the T4 molecule. Science 1986; 231: 382-5
    • (1986) Science , vol.231 , pp. 382-385
    • McDougal, J.S.1    Kennedy, M.2    Sligh, J.3
  • 12
    • 0023217711 scopus 로고
    • Functional regions of the human immunodeficiency virus envelope glycoprotein
    • Kowalski M, Potz J, Basiripour L, et al. Functional regions of the human immunodeficiency virus envelope glycoprotein. Science 1987; 237: 1351-5
    • (1987) Science , vol.237 , pp. 1351-1355
    • Kowalski, M.1    Potz, J.2    Basiripour, L.3
  • 13
    • 0023028190 scopus 로고
    • The T4 gene encodes the AIDS virus receptor and is expressed in the immune system and the brain
    • Maddon PJ, Dalgleish AC, McDougal JS, et al. The T4 gene encodes the AIDS virus receptor and is expressed in the immune system and the brain. Cell 1986; 47: 333-48
    • (1986) Cell , vol.47 , pp. 333-348
    • Maddon, P.J.1    Dalgleish, A.C.2    McDougal, J.S.3
  • 14
    • 0023002043 scopus 로고
    • Epitopes of the CD4 antigen and HIV infection
    • Sattentau QJ, Dalgleish AG, Weiss RA, et al. Epitopes of the CD4 antigen and HIV infection. Science 1986; 234: 1120-3
    • (1986) Science , vol.234 , pp. 1120-1123
    • Sattentau, Q.J.1    Dalgleish, A.G.2    Weiss, R.A.3
  • 15
    • 0023840802 scopus 로고
    • The CD4 antigen: Physiological ligand and HIV receptor
    • Sattentau QJ, Weiss R. The CD4 antigen: physiological ligand and HIV receptor. Cell 1988; 52: 631-3
    • (1988) Cell , vol.52 , pp. 631-633
    • Sattentau, Q.J.1    Weiss, R.2
  • 16
    • 0024520882 scopus 로고
    • Identification of the residues in human CD4 critical for the binding of HIV
    • Arthos J, Deen KC, Chaikin MA, et al. Identification of the residues in human CD4 critical for the binding of HIV. Cell 1989; 57: 469-81
    • (1989) Cell , vol.57 , pp. 469-481
    • Arthos, J.1    Deen, K.C.2    Chaikin, M.A.3
  • 17
    • 0023651341 scopus 로고
    • Delineation of a region of the human immunodeficiency virus type 1 gp120 glycoprotein critical for interaction with the CD4 receptor
    • Lasky LA, Nakamura G, Smith DH, et al. Delineation of a region of the human immunodeficiency virus type 1 gp120 glycoprotein critical for interaction with the CD4 receptor. Cell 1987; 50: 975-85
    • (1987) Cell , vol.50 , pp. 975-985
    • Lasky, L.A.1    Nakamura, G.2    Smith, D.H.3
  • 18
    • 0023948568 scopus 로고
    • Internalization of the human immunodeficiency virus does not require the cytoplasmic domain of CD4
    • Bedinger P, Moriarty A, von Borstel RC, et al. Internalization of the human immunodeficiency virus does not require the cytoplasmic domain of CD4. Nature 1988; 334: 162-5
    • (1988) Nature , vol.334 , pp. 162-165
    • Bedinger, P.1    Moriarty, A.2    Von Borstel, R.C.3
  • 19
    • 0024386958 scopus 로고
    • The MHC-binding and the gp120-binding functions of CD4 are separable
    • Lamarre D, Ashkenazi A, Fleury S, et al. The MHC-binding and the gp120-binding functions of CD4 are separable. Science 1989; 245: 743-6
    • (1989) Science , vol.245 , pp. 743-746
    • Lamarre, D.1    Ashkenazi, A.2    Fleury, S.3
  • 20
    • 0025832880 scopus 로고
    • The CD4-gp120 interaction and AIDS pathogenesis
    • Capon DJ, Ward RH. The CD4-gp120 interaction and AIDS pathogenesis. Annu Rev Immunol 1991; 9: 649-78
    • (1991) Annu Rev Immunol , vol.9 , pp. 649-678
    • Capon, D.J.1    Ward, R.H.2
  • 21
    • 0023580063 scopus 로고
    • Blocking of HIV-1 infectivity by a soluble, secreted form of the CD4 antigen
    • Smith DH, Byrn RA, Marsters SA, et al. Blocking of HIV-1 infectivity by a soluble, secreted form of the CD4 antigen. Science 1987; 238: 1704-7
    • (1987) Science , vol.238 , pp. 1704-1707
    • Smith, D.H.1    Byrn, R.A.2    Marsters, S.A.3
  • 22
    • 0023845937 scopus 로고
    • A soluble form of CD4 (T4) protein inhibit: AIDS virus infection
    • Deen KC, McDougal SJ, Inacker R, et al. A soluble form of CD4 (T4) protein inhibit: AIDS virus infection. Nature 1988; 331: 82-4
    • (1988) Nature , vol.331 , pp. 82-84
    • Deen, K.C.1    McDougal, S.J.2    Inacker, R.3
  • 23
    • 0024226884 scopus 로고
    • HIV-infected cells are killed by rCD4-ricin A chain
    • Till MA, Ghetie V, Gregory T, et al. HIV-infected cells are killed by rCD4-ricin A chain. Science 1988; 242: 1166-8
    • (1988) Science , vol.242 , pp. 1166-1168
    • Till, M.A.1    Ghetie, V.2    Gregory, T.3
  • 24
    • 0026072329 scopus 로고
    • Effects of soluble CD4 and CD4-Pseudomonas exotoxin A chimeric protein on human peripheral blood lymphocytes: Lymphocyte activation and anti-HIV activity in vitro
    • Rubino KL, Tarpley WG, Nicholas JA. Effects of soluble CD4 and CD4-Pseudomonas exotoxin A chimeric protein on human peripheral blood lymphocytes: lymphocyte activation and anti-HIV activity in vitro. Antiviral Res 1991; 16: 267-79
    • (1991) Antiviral Res , vol.16 , pp. 267-279
    • Rubino, K.L.1    Tarpley, W.G.2    Nicholas, J.A.3
  • 25
    • 0024549563 scopus 로고
    • Highly efficient neutralization of HIV with recombinant CD4-immunglobulin molecules
    • Traunecker A, Schneider J, Kiefer H, et al. Highly efficient neutralization of HIV with recombinant CD4-immunglobulin molecules. Nature 1989; 339: 68-70
    • (1989) Nature , vol.339 , pp. 68-70
    • Traunecker, A.1    Schneider, J.2    Kiefer, H.3
  • 26
    • 0026451459 scopus 로고
    • Characterization and anti-HIV properties of CD4-coated red blood cells
    • Idziorek T, Chams V, Klatzmann D. Characterization and anti-HIV properties of CD4-coated red blood cells. Arch Virol 1992; 126: 81-91
    • (1992) Arch Virol , vol.126 , pp. 81-91
    • Idziorek, T.1    Chams, V.2    Klatzmann, D.3
  • 27
    • 0025299912 scopus 로고
    • Prevention of HIV-1 glycoprotein transport by soluble CD4 retained in the endoplasmic reticulum
    • Buonocore L, Rose JK. Prevention of HIV-1 glycoprotein transport by soluble CD4 retained in the endoplasmic reticulum. Nature 1990; 345: 625-8
    • (1990) Nature , vol.345 , pp. 625-628
    • Buonocore, L.1    Rose, J.K.2
  • 28
    • 0026011315 scopus 로고
    • Binding of soluble CD4 proteins to human immunodeficiency virus type 1 and infected cells induces release of envelope glycoprotein gp120
    • Hart TK, Kirsh R, Ellens H, et al. Binding of soluble CD4 proteins to human immunodeficiency virus type 1 and infected cells induces release of envelope glycoprotein gp120. Proc Natl Acad Sci U S A 1991; 88: 2189-93
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 2189-2193
    • Hart, T.K.1    Kirsh, R.2    Ellens, H.3
  • 29
    • 0025913151 scopus 로고
    • Stimulation of glycoprotein gp120 dissociation from the envelope glycoprotein complex of human immunodeficiency virus type 1 by soluble CD4 and CD4 peptide derivatives: Implications for the role of the complementarity- determining region 3-like region in membrane fusion
    • Berger EA, Lifson JD, Eiden LE. Stimulation of glycoprotein gp120 dissociation from the envelope glycoprotein complex of human immunodeficiency virus type 1 by soluble CD4 and CD4 peptide derivatives: implications for the role of the complementarity-determining region 3-like region in membrane fusion. Proc Natl Acad Sci U S A 1991; 88: 8082-6
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 8082-8086
    • Berger, E.A.1    Lifson, J.D.2    Eiden, L.E.3
  • 30
    • 0026792879 scopus 로고
    • Lack of correlation between soluble CD4-induced shedding of the human immunodeficiency virus type 1 exterior envelope glycoprotein and subsequent membrane fusion events
    • Thali M, Furman C, Helseth E, et al. Lack of correlation between soluble CD4-induced shedding of the human immunodeficiency virus type 1 exterior envelope glycoprotein and subsequent membrane fusion events. J Virol 1992; 66: 5516-24
    • (1992) J Virol , vol.66 , pp. 5516-5524
    • Thali, M.1    Furman, C.2    Helseth, E.3
  • 31
    • 0025284777 scopus 로고
    • Three-drug synergistic inhibition of HIV-1 replication in vitro by zidovudine, recombinant soluble CD4, and recombinant interferon-alpha A
    • Johnson VA, Barlow MA, Merrill DP, et al. Three-drug synergistic inhibition of HIV-1 replication in vitro by zidovudine, recombinant soluble CD4, and recombinant interferon-alpha A. J Infect Dis 1990; 161: 1059-67
    • (1990) J Infect Dis , vol.161 , pp. 1059-1067
    • Johnson, V.A.1    Barlow, M.A.2    Merrill, D.P.3
  • 32
    • 0025155184 scopus 로고
    • New antiretroviral agents in the clinic
    • Myers MW. New antiretroviral agents in the clinic. Rev Infect Dis 1990; 12: 944-50
    • (1990) Rev Infect Dis , vol.12 , pp. 944-950
    • Myers, M.W.1
  • 33
    • 0025245831 scopus 로고
    • Soluble CD4 enhances simian immunodeficiency virus SIVagm infection
    • Werner A, Winskowsky G, Kurth R. Soluble CD4 enhances simian immunodeficiency virus SIVagm infection. J Virol 1990; 64: 6252-6
    • (1990) J Virol , vol.64 , pp. 6252-6256
    • Werner, A.1    Winskowsky, G.2    Kurth, R.3
  • 34
    • 0025304589 scopus 로고
    • Human immunodeficiency virus envelope glycoprotein CD4-mediated fusion of nonprimate cells with human cells
    • Ashorn PA, Berger EA, Moss B. Human immunodeficiency virus envelope glycoprotein CD4-mediated fusion of nonprimate cells with human cells. J Virol 1990; 64: 2149-56
    • (1990) J Virol , vol.64 , pp. 2149-2156
    • Ashorn, P.A.1    Berger, E.A.2    Moss, B.3
  • 35
    • 0027080399 scopus 로고
    • Expression of human CD4 in transgenic mice does not confer sensitivity to human immunodeficiency virus infection
    • Lores P, Boucher V, Mackay C, et al. Expression of human CD4 in transgenic mice does not confer sensitivity to human immunodeficiency virus infection. AIDS Res Hum Retroviruses 1992; 8: 2063-71
    • (1992) AIDS Res Hum Retroviruses , vol.8 , pp. 2063-2071
    • Lores, P.1    Boucher, V.2    Mackay, C.3
  • 36
    • 0028282775 scopus 로고
    • HIV-2 and SIV infection of nonprimate cell lines expressing human CD4: Restrictions to replication at distinct stages
    • McKnight A, Clapham PR, Weiss RA. HIV-2 and SIV infection of nonprimate cell lines expressing human CD4: restrictions to replication at distinct stages. Virology 1994; 201: 8-18
    • (1994) Virology , vol.201 , pp. 8-18
    • McKnight, A.1    Clapham, P.R.2    Weiss, R.A.3
  • 37
    • 0026044404 scopus 로고
    • Inhibition of human immunodeficiency virus replication in acutely infected CD4+ cells by CD8+ cells involves a noncytotoxic mechanism
    • Walker CM, Erickson AL, Hsueh FC, et al. Inhibition of human immunodeficiency virus replication in acutely infected CD4+ cells by CD8+ cells involves a noncytotoxic mechanism. J Virol 1991; 65: 5921-7
    • (1991) J Virol , vol.65 , pp. 5921-5927
    • Walker, C.M.1    Erickson, A.L.2    Hsueh, F.C.3
  • 38
    • 0029417004 scopus 로고
    • Identification of RANTES, MIP-1α, and MIP-1β as the major HIV-suppressive factors produced by CD8+ T cells
    • Cocchi F, DeVico AL, Garzino-Demo A, et al. Identification of RANTES, MIP-1α, and MIP-1β as the major HIV-suppressive factors produced by CD8+ T cells. Science 1995; 270: 1811-5
    • (1995) Science , vol.270 , pp. 1811-1815
    • Cocchi, F.1    DeVico, A.L.2    Garzino-Demo, A.3
  • 39
    • 0029856309 scopus 로고    scopus 로고
    • Chemokine receptors: Gateways to inflammation and infection
    • Premack BA, Schall TJ. Chemokine receptors: Gateways to inflammation and infection. Nat Med 1996; 2: 1174-8
    • (1996) Nat Med , vol.2 , pp. 1174-1178
    • Premack, B.A.1    Schall, T.J.2
  • 40
    • 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
  • 41
    • 0030018156 scopus 로고    scopus 로고
    • CC CKR5: A RANTES, MIP-1α, MIP-1β receptor as a fusion cofactor for macrophage-tropic HIV-1
    • Alkhatib G, Combadiere C, Broder CC, et al. CC CKR5: a RANTES, MIP-1α, MIP-1β receptor as a fusion cofactor for macrophage-tropic HIV-1. Science 1996; 272: 1955-8
    • (1996) Science , vol.272 , pp. 1955-1958
    • Alkhatib, G.1    Combadiere, C.2    Broder, C.C.3
  • 42
    • 0005014748 scopus 로고    scopus 로고
    • The beta-chemokine receptors CCR3 and CCR5 facilitate infection by primary HIV-1 isolates
    • Choe H, Farzan M, Sun Y, et al. The beta-chemokine receptors CCR3 and CCR5 facilitate infection by primary HIV-1 isolates. Cell 1996; 85: 1135-48
    • (1996) Cell , vol.85 , pp. 1135-1148
    • Choe, H.1    Farzan, M.2    Sun, Y.3
  • 43
    • 15844419153 scopus 로고    scopus 로고
    • Identification of a major coreceptor for primary isolates of HIV-1
    • Deng H, Liu R, Ellmeier W, et al. Identification of a major coreceptor 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
  • 44
    • 15844389650 scopus 로고    scopus 로고
    • HIV-1 entry into CD4+ cells is mediated by the chemokine receptor CC-CKR-5
    • Dragic T, Litwin V, Allaway GP, et al. HIV-1 entry into CD4+ cells is mediated by the chemokine receptor CC-CKR-5. Nature 1996; 381: 667-73
    • (1996) Nature , vol.381 , pp. 667-673
    • Dragic, T.1    Litwin, V.2    Allaway, G.P.3
  • 45
    • 0030604727 scopus 로고    scopus 로고
    • A dual-tropic primary HIV-1 isolate that uses fusin and the beta-chemokine receptors CKR-5, CKR-3, and CKR-2b as fusion cofactors
    • Doranz BJ, Rucker J, Yi Y, et al. A dual-tropic primary HIV-1 isolate that uses fusin and the beta-chemokine receptors CKR-5, CKR-3, and CKR-2b as fusion cofactors. Cell 1996; 85: 1149-58
    • (1996) Cell , vol.85 , pp. 1149-1158
    • Doranz, B.J.1    Rucker, J.2    Yi, Y.3
  • 46
    • 0030002637 scopus 로고    scopus 로고
    • HIV-1 entry cofactor: Cloning of a seven transmembrane G protein-coupled receptor
    • Feng Y, Broder CC, Kennedy PE, et al. HIV-1 entry cofactor: cloning of a seven transmembrane G protein-coupled receptor. Science 1996; 272: 872-7
    • (1996) Science , vol.272 , pp. 872-877
    • Feng, Y.1    Broder, C.C.2    Kennedy, P.E.3
  • 47
    • 0042376485 scopus 로고    scopus 로고
    • A new classification for HIV-1
    • Berger EA, Doms RW, Fenyo EM, et al. A new classification for HIV-1 [letter]. Nature 1998; 391: 240
    • (1998) Nature , vol.391 , pp. 240
    • Berger, E.A.1    Doms, R.W.2    Fenyo, E.M.3
  • 48
    • 0029775576 scopus 로고    scopus 로고
    • The lymphocyte chemoattractant SDF-1 is a ligand for LESTR/fusin and blocks HIV-1 entry
    • Bleul CC, Farzan M, Choe H, et al. The lymphocyte chemoattractant SDF-1 is a ligand for LESTR/fusin and blocks HIV-1 entry. Nature 1996; 382: 829-33
    • (1996) Nature , vol.382 , pp. 829-833
    • Bleul, C.C.1    Farzan, M.2    Choe, H.3
  • 49
    • 16044370087 scopus 로고    scopus 로고
    • The CXC chemokine SDF-1 is the ligand for LESTR/fusin and prevents infection by T-cell-line-adapted HIV-1
    • Oberlin E, Amara A, Bachelerie F, et al. The CXC chemokine SDF-1 is the ligand for LESTR/fusin and prevents infection by T-cell-line-adapted HIV-1. Nature 1996; 382: 833-5
    • (1996) Nature , vol.382 , pp. 833-835
    • Oberlin, E.1    Amara, A.2    Bachelerie, F.3
  • 50
    • 0030670330 scopus 로고    scopus 로고
    • In vivo evolution of HIV-1 co-receptor usage and sensitivity to chemokine-mediated suppression
    • Scarlatti G, Tresoldi E, Bjorndal A, et al. In vivo evolution of HIV-1 co-receptor usage and sensitivity to chemokine-mediated suppression. Nat Med 1997; 3: 1259-65
    • (1997) Nat Med , vol.3 , pp. 1259-1265
    • Scarlatti, G.1    Tresoldi, E.2    Bjorndal, A.3
  • 51
    • 0031575431 scopus 로고    scopus 로고
    • Change in coreceptor use correlates with disease progression in HIV-1-infected individuals
    • Connor RI, Sheridan KE, Ceradini D, et al. 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
  • 52
    • 0034092634 scopus 로고    scopus 로고
    • XXII: Nomenclature for chemokine receptors
    • International union of pharmacology
    • Murphy PM, Baggiolini M, Charo IF, et al. International union of pharmacology. XXII: nomenclature for chemokine receptors. Pharmacol Rev 2000; 52: 145-76
    • (2000) Pharmacol Rev , vol.52 , pp. 145-176
    • Murphy, P.M.1    Baggiolini, M.2    Charo, I.F.3
  • 53
    • 0030812438 scopus 로고    scopus 로고
    • Molecular mechanism of desensitization of the chemokine receptor CCR-5: Receptor signaling and internalization are dissociable from its role as an HIV-1 co-receptor
    • Aramori I, Zhang J, Ferguson SG, et al. Molecular mechanism of desensitization of the chemokine receptor CCR-5: receptor signaling and internalization are dissociable from its role as an HIV-1 co-receptor. EMBO J 1997; 16: 4606-16
    • (1997) EMBO J , vol.16 , pp. 4606-4616
    • Aramori, I.1    Zhang, J.2    Ferguson, S.G.3
  • 54
    • 0030922697 scopus 로고    scopus 로고
    • Molecular uncoupling of C-C chemokine receptor 5-induced chemotaxis and signal transduction from HIV coreceptor activity
    • Gosling J, Monteclaro FS, Atchison RE, et al. Molecular uncoupling of C-C chemokine receptor 5-induced chemotaxis and signal transduction from HIV coreceptor activity. Proc Natl Acad Sci U S A 1997; 94: 5061-6
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 5061-5066
    • Gosling, J.1    Monteclaro, F.S.2    Atchison, R.E.3
  • 55
    • 0030745286 scopus 로고    scopus 로고
    • HIV coreceptor downregulation as antiviral principle: SDF-1α-dependent internalization of the chemokine receptor CXCR4 contributes to inhibition of viral replication
    • Amara A, Le Gall S, Schwartz O, et al. HIV coreceptor downregulation as antiviral principle: SDF-1α-dependent internalization of the chemokine receptor CXCR4 contributes to inhibition of viral replication. J Exp Med 1997; 186: 139-46
    • (1997) J Exp Med , vol.186 , pp. 139-146
    • Amara, A.1    Le Gall, S.2    Schwartz, O.3
  • 56
    • 0030749666 scopus 로고    scopus 로고
    • HIV-1 coreceptor activity of CCR5 and its inhibition by chemokines: Independence from G protein signaling and importance of coreceptor downmodulation
    • Alkhatib G, Locati M, Kennedy PE, et al. HIV-1 coreceptor activity of CCR5 and its inhibition by chemokines: independence from G protein signaling and importance of coreceptor downmodulation. Virology 1997; 234: 340-8
    • (1997) Virology , vol.234 , pp. 340-348
    • Alkhatib, G.1    Locati, M.2    Kennedy, P.E.3
  • 57
    • 11844302187 scopus 로고    scopus 로고
    • Chemokine receptors as new molecular targets for antiviral therapy
    • Santoro F, Vassena L, Lusso P. Chemokine receptors as new molecular targets for antiviral therapy. New Microbiol 2004; 27 Suppl. 1: 17-29
    • (2004) New Microbiol , vol.27 , Issue.SUPPL. , pp. 17-29
    • Santoro, F.1    Vassena, L.2    Lusso, P.3
  • 58
    • 0033152142 scopus 로고    scopus 로고
    • The chemokine system: Redundancy for robust outputs
    • Mantovani A. The chemokine system: redundancy for robust outputs. Immunol Today 1999; 20: 254-7
    • (1999) Immunol Today , vol.20 , pp. 254-257
    • Mantovani, A.1
  • 59
    • 0001633495 scopus 로고    scopus 로고
    • Genetic restriction of HIV-1 infection and progression to AIDS by a deletion allele of the CKR5 structural gene
    • Dean M, Carrington M, Winkler C, et al. Genetic restriction of HIV-1 infection and progression to AIDS by a deletion allele of the CKR5 structural gene. Science 1996; 273: 1856-62
    • (1996) Science , vol.273 , pp. 1856-1862
    • Dean, M.1    Carrington, M.2    Winkler, C.3
  • 60
    • 16044367526 scopus 로고    scopus 로고
    • The role of a mutant CCR5 allele in HIV-1 transmission and disease progression
    • Huang Y, Paxton WA, Wolinsky SM, et al. The role of a mutant CCR5 allele in HIV-1 transmission and disease progression. Nat Med 1996; 2: 1240-3
    • (1996) Nat Med , vol.2 , pp. 1240-1243
    • Huang, Y.1    Paxton, W.A.2    Wolinsky, S.M.3
  • 61
    • 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, 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
  • 62
    • 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, 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
  • 63
    • 8244227329 scopus 로고    scopus 로고
    • Inherited resistance to HIV-1 conferred by an inactivating mutation in CC chemokine receptor 5: Studies in populations with contrasting clinical phenotypes, defined racial background, and quantified risk
    • Zimmerman PA, Buckler-White A, Alkhatib G, et al. Inherited resistance to HIV-1 conferred by an inactivating mutation in CC chemokine receptor 5: studies in populations with contrasting clinical phenotypes, defined racial background, and quantified risk. Mol Med 1997; 3: 23-36
    • (1997) Mol Med , vol.3 , pp. 23-36
    • Zimmerman, P.A.1    Buckler-White, A.2    Alkhatib, G.3
  • 64
    • 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, 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
  • 65
    • 16144365317 scopus 로고    scopus 로고
    • CD4-independent, antibody-sensitive interactions between HIV-1 and its co-receptor CCR-5
    • Trkola A, Dragic T, Arthos J, et al. CD4-independent, 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
  • 66
    • 0032546952 scopus 로고    scopus 로고
    • A conserved HIV gp120 glycoprotein structure involved in chemokine receptor binding
    • Rizzuto CD, Wyatt R, Hernandez-Ramos N, et al. A conserved HIV gp120 glycoprotein structure involved in chemokine receptor binding. Science 1998; 280: 1949-53
    • (1998) Science , vol.280 , pp. 1949-1953
    • Rizzuto, C.D.1    Wyatt, R.2    Hernandez-Ramos, N.3
  • 67
    • 2442625211 scopus 로고    scopus 로고
    • HIV-1 gp41 as a target for viral entry inhibition
    • Root MJ, Steger HK. HIV-1 gp41 as a target for viral entry inhibition. Curr Pharm Des 2004; 10: 1805-25
    • (2004) Curr Pharm Des , vol.10 , pp. 1805-1825
    • Root, M.J.1    Steger, H.K.2
  • 68
    • 0030962291 scopus 로고    scopus 로고
    • Atomic structure of the ectodomain from HIV-1 gp41
    • Weissenhorn W, Dessen A, Harrison SC, et al. Atomic structure of the ectodomain from HIV-1 gp41. Nature 1997; 387: 426-30
    • (1997) Nature , vol.387 , pp. 426-430
    • Weissenhorn, W.1    Dessen, A.2    Harrison, S.C.3
  • 69
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan DC, Fass D, Berger JM, et al. 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
  • 70
    • 0030780614 scopus 로고    scopus 로고
    • Atomic structure of a thermostable subdomain of HIV-1 gp41
    • Tan K, Liu J, Wang J, et al. Atomic structure of a thermostable subdomain of HIV-1 gp41. Proc Natl Acad Sci U S A 1997; 94: 12303-8
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 12303-12308
    • Tan, K.1    Liu, J.2    Wang, J.3
  • 71
    • 0028575843 scopus 로고
    • Propensity for a leucine zipper-like domain of the human immunodeficiency virus type 1 gp41 to form oligomers correlates with a role in virus-induced fusion rather than assembly of the glycoprotein complex
    • Wild C, Dubay JW, Greenwell T, et al. Propensity for a leucine zipper-like domain of the human immunodeficiency virus type 1 gp41 to form oligomers correlates with a role in virus-induced fusion rather than assembly of the glycoprotein complex. Proc Natl Acad Sci U S A 1994; 91: 12676-80
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 12676-12680
    • Wild, C.1    Dubay, J.W.2    Greenwell, T.3
  • 72
    • 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
  • 73
    • 0027959493 scopus 로고
    • Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection
    • Wild CT, Shugars DC, Greenwell TK, et al. Peptides corresponding to a predictive alpha-helical 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
  • 74
    • 0029926552 scopus 로고    scopus 로고
    • HIV-1 membrane fusion mechanism: Structural studies of the interactions between biologically-active peptides from gp41
    • Lawless MK, Barney S, Guthrie KI, et al. HIV-1 membrane fusion mechanism: structural studies of the interactions between biologically-active peptides from gp41. Biochemistry 1996; 35: 13697-708
    • (1996) Biochemistry , vol.35 , pp. 13697-13708
    • Lawless, M.K.1    Barney, S.2    Guthrie, K.I.3
  • 75
    • 0031473771 scopus 로고    scopus 로고
    • Inhibition of HIV type I infectivity by constrained alpha-helical peptides: Implications for viral fusion mechanism
    • Judice JK, Tom JY, Huang W, et al. Inhibition of HIV type I infectivity by constrained alpha-helical peptides: implications for viral fusion mechanism. Proc Natl Acad Sci U S A 1997; 94: 13426-30
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 13426-13430
    • Judice, J.K.1    Tom, J.Y.2    Huang, W.3
  • 76
    • 0031959601 scopus 로고    scopus 로고
    • Capture of an early fusion-active conformation of HIV-1 gp41
    • Furuta RA, Wild CT, Weng Y, et al. Capture of an early fusion-active conformation of HIV-1 gp41. 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
  • 77
    • 0026019437 scopus 로고
    • Dextran sulfate blocks antibody binding to the principal neutralizing domain of human immunodeficiency virus type 1 without interfering with gp120-CD4 interactions
    • Callahan LN, Phelan M, Mallinson M, et al. Dextran sulfate blocks antibody binding to the principal neutralizing domain of human immunodeficiency virus type 1 without interfering with gp120-CD4 interactions. J Virol 1991; 65: 1543-50
    • (1991) J Virol , vol.65 , pp. 1543-1550
    • Callahan, L.N.1    Phelan, M.2    Mallinson, M.3
  • 78
    • 0026705746 scopus 로고
    • The V3 region of the envelope glycoprotein of human immunodeficiency virus type 1 binds sulfated polysaccharides and CD4-derived synthetic peptides
    • Batinic D, Robey FA. The V3 region of the envelope glycoprotein of human immunodeficiency virus type 1 binds sulfated polysaccharides and CD4-derived synthetic peptides. J Biol Chem 1992; 267: 6664-71
    • (1992) J Biol Chem , vol.267 , pp. 6664-6671
    • Batinic, D.1    Robey, F.A.2
  • 79
    • 0028207130 scopus 로고
    • Heparin specifically inhibits binding of V3 loop antibodies to HIV-1 gp120, an effect potentiated by CD4 binding
    • Harrop HA, Coombe DR, Rider CC. Heparin specifically inhibits binding of V3 loop antibodies to HIV-1 gp120, an effect potentiated by CD4 binding. AIDS 1994; 8: 183-92
    • (1994) AIDS , vol.8 , pp. 183-192
    • Harrop, H.A.1    Coombe, D.R.2    Rider, C.C.3
  • 80
    • 0024502416 scopus 로고
    • Oral dextran sulfate (UA001) in the treatment of the acquired immunodeficiency syndrome (AIDS) and AIDS-related complex
    • Abrams DI, Kuno S, Wong R, et al. Oral dextran sulfate (UA001) in the treatment of the acquired immunodeficiency syndrome (AIDS) and AIDS-related complex. Ann Intern Med 1989; 110: 183-8
    • (1989) Ann Intern Med , vol.110 , pp. 183-188
    • Abrams, D.I.1    Kuno, S.2    Wong, R.3
  • 81
    • 0028021370 scopus 로고
    • Infection by HIV-1 blocked by binding of dextrin 2-sulphate to the cell surface of activated human peripheral blood mononuclear cells and cultured T-cells
    • Shaunak S, Gooderham NJ, Edwards RJ, et al. Infection by HIV-1 blocked by binding of dextrin 2-sulphate to the cell surface of activated human peripheral blood mononuclear cells and cultured T-cells. Br J Pharmacol 1994; 113: 151-8
    • (1994) Br J Pharmacol , vol.113 , pp. 151-158
    • Shaunak, S.1    Gooderham, N.J.2    Edwards, R.J.3
  • 82
    • 0030979349 scopus 로고    scopus 로고
    • Anti-HIV type 1 activity of sulfated derivatives of dextrin against primary viral isolates of HIV type 1 in ymphocytes and monocyte-derived macrophages
    • Javan CM, Gooderham NJ, Edwards RJ, et al. Anti-HIV type 1 activity of sulfated derivatives of dextrin against primary viral isolates of HIV type 1 in ymphocytes and monocyte-derived macrophages. AIDS Res Hum Retroviruses 1997; 13: 875-80
    • (1997) AIDS Res Hum Retroviruses , vol.13 , pp. 875-880
    • Javan, C.M.1    Gooderham, N.J.2    Edwards, R.J.3
  • 83
    • 12644279857 scopus 로고    scopus 로고
    • A placebo-controlled, double-blind prospective study in healthy female volunteers of dextrin sulphate gel: A novel potential intravaginal virucide
    • Stafford MK, Cain D, Rosenstein I, et al. A placebo-controlled, double-blind prospective study in healthy female volunteers of dextrin sulphate gel: a novel potential intravaginal virucide. J Acquir Immune Defic Syndr Hum Retrovirol 1997; 14: 213-8
    • (1997) J Acquir Immune Defic Syndr Hum Retrovirol , vol.14 , pp. 213-218
    • Stafford, M.K.1    Cain, D.2    Rosenstein, I.3
  • 84
    • 0031924987 scopus 로고    scopus 로고
    • Effect on normal vaginal flora of three intravaginal microbicidal agents potentially active against human immunodeficiency virus type 1
    • Rosenstein IJ, Stafford MK, Kitchen VS, et al. Effect on normal vaginal flora of three intravaginal microbicidal agents potentially active against human immunodeficiency virus type 1. J Infect Dis 1998; 177: 1385-90
    • (1998) J Infect Dis , vol.177 , pp. 1385-1390
    • Rosenstein, I.J.1    Stafford, M.K.2    Kitchen, V.S.3
  • 85
    • 0036892030 scopus 로고    scopus 로고
    • Dextrin sulfate as a vaginal microbicide: Randomized, double-blind, placebo-controlled trial including healthy female volunteers and their male partners
    • Low-Beer N, Gabe R, McCormack S, et al. Dextrin sulfate as a vaginal microbicide: randomized, double-blind, placebo-controlled trial including healthy female volunteers and their male partners. J Acquir Immune Defic Syndr 2002; 31: 391-8
    • (2002) J Acquir Immune Defic Syndr , vol.31 , pp. 391-398
    • Low-Beer, N.1    Gabe, R.2    McCormack, S.3
  • 86
    • 0029062687 scopus 로고
    • Expression and characterization of CD4-IgG2, a novel heterotetramer that neutralizes primary HIV type 1 isolates
    • Allaway GP, Davis-Bruno KL, Beaudry GA, et al. Expression and characterization of CD4-IgG2, a novel heterotetramer that neutralizes primary HIV type 1 isolates. AIDS Res Hum Retroviruses 1995; 11: 533-9
    • (1995) AIDS Res Hum Retroviruses , vol.11 , pp. 533-539
    • Allaway, G.P.1    Davis-Bruno, K.L.2    Beaudry, G.A.3
  • 87
    • 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, 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
  • 88
    • 0031936306 scopus 로고    scopus 로고
    • Neutralization sensitivity of human immunodeficiency virus type 1 primary isolates to antibodies and CD4-based reagents is independent of coreceptor usage
    • Trkola A, Ketas T, Kewalramani VN, et al. Neutralization sensitivity of human immunodeficiency virus type 1 primary isolates to antibodies and CD4-based reagents is independent of coreceptor usage. J Virol 1998; 72: 1876-85
    • (1998) J Virol , vol.72 , pp. 1876-1885
    • Trkola, A.1    Ketas, T.2    Kewalramani, V.N.3
  • 89
    • 0037321703 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 attachment, coreceptor, and fusion inhibitors are active against both direct and trans infection of primary cells
    • Ketas TJ, Frank I, Klasse PJ, et al. Human immunodeficiency virus type 1 attachment, coreceptor, and fusion inhibitors are active against both direct and trans infection of primary cells. J Virol 2003; 77: 2762-7
    • (2003) J Virol , vol.77 , pp. 2762-2767
    • Ketas, T.J.1    Frank, I.2    Klasse, P.J.3
  • 90
    • 2442428094 scopus 로고    scopus 로고
    • Blockade of attachment and fusion receptors inhibits HIV-1 infection of human cervical tissue
    • Hu Q, Frank I, Williams V et al. Blockade of attachment and fusion receptors inhibits HIV-1 infection of human cervical tissue. J Exp Med 2004; 199: 1065-75
    • (2004) J Exp Med , vol.199 , pp. 1065-1075
    • Hu, Q.1    Frank, I.2    Williams, V.3
  • 91
    • 0033914939 scopus 로고    scopus 로고
    • Single-dose safety, pharmacology, and antiviral activity of the human immunodeficiency virus (HIV) type 1 entry inhibitor PRO 542 in HIV-infected adults
    • Jacobson JM, Lowy I, Fletcher CV, et al. Single-dose safety, pharmacology, and antiviral activity of the human immunodeficiency virus (HIV) type 1 entry inhibitor PRO 542 in HIV-infected adults. J Infect Dis 2000; 182: 326-9
    • (2000) J Infect Dis , vol.182 , pp. 326-329
    • Jacobson, J.M.1    Lowy, I.2    Fletcher, C.V.3
  • 92
    • 0033712475 scopus 로고    scopus 로고
    • Recombinant CD4-IgG2 in human immunodeficiency virus type 1-infected children: Phase 1/2 study
    • The Pediatric AIDS Clinical Trials Group Protocol 351 Study Team
    • Shearer WT, Israel RJ, Starr S, et al. Recombinant CD4-IgG2 in human immunodeficiency virus type 1-infected children: phase 1/2 study. The Pediatric AIDS Clinical Trials Group Protocol 351 Study Team. J Infect Dis 2000; 182: 1774-9
    • (2000) J Infect Dis , vol.182 , pp. 1774-1779
    • Shearer, W.T.1    Israel, R.J.2    Starr, S.3
  • 94
    • 9144250171 scopus 로고    scopus 로고
    • Treatment of advanced human immunodeficiency virus type 1 disease with the viral entry inhibitor PRO 542
    • Jacobson JM, Israel RJ, Lowy I, et al. Treatment of advanced human immunodeficiency virus type 1 disease with the viral entry inhibitor PRO 542. Antimicrob Agents Chemother 2004; 48: 423-9
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 423-429
    • Jacobson, J.M.1    Israel, R.J.2    Lowy, I.3
  • 95
    • 0035313589 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 entry inhibitors PRO 542 and T-20 are potently synergistic in blocking virus-cell and cell-cell fusion
    • Nagashima KA, Thompson DA, Rosenfield SI, et al. Human immunodeficiency virus type 1 entry inhibitors PRO 542 and T-20 are potently synergistic in blocking virus-cell and cell-cell fusion. J Infect Dis 2001; 183: 1121-5
    • (2001) J Infect Dis , vol.183 , pp. 1121-1125
    • Nagashima, K.A.1    Thompson, D.A.2    Rosenfield, S.I.3
  • 96
    • 0026654557 scopus 로고
    • A monoclonal antibody to CD4 domain 2 blocks soluble CD4-induced conformational changes in the envelope glycoproteins of human immunodeficiency virus type 1 (HIV-1) and HIV infection of CD4+ cells
    • Moore JP, Sattentau QJ, Klasse PJ, et al. A monoclonal antibody to CD4 domain 2 blocks soluble CD4-induced conformational changes in the envelope glycoproteins of human immunodeficiency virus type 1 (HIV-1) and HIV infection of CD4+ cells. J Virol 1992; 66: 4784-93
    • (1992) J Virol , vol.66 , pp. 4784-4793
    • Moore, J.P.1    Sattentau, Q.J.2    Klasse, P.J.3
  • 97
    • 0027477548 scopus 로고
    • In vivo administration to rhesus monkeys of a CD4-spedfic monoclonal antibody capable of blocking AIDS virus replication
    • Reimann KA, Burkly LC, Burrus B, et al. In vivo administration to rhesus monkeys of a CD4-spedfic monoclonal antibody capable of blocking AIDS virus replication. AIDS Res Hum Retroviruses 1993; 9: 199-207
    • (1993) AIDS Res Hum Retroviruses , vol.9 , pp. 199-207
    • Reimann, K.A.1    Burkly, L.C.2    Burrus, B.3
  • 98
    • 0030788879 scopus 로고    scopus 로고
    • A humanized form of a CD4-specific monoclonal antibody exhibits decreased antigenicity and prolonged plasma half-life in rhesus monkeys while retaining its unique biological and antiviral properties
    • Reimann KA, Lin W, Bixler S, et al. A humanized form of a CD4-specific monoclonal antibody exhibits decreased antigenicity and prolonged plasma half-life in rhesus monkeys while retaining its unique biological and antiviral properties. AIDS Res Hum Retroviruses 1997; 13: 933-43
    • (1997) AIDS Res Hum Retroviruses , vol.13 , pp. 933-943
    • Reimann, K.A.1    Lin, W.2    Bixler, S.3
  • 99
    • 0036343301 scopus 로고    scopus 로고
    • A humanized, nondepleting anti-CD4 antibody that blocks virus entry inhibits virus replication in rhesus monkeys chronically infected with simian immunodeficiency virus
    • Reimann KA, Khunkhun R, Lin W, et al. A humanized, nondepleting anti-CD4 antibody that blocks virus entry inhibits virus replication in rhesus monkeys chronically infected with simian immunodeficiency virus. AIDS Res Hum Retroviruses 2002; 18: 747-55
    • (2002) AIDS Res Hum Retroviruses , vol.18 , pp. 747-755
    • Reimann, K.A.1    Khunkhun, R.2    Lin, W.3
  • 100
    • 0037006883 scopus 로고    scopus 로고
    • Development of anti-CD4 MAb hu5A8 for treatment of HIV-1 infection: Preclinical assessment in non-human primates
    • Boon L, Holland B, Gordon W, et al. Development of anti-CD4 MAb hu5A8 for treatment of HIV-1 infection: preclinical assessment in non-human primates. Toxicology 2002; 172: 191-203
    • (2002) Toxicology , vol.172 , pp. 191-203
    • Boon, L.1    Holland, B.2    Gordon, W.3
  • 101
    • 9144236197 scopus 로고    scopus 로고
    • Antiretroviral activity of the anti-CD4 monoclonal antibody TNX-355 in patients infected with HIV type 1
    • Kuritzkes DR, Jacobson J, Powderly WG, et al. Antiretroviral activity of the anti-CD4 monoclonal antibody TNX-355 in patients infected with HIV type 1. J Infect Dis 2004; 189: 286-91
    • (2004) J Infect Dis , vol.189 , pp. 286-291
    • Kuritzkes, D.R.1    Jacobson, J.2    Powderly, W.G.3
  • 102
    • 85069108481 scopus 로고    scopus 로고
    • [Online]. Available from URL
    • Tanox, Inc. [online]. Available from URL: http://www.tanox.com [Accessed 2005 Mar 7]
  • 104
    • 20844457360 scopus 로고    scopus 로고
    • Characterization of a small molecule HIV-1 attachment inhibitor BMS-488043: Virology, resistance and mechanism of action
    • Feb 8-11; Chicago
    • Lin PF, Ho HT, Gong YF, et al. Characterization of a small molecule HIV-1 attachment inhibitor BMS-488043: virology, resistance and mechanism of action [abstract no. 535]. 11th Conference on Retroviruses and Opportunistic Infections (CROI); 2004 Feb 8-11; Chicago
    • (2004) 11th Conference on Retroviruses and Opportunistic Infections (CROI)
    • Lin, P.F.1    Ho, H.T.2    Gong, Y.F.3
  • 105
    • 1842851672 scopus 로고    scopus 로고
    • Safety, tolerability, and pharmacokinetics of a novel, small-molecule HIV-1 attachment inhibitor, BMS-488043, after single and multiple oral doses in healthy subjects
    • Feb 8-11; Chicago
    • Hanna G, Yan JH, Fiske W, et al. Safety, tolerability, and pharmacokinetics of a novel, small-molecule HIV-1 attachment inhibitor, BMS-488043, after single and multiple oral doses in healthy subjects [abstract no. 535]. 11th Conference on Retroviruses and Opportunistic Infections (CROI); 2004 Feb 8-11; Chicago
    • (2004) 11th Conference on Retroviruses and Opportunistic Infections (CROI)
    • Hanna, G.1    Yan, J.H.2    Fiske, W.3
  • 106
    • 2642541113 scopus 로고    scopus 로고
    • Antiviral activity, safety, and tolerability of a novel, oral small-molecule HIV-1 attachment inhibitor, BMS-488043, in HIV-1 infected subjects
    • Feb 8-11; Chicago
    • Hanna G, Lalezari J, Hellinger J, et al. Antiviral activity, safety, and tolerability of a novel, oral small-molecule HIV-1 attachment inhibitor, BMS-488043, in HIV-1 infected subjects [abstract no. 141 (oral)]. 11th Conference on Retroviruses and Opportunistic Infections (CROI); 2004 Feb 8-11; Chicago
    • (2004) 11th Conference on Retroviruses and Opportunistic Infections (CROI)
    • Hanna, G.1    Lalezari, J.2    Hellinger, J.3
  • 107
    • 4644227515 scopus 로고    scopus 로고
    • Safety, pharmacokinetics, and antiviral activity of AMD3100, a selective CXCR4 receptor inhibitor, in HIV-1 infection
    • Hendrix CW, Collier AC, Lederman MM, et al. Safety, pharmacokinetics, and antiviral activity of AMD3100, a selective CXCR4 receptor inhibitor, in HIV-1 infection. J Acquir Immune Defic Syndr 2004; 37: 1253-62
    • (2004) J Acquir Immune Defic Syndr , vol.37 , pp. 1253-1262
    • Hendrix, C.W.1    Collier, A.C.2    Lederman, M.M.3
  • 108
    • 2342544143 scopus 로고    scopus 로고
    • Piperazine-based CCR5 antagonists as HIV-1 inhibitors. IV: Discovery of 1-[(4,6-dimethyl-5-pyrimidinyl)carbonyl]-4-[4-[2-methoxy-1(R) -4-(trifluoromethyl)phenyl]ethyl-3(S)-methyl-1-piperazinyl]4-methylpiperidine (Sch-417690/Sch-D), a potent, highly selective, and orally bioavailable CCR5 antagonist
    • Tagat JR, McCombie SW, Nazareno D, et al. Piperazine-based CCR5 antagonists as HIV-1 inhibitors. IV: discovery of 1-[(4,6-dimethyl-5- pyrimidinyl)carbonyl]-4-[4-[2-methoxy-1(R)-4-(trifluoromethyl)phenyl]ethyl-3(S) -methyl-1-piperazinyl]4-methylpiperidine (Sch-417690/Sch-D), a potent, highly selective, and orally bioavailable CCR5 antagonist. J Med Chem 2004; 47: 2405-8
    • (2004) J Med Chem , vol.47 , pp. 2405-2408
    • Tagat, J.R.1    McCombie, S.W.2    Nazareno, D.3
  • 109
    • 85069106821 scopus 로고    scopus 로고
    • Data on file, Schering-Plough Research Institute, 2004 Sep 23
    • Data on file, Schering-Plough Research Institute, 2004 Sep 23
  • 111
    • 0042896003 scopus 로고    scopus 로고
    • UK-427,857, a novel small molecule HIV entry inhibitor is a specific antagonist of the chemokine receptor CCR5
    • Feb 10-14; Boston
    • Dorr P, Macartney M, Rickett G, et al. UK-427,857, a novel small molecule HIV entry inhibitor is a specific antagonist of the chemokine receptor CCR5 [abstract no. 12 (oral)]. 10th Conference on Retroviruses and Opportunistic Infections (CROI); 2003 Feb 10-14; Boston
    • (2003) 10th Conference on Retroviruses and Opportunistic Infections (CROI)
    • Dorr, P.1    Macartney, M.2    Rickett, G.3
  • 114
    • 3543092371 scopus 로고    scopus 로고
    • The effect of P450 inducers on the pharmacokinetics of CCR5 antagonist UK-427,857, in healthy volunteers
    • Apr 1-3; Rome
    • Jenkins T, Abel S, Russell D, et al. The effect of P450 inducers on the pharmacokinetics of CCR5 antagonist UK-427,857, in healthy volunteers [abstract no. 37 (oral)]. 5th International Workshop on Clinical Pharmacology of HIV Therapy; 2004 Apr 1-3; Rome
    • (2004) 5th International Workshop on Clinical Pharmacology of HIV Therapy
    • Jenkins, T.1    Abel, S.2    Russell, D.3
  • 115
    • 3543092371 scopus 로고    scopus 로고
    • The effect of CYP3A4 inhibitors on the pharmacokinetics of CCR5 antagonist UK-427,857, in healthy volunteers
    • Apr 1-3; Rome
    • Abel S, Russell D, Ridgway C, et al. The effect of CYP3A4 inhibitors on the pharmacokinetics of CCR5 antagonist UK-427,857, in healthy volunteers [abstract no. 41]. 5th International Workshop on Clinical Pharmacology of HIV Therapy; 2004 Apr 1-3; Rome
    • (2004) 5th International Workshop on Clinical Pharmacology of HIV Therapy
    • Abel, S.1    Russell, D.2    Ridgway, C.3
  • 117
    • 9744254946 scopus 로고    scopus 로고
    • Evaluation of dosing frequency and food effect on viral load reduction during short-term monotherapy with UK-427,857, a novel CCR5 antagonist
    • Jul 11-16; Bangkok
    • Fätkenheuer G, Pozniak A, Johnson M, et al. Evaluation of dosing frequency and food effect on viral load reduction during short-term monotherapy with UK-427,857, a novel CCR5 antagonist [abstract no. B4489]. 15th International AIDS Conference (IAC); 2004 Jul 11-16; Bangkok
    • (2004) 15th International AIDS Conference (IAC)
    • Fätkenheuer, G.1    Pozniak, A.2    Johnson, M.3
  • 118
    • 9744274175 scopus 로고    scopus 로고
    • Modeling of UK-427,857, a novel CCR5 antagonist, efficacy in short-term monotherapy
    • Jul 11-16; Bangkok
    • Rosario MC, Poland W, Felstead S, et al. Modeling of UK-427,857, a novel CCR5 antagonist, efficacy in short-term monotherapy [poster; abstract no. B4479]. 15th International AIDS Conference (IAC); 2004 Jul 11-16; Bangkok
    • (2004) 15th International AIDS Conference (IAC)
    • Rosario, M.C.1    Poland, W.2    Felstead, S.3
  • 119
    • 85069109594 scopus 로고    scopus 로고
    • Data on file, Pfizer, 2004 Aug 24
    • Data on file, Pfizer, 2004 Aug 24
  • 120
    • 56749105701 scopus 로고    scopus 로고
    • In vitro escape of R5 primary isolates from the CCR5 antagonist, UK-427,857 is difficult and involves continued use of the CCR5 receptor
    • Jun 8-12; Tenerife
    • Westby M, Smith-Burchnell C, Mori J, et al. In vitro escape of R5 primary isolates from the CCR5 antagonist, UK-427,857 is difficult and involves continued use of the CCR5 receptor [abstract no. 6 (oral)]. 13th International HIV Drug Resistance Workshop; 2004 Jun 8-12; Tenerife
    • (2004) 13th International HIV Drug Resistance Workshop
    • Westby, M.1    Smith-Burchnell, C.2    Mori, J.3
  • 121
    • 3543144738 scopus 로고    scopus 로고
    • Spirodiketopiperazine-based CCR5 inhibitor which preserves CC-chemokine/CCR5 interactions and exerts potent activity against R5 human immunodeficiency virus type 1 in vitro
    • Maeda K, Nakata H, Koh Y, et al. Spirodiketopiperazine-based CCR5 inhibitor which preserves CC-chemokine/CCR5 interactions and exerts potent activity against R5 human immunodeficiency virus type 1 in vitro. J Virol 2004; 78: 8654-62
    • (2004) J Virol , vol.78 , pp. 8654-8662
    • Maeda, K.1    Nakata, H.2    Koh, Y.3
  • 122
    • 33749175267 scopus 로고    scopus 로고
    • A novel CCR5 antagonist, 873140, exhibits potent in vitro anti-HIV activity
    • Jul 11-16; Bangkok
    • Demarest J, Shibayama S, Ferris R, et al. A novel CCR5 antagonist, 873140, exhibits potent in vitro anti-HIV activity [abstract no. 1231 (oral)]. 15th International AIDS Conference (IAC); 2004 Jul 11-16; Bangkok
    • (2004) 15th International AIDS Conference (IAC)
    • Demarest, J.1    Shibayama, S.2    Ferris, R.3
  • 123
    • 0042896002 scopus 로고    scopus 로고
    • Potent in vivo anti-R5-HIV effects of AK602, a novel spirodiketopiperazine (SPD)-containing HIV-specific CCR5 inhibitor, in hu-PBMC-NOD-mice
    • Feb 10-14; Boston
    • Nakata H, Maeda K, Kawano Y, et al. Potent in vivo anti-R5-HIV effects of AK602, a novel spirodiketopiperazine (SPD)-containing HIV-specific CCR5 inhibitor, in hu-PBMC-NOD-mice [abstract no. 564a]. 10th Conference on Retroviruses and Opportunistic Infections (CROI); 2003 Feb 10-14; Boston
    • (2003) 10th Conference on Retroviruses and Opportunistic Infections (CROI)
    • Nakata, H.1    Maeda, K.2    Kawano, Y.3
  • 124
    • 18644367615 scopus 로고    scopus 로고
    • Greater synergistic anti-HIV effects upon combinations of CCR5 inhibitor AK602/ONO4128/GW873140 with CXCR4 inhibitors than with other anti-HIV drugs
    • Feb 22-25; Boston
    • Nakata H, Koh Y, Maeda K, et al. Greater synergistic anti-HIV effects upon combinations of CCR5 inhibitor AK602/ONO4128/GW873140 with CXCR4 inhibitors than with other anti-HIV drugs [abstract no. 543]. 12th Conference on Retroviruses and Opportunistic Infections (CROI); 2005 Feb 22-25; Boston
    • (2005) 12th Conference on Retroviruses and Opportunistic Infections (CROI)
    • Nakata, H.1    Koh, Y.2    Maeda, K.3
  • 125
    • 2642541894 scopus 로고    scopus 로고
    • Single and multiple dose escalation study to investigate the safety, pharmacokinetics, and receptor binding of GW873140, a novel CCR5 receptor antagonist, in healthy subjects
    • Feb 8-11; San Francisco
    • Demarest J, Adkison K, Sparks S, et al. Single and multiple dose escalation study to investigate the safety, pharmacokinetics, and receptor binding of GW873140, a novel CCR5 receptor antagonist, in healthy subjects [abstract no. 139 (oral)]. 11th Conference on Retroviruses and Opportunistic Infections (CROI); 2004 Feb 8-11; San Francisco
    • (2004) 11th Conference on Retroviruses and Opportunistic Infections (CROI)
    • Demarest, J.1    Adkison, K.2    Sparks, S.3
  • 126
    • 0032902710 scopus 로고    scopus 로고
    • Differential inhibition of human immunodeficiency virus type 1 fusion, gp120 binding, and CC-chemokine activity by monoclonal antibodies to CCR5
    • Olson WC, Rabut GE, Nagashima KA, et al. Differential inhibition of human immunodeficiency virus type 1 fusion, gp120 binding, and CC-chemokine activity by monoclonal antibodies to CCR5. J Virol 1999; 73: 4145-55
    • (1999) J Virol , vol.73 , pp. 4145-4155
    • Olson, W.C.1    Rabut, G.E.2    Nagashima, K.A.3
  • 127
    • 0035173073 scopus 로고    scopus 로고
    • Potent, broad-spectrum inhibition of human immunodeficiency virus type 1 by the CCR5 monoclonal antibody PRO 140
    • Trkola A, Ketas TJ, Nagashima KA, et al. Potent, broad-spectrum inhibition of human immunodeficiency virus type 1 by the CCR5 monoclonal antibody PRO 140. J Virol 2001; 75: 579-88
    • (2001) J Virol , vol.75 , pp. 579-588
    • Trkola, A.1    Ketas, T.J.2    Nagashima, K.A.3
  • 130
    • 3543120534 scopus 로고    scopus 로고
    • In vitro anti-HIV activity profile of AMD877, a novel CCR5 antagonist, in combination with the CXCR4 inhibitor AMD070
    • Feb 8-11; San Francisco
    • Schols D, Vermeire K, Hatse S, et al. In vitro anti-HIV activity profile of AMD877, a novel CCR5 antagonist, in combination with the CXCR4 inhibitor AMD070 [abstract no. 539]. 11th Conference on Retroviruses and Opportunistic Infections (CROI); 2004 Feb 8-11; San Francisco
    • (2004) 11th Conference on Retroviruses and Opportunistic Infections (CROI)
    • Schols, D.1    Vermeire, K.2    Hatse, S.3
  • 131
    • 0036302147 scopus 로고    scopus 로고
    • G-CSF induced stem cell mobilization by decreasing bone marrow SDF-1 and upregulating CXCR4
    • Petit I, Szyper-Kravitz M, Nagler A, et al. G-CSF induced stem cell mobilization by decreasing bone marrow SDF-1 and upregulating CXCR4. Nat Immunol 2002; 3: 687-94
    • (2002) Nat Immunol , vol.3 , pp. 687-694
    • Petit, I.1    Szyper-Kravitz, M.2    Nagler, A.3
  • 132
    • 84856504974 scopus 로고    scopus 로고
    • Biologic activity of an orally bioavailable CXCR4 antagonist in human subjects
    • Jul 11-16; Bangkok
    • Hendrix CW, Stone N, Dunaway S, et al. Biologic activity of an orally bioavailable CXCR4 antagonist in human subjects [abstract no. B4-475]. 15th International AIDS Conference (IAC); 2004 Jul 11-16; Bangkok
    • (2004) 15th International AIDS Conference (IAC)
    • Hendrix, C.W.1    Stone, N.2    Dunaway, S.3
  • 134
    • 18644382810 scopus 로고    scopus 로고
    • KRH-2731-5HCl: A new potent and orally bioavailable X4 HIV-1 inhibiting CXCR4 antagonist in vivo
    • Jul 11-16; Bangkok
    • Murakami T, Yoshida A, Kumakura S, et al. KRH-2731-5HCl: a new potent and orally bioavailable X4 HIV-1 inhibiting CXCR4 antagonist in vivo [abstract no. LbA01 (oral)]. 15th International AIDS Conference (IAC); 2004 Jul 11-16; Bangkok
    • (2004) 15th International AIDS Conference (IAC)
    • Murakami, T.1    Yoshida, A.2    Kumakura, S.3
  • 136
    • 1642391068 scopus 로고    scopus 로고
    • Enfuvirtide: The first therapy to inhibit the entry of HIV-1 into host CD4 lymphocytes
    • Matthews T, Salgo M, Greenberg M, et al. Enfuvirtide: the first therapy to inhibit the entry of HIV-1 into host CD4 lymphocytes. Nat Rev Drug Discov 2004; 3: 215
    • (2004) Nat Rev Drug Discov , vol.3 , pp. 215
    • Matthews, T.1    Salgo, M.2    Greenberg, M.3
  • 137
    • 1642276292 scopus 로고    scopus 로고
    • Enfuvirtide: Antiretroviral class 4, drug 1
    • Asboe D. Enfuvirtide: antiretroviral class 4, drug 1. HIV Clin Trials 2004; 5: 1-6
    • (2004) HIV Clin Trials , vol.5 , pp. 1-6
    • Asboe, D.1
  • 138
    • 0037569181 scopus 로고    scopus 로고
    • Enfuvirtide, a new drug for HIV infection
    • Fletcher CV. Enfuvirtide, a new drug for HIV infection. Lancet 2003; 361: 1577-8
    • (2003) Lancet , vol.361 , pp. 1577-1578
    • Fletcher, C.V.1
  • 139
    • 0347989455 scopus 로고    scopus 로고
    • Enfuvirtide
    • Dando TM, Perry CM. Enfuvirtide. Drugs 2003; 63 (24): 2755-66
    • (2003) Drugs , vol.63 , Issue.24 , pp. 2755-2766
    • Dando, T.M.1    Perry, C.M.2
  • 140
    • 0142187273 scopus 로고    scopus 로고
    • Enfuvirtide (T-20): A novel human immunodeficiency virus type 1 fusion inhibitor
    • Cervia JS, Smith MA. Enfuvirtide (T-20): a novel human immunodeficiency virus type 1 fusion inhibitor. Clin Infect Dis 2003; 37: 1102-6
    • (2003) Clin Infect Dis , vol.37 , pp. 1102-1106
    • Cervia, J.S.1    Smith, M.A.2
  • 141
    • 0642340674 scopus 로고    scopus 로고
    • US FDA approves new class of HIV therapeutics
    • Robertson D. US FDA approves new class of HIV therapeutics. Nat Biotechnol 2003; 21: 470-1
    • (2003) Nat Biotechnol , vol.21 , pp. 470-471
    • Robertson, D.1
  • 142
    • 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
  • 143
    • 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, et al. 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
  • 144
    • 0037667047 scopus 로고    scopus 로고
    • Large-scale manufacture of peptide therapeutics by chemical synthesis
    • Bray BL. Large-scale manufacture of peptide therapeutics by chemical synthesis. Nat Rev Drug Discov 2003; 2: 587-93
    • (2003) Nat Rev Drug Discov , vol.2 , pp. 587-593
    • Bray, B.L.1
  • 145
    • 0035120510 scopus 로고    scopus 로고
    • Membrane-anchored peptide inhibits human immunodeficiency virus entry
    • Hildinger M, Dittmar MT, Schult-Dietrich P, et al. Membrane-anchored peptide inhibits human immunodeficiency virus entry. J Virol 2001; 75: 3038-42
    • (2001) J Virol , vol.75 , pp. 3038-3042
    • Hildinger, M.1    Dittmar, M.T.2    Schult-Dietrich, P.3
  • 146
    • 0037059049 scopus 로고    scopus 로고
    • Sensitivity of HIV-1 to entry inhibitors correlates with envelope/coreceptor affinity, receptor density, and fusion kinetics
    • Reeves JD, Gallo SA, Ahmid N, et al. Sensitivity of HIV-1 to entry inhibitors correlates with envelope/coreceptor affinity, receptor density, and fusion kinetics. Proc Natl Acad Sci U S A 2002; 99: 16249-54
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 16249-16254
    • Reeves, J.D.1    Gallo, S.A.2    Ahmid, N.3
  • 147
    • 0033856458 scopus 로고    scopus 로고
    • Sensitivity of human immunodeficiency virus type 1 to the fusion inhibitor T-20 is modulated by corereptor specificity defined by the V3 loop of gp120
    • Derdeyn CA, Decker JM, Sfakianos JN, et al. Sensitivity of human immunodeficiency virus type 1 to the fusion inhibitor T-20 is modulated by corereptor specificity defined by the V3 loop of gp120. J Virol 2000; 74: 8358-67
    • (2000) J Virol , vol.74 , pp. 8358-8367
    • Derdeyn, C.A.1    Decker, J.M.2    Sfakianos, J.N.3
  • 148
    • 0034890660 scopus 로고    scopus 로고
    • Sensitivity of human immunodeficiency virus type 1 to fusion inhibitors targeted to the gp41 first heptad repeat involves distinct regions of gp41 and is consistently modulated by gp120 interactions with the coreceptor
    • Derdeyn CA, Decker JM, Sfakianos JN, et al. Sensitivity of human immunodeficiency virus type 1 to fusion inhibitors targeted to the gp41 first heptad repeat involves distinct regions of gp41 and is consistently modulated by gp120 interactions with the coreceptor. J Virol 2001; 75: 8605-14
    • (2001) J Virol , vol.75 , pp. 8605-8614
    • Derdeyn, C.A.1    Decker, J.M.2    Sfakianos, J.N.3
  • 149
    • 2642547308 scopus 로고    scopus 로고
    • Sensitivity of HIV type 1 subtype C isolates to the entry inhibitor T-20
    • Cilliers T, Patience T, Pillay C, et al. Sensitivity of HIV type 1 subtype C isolates to the entry inhibitor T-20. AIDS Res Hum Retroviruses 2004; 20: 477-82
    • (2004) AIDS Res Hum Retroviruses , vol.20 , pp. 477-482
    • Cilliers, T.1    Patience, T.2    Pillay, C.3
  • 150
    • 1842502574 scopus 로고    scopus 로고
    • Are fusion inhibitors active against all HIV variants?
    • Poveda E, Rodes B, Toro C, et al. Are fusion inhibitors active against all HIV variants? AIDS Res Hum Retroviruses 2004; 20: 347-8
    • (2004) AIDS Res Hum Retroviruses , vol.20 , pp. 347-348
    • Poveda, E.1    Rodes, B.2    Toro, C.3
  • 151
    • 1542319002 scopus 로고    scopus 로고
    • Susceptibility of HIV-2, SIV and SHIV to various anti-HIV-1 compounds: Implications for treatment and postexposure prophylaxis
    • Witvrouw M, Pannecouque C, Switzer WM, et al. Susceptibility of HIV-2, SIV and SHIV to various anti-HIV-1 compounds: implications for treatment and postexposure prophylaxis. Antiviral Ther 2004; 9: 57-65
    • (2004) Antiviral Ther , vol.9 , pp. 57-65
    • Witvrouw, M.1    Pannecouque, C.2    Switzer, W.M.3
  • 152
    • 0000934194 scopus 로고    scopus 로고
    • T20/DP178, an ectodomain peptide of human immunodeficiency virus type 1 gp41, is an activator of human phagocyte N-formyl peptide receptor
    • Su SB, Gong WH, Gao JL et al. T20/DP178, an ectodomain peptide of human immunodeficiency virus type 1 gp41, is an activator of human phagocyte N-formyl peptide receptor. Blood 1999; 93: 3885-92
    • (1999) Blood , vol.93 , pp. 3885-3892
    • Su, S.B.1    Gong, W.H.2    Gao, J.L.3
  • 153
    • 0034674332 scopus 로고    scopus 로고
    • The HIV-1 cell entry inhibitor T-20 potently chemoattracts neutrophils by specifically activating the N-formylpeptide receptor
    • Hartt JK, Liang T, Sahagun-Ruiz A, et al. The HIV-1 cell entry inhibitor T-20 potently chemoattracts neutrophils by specifically activating the N-formylpeptide receptor. Biochem Biophys Res Commun 2000; 272: 699-704
    • (2000) Biochem Biophys Res Commun , vol.272 , pp. 699-704
    • Hartt, J.K.1    Liang, T.2    Sahagun-Ruiz, A.3
  • 154
    • 0035383774 scopus 로고    scopus 로고
    • Activation of the formyl peptide receptor by the HIV-derived peptide T-20 suppresses interleukin-12 p70 production by human monocytes
    • Braun MC, Wang JM, Lahey E, et al. Activation of the formyl peptide receptor by the HIV-derived peptide T-20 suppresses interleukin-12 p70 production by human monocytes. Blood 2001; 97: 3531-6
    • (2001) Blood , vol.97 , pp. 3531-3536
    • Braun, M.C.1    Wang, J.M.2    Lahey, E.3
  • 156
    • 3543049211 scopus 로고    scopus 로고
    • Inter- and intra-individual variability of enfuvirtide (ENV) plasma trough concentrations (Ctrough) in the clinical setting
    • Apr 1-3; Rome
    • Bonora S, Castagna A, Aguilar Marucco D, et al. Inter- and intra-individual variability of enfuvirtide (ENV) plasma trough concentrations (Ctrough) in the clinical setting [abstract no. 46]. 5th International Workshop on Clinical Pharmacology of HIV Therapy; 2004 Apr 1-3; Rome
    • (2004) 5th International Workshop on Clinical Pharmacology of HIV Therapy
    • Bonora, S.1    Castagna, A.2    Aguilar Marucco, D.3
  • 157
    • 4744357409 scopus 로고    scopus 로고
    • Penetration of enfuvirtide, tenofovir, efavirenz, and protease inhibitors in the genital tract of HIV-1-infected men
    • Ghosn J, Chaix ML, Peytavin G, et al. Penetration of enfuvirtide, tenofovir, efavirenz, and protease inhibitors in the genital tract of HIV-1-infected men. AIDS 2004; 18: 1958-61
    • (2004) AIDS , vol.18 , pp. 1958-1961
    • Ghosn, J.1    Chaix, M.L.2    Peytavin, G.3
  • 158
    • 0036066762 scopus 로고    scopus 로고
    • The safety, plasma pharmacokinetics, and antiviral activity of subcutaneous enfuvirtide (T-20), a peptide inhibitor of gp41-mediated virus fusion, in HIV-infected ac ults
    • Kilby JM, Lalezari JP, Eron JJ, et al. The safety, plasma pharmacokinetics, and antiviral activity of subcutaneous enfuvirtide (T-20), a peptide inhibitor of gp41-mediated virus fusion, in HIV-infected ac ults. AIDS Res Hum Retroviruses 2002; 18: 685-93
    • (2002) AIDS Res Hum Retroviruses , vol.18 , pp. 685-693
    • Kilby, J.M.1    Lalezari, J.P.2    Eron, J.J.3
  • 159
    • 0036335809 scopus 로고    scopus 로고
    • Pharmacokinetics of plasma enfuvirtide after subcutaneous administration to patients with human immunodeficiency virus: Inverse Gaussian density absorption and 2-compartment disposition
    • Zhang X, Nieforth K, Lang JM, et al. Pharmacokinetics of plasma enfuvirtide after subcutaneous administration to patients with human immunodeficiency virus: inverse Gaussian density absorption and 2-compartment disposition. Clin Pharmacol Ther 2002; 72: 10-9
    • (2002) Clin Pharmacol Ther , vol.72 , pp. 10-19
    • Zhang, X.1    Nieforth, K.2    Lang, J.M.3
  • 160
    • 0037471311 scopus 로고    scopus 로고
    • A phase II clinical study of the long-term safety and antiviral activity of enfuvirtide-based antiretroviral therapy
    • Lalezari JP, Eron JJ, Carlson M, et al. A phase II clinical study of the long-term safety and antiviral activity of enfuvirtide-based antiretroviral therapy. AIDS 2003; 17: 691-8
    • (2003) AIDS , vol.17 , pp. 691-698
    • Lalezari, J.P.1    Eron, J.J.2    Carlson, M.3
  • 161
    • 0042885473 scopus 로고    scopus 로고
    • Influence of subcutaneous injection site on the steady-state pharmacokinetics of enfuvirtide (T-20) in HIV-1-infected patients
    • Lalezari JP, Patel IH, Zhang X, et al. Influence of subcutaneous injection site on the steady-state pharmacokinetics of enfuvirtide (T-20) in HIV-1-infected patients. J Clin Virol 2003; 28: 217-22
    • (2003) J Clin Virol , vol.28 , pp. 217-222
    • Lalezari, J.P.1    Patel, I.H.2    Zhang, X.3
  • 162
    • 13244286223 scopus 로고    scopus 로고
    • Pharmacokinetics of enfuvirtide in pediatric human immunodeficiency virus 1-infected patients receiving combination therapy
    • Bellibas SE, Siddique Z, Dorr A, et al. Pharmacokinetics of enfuvirtide in pediatric human immunodeficiency virus 1-infected patients receiving combination therapy. Pediatr Infect Dis J 2004; 23: 1137-41
    • (2004) Pediatr Infect Dis J , vol.23 , pp. 1137-1141
    • Bellibas, S.E.1    Siddique, Z.2    Dorr, A.3
  • 163
    • 2942642589 scopus 로고    scopus 로고
    • Lack of interaction between enfuvirtide and ritonavir or ritonavir-boosted saquinavir in HIV-1-infected patients
    • Ruxrungtham K, Boyd M, Bellibas SE, et al. Lack of interaction between enfuvirtide and ritonavir or ritonavir-boosted saquinavir in HIV-1-infected patients. J Clin Pharmacol 2004; 44: 793-803
    • (2004) J Clin Pharmacol , vol.44 , pp. 793-803
    • Ruxrungtham, K.1    Boyd, M.2    Bellibas, S.E.3
  • 164
    • 0242469076 scopus 로고    scopus 로고
    • Lack of enzyme-inducing effect of rifampicin on the pharmacokinetics of enfuvirtide
    • Boyd MA, Zhang X, Dorr A, et al. Lack of enzyme-inducing effect of rifampicin on the pharmacokinetics of enfuvirtide. J Clin Pharmacol 2003; 43: 1382-91
    • (2003) J Clin Pharmacol , vol.43 , pp. 1382-1391
    • Boyd, M.A.1    Zhang, X.2    Dorr, A.3
  • 165
    • 2942594069 scopus 로고    scopus 로고
    • Assessment of drug-drug interaction potential of enfuvirtide in human immunodeficiency virus type 1-infected patients
    • Zhang X, Lalezari JP, Badley AD, et al. Assessment of drug-drug interaction potential of enfuvirtide in human immunodeficiency virus type 1-infected patients. Clin Pharmacol Ther 2004; 75: 558-68
    • (2004) Clin Pharmacol Ther , vol.75 , pp. 558-568
    • Zhang, X.1    Lalezari, J.P.2    Badley, A.D.3
  • 166
    • 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, 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
  • 167
    • 0038576281 scopus 로고    scopus 로고
    • Enfuvirtide, an HIV-1 fusion inhibitor, for drug-resistant HIV infection in North and South America
    • Lalezari JP, Henry K, O'Hearn M, et al. Enfuvirtide, an HIV-1 fusion inhibitor, for drug-resistant HIV infection in North and South America. N Engl J Med 2003; 348: 2175-85
    • (2003) N Engl J Med , vol.348 , pp. 2175-2185
    • Lalezari, J.P.1    Henry, K.2    O'Hearn, M.3
  • 168
    • 0037849954 scopus 로고    scopus 로고
    • Efficacy of enfuvirtide in patients infected with drug-resistant HIV-1 in Europe and Australia
    • Lazzarin A, Clotet B, Cooper D, et al. Efficacy of enfuvirtide in
    • (2003) N Engl J Med , vol.348 , pp. 2186-2195
    • Lazzarin, A.1    Clotet, B.2    Cooper, D.3
  • 169
    • 11844275297 scopus 로고    scopus 로고
    • The introduction of fusion inhibitors in the HAART-regimens
    • Hasson H, Castagna A, Clementi M, et al. The introduction of fusion inhibitors in the HAART-regimens. New Microbiol 2004; 27 Suppl. 1: 11-6
    • (2004) New Microbiol , vol.27 , Issue.SUPPL. , pp. 11-16
    • Hasson, H.1    Castagna, A.2    Clementi, M.3
  • 170
    • 17144417071 scopus 로고    scopus 로고
    • TORO: 96 Week virological and immunological response and safety evaluation of enfuvirtide with an optimized background regimen
    • Jul 11-16; Bangkok
    • Arasteh K, Lazzarin A, Clotet B, et al. TORO: 96 week virological and immunological response and safety evaluation of enfuvirtide with an optimized background regimen [abstract no. B1058 (oral)]. 15th International AIDS Conference (IAC); 2004 Jul 11-16; Bangkok
    • (2004) 15th International AIDS Conference (IAC)
    • Arasteh, K.1    Lazzarin, A.2    Clotet, B.3
  • 172
    • 4043094071 scopus 로고    scopus 로고
    • Long term tolerability and safety of enfuvirtide for human immunodeficiency virus 1-infected children
    • Church JA, Hughes M, Chen J, et al. Long term tolerability and safety of enfuvirtide for human immunodeficiency virus 1-infected children. Pediatr Infect Dis J 2004; 23: 713-8
    • (2004) Pediatr Infect Dis J , vol.23 , pp. 713-718
    • Church, J.A.1    Hughes, M.2    Chen, J.3
  • 173
    • 1842502994 scopus 로고    scopus 로고
    • Enfuvirtide: A fusion inhibitor for the treatment of HIV infection
    • Fung HB, Guo Y. Enfuvirtide: a fusion inhibitor for the treatment of HIV infection. Clin Ther 2004; 26: 352-78
    • (2004) Clin Ther , vol.26 , pp. 352-378
    • Fung, H.B.1    Guo, Y.2
  • 174
    • 1142310723 scopus 로고    scopus 로고
    • Enfuvirtide, a new fusion inhibitor for therapy of human immunodeficiency virus infection
    • Hardy H, Skolnik PR. Enfuvirtide, a new fusion inhibitor for therapy of human immunodeficiency virus infection. Pharmacotherapy 2004; 24: 198-211
    • (2004) Pharmacotherapy , vol.24 , pp. 198-211
    • Hardy, H.1    Skolnik, P.R.2
  • 175
    • 3042606321 scopus 로고    scopus 로고
    • Peptide inhibitors of virus-cell fusion: Enfuvirtide as a case study in clinical discovery and development
    • Cooper DA, Lange JM. Peptide inhibitors of virus-cell fusion: enfuvirtide as a case study in clinical discovery and development. Lancet Infect Dis 2004; 4: 426-36
    • (2004) Lancet Infect Dis , vol.4 , pp. 426-436
    • Cooper, D.A.1    Lange, J.M.2
  • 177
    • 0142186214 scopus 로고    scopus 로고
    • Patient acceptance of self-injected enfuvirtide at 8 and 24 weeks
    • Cohen C, Hellinger J, Johnson M, et al. Patient acceptance of self-injected enfuvirtide at 8 and 24 weeks. HIV Clin Trials 2003; 4: 347-57
    • (2003) HIV Clin Trials , vol.4 , pp. 347-357
    • Cohen, C.1    Hellinger, J.2    Johnson, M.3
  • 178
    • 4444234979 scopus 로고    scopus 로고
    • Health-related quality of life with Enfuvirtide (ENF; T-20) in combination with an optimized background regimen
    • Cohen CJ, Clumeck N, Molina JM, et al. Health-related quality of life with Enfuvirtide (ENF; T-20) in combination with an optimized background regimen. J Acquir Immune Defic Syndr 2004; 37: 1140-6
    • (2004) J Acquir Immune Defic Syndr , vol.37 , pp. 1140-1146
    • Cohen, C.J.1    Clumeck, N.2    Molina, J.M.3
  • 179
    • 9144264190 scopus 로고    scopus 로고
    • Enfuvirtide (T-20) cross-reactive glycoprotein 41 antibody does not impair the efficacy or safety of enfuvirtide
    • Walmsley S, Henry K, Katlama C, et al. Enfuvirtide (T-20) cross-reactive glycoprotein 41 antibody does not impair the efficacy or safety of enfuvirtide. J Infect Dis 2003; 188: 1827-33
    • (2003) J Infect Dis , vol.188 , pp. 1827-1833
    • Walmsley, S.1    Henry, K.2    Katlama, C.3
  • 180
    • 17144406247 scopus 로고    scopus 로고
    • Increase in serum IgE levels during enfuvirtide treatment in multidrug-resistant HIV-1 infected patients
    • Jul 11-16; Bangkok
    • Hasson H, Danise A, Carini E, et al. Increase in serum IgE levels during enfuvirtide treatment in multidrug-resistant HIV-1 infected patients [abstract no. B4560]. 15th International AIDS Conference (IAC); 2004 Jul 11-16; Bangkok
    • (2004) 15th International AIDS Conference (IAC)
    • Hasson, H.1    Danise, A.2    Carini, E.3
  • 181
    • 4143148495 scopus 로고    scopus 로고
    • Immunological and virological study of enfuvirtide-treated HIV-positive patients
    • Barretina J, Blanco J, Bonjoch A, et al. Immunological and virological study of enfuvirtide-treated HIV-positive patients. AIDS 2004; 18: 1673-82
    • (2004) AIDS , vol.18 , pp. 1673-1682
    • Barretina, J.1    Blanco, J.2    Bonjoch, A.3
  • 182
    • 0031883832 scopus 로고    scopus 로고
    • Determinants of human immunodeficiency virus type 1 resistance to gp41-derived inhibitory peptides
    • Rimsky LT, Shugars DC, Matthews TJ. Determinants of human immunodeficiency virus type 1 resistance to gp41-derived inhibitory peptides. J Virol 1998; 72: 986-93
    • (1998) J Virol , vol.72 , pp. 986-993
    • Rimsky, L.T.1    Shugars, D.C.2    Matthews, T.J.3
  • 183
    • 0035805185 scopus 로고    scopus 로고
    • Primary genotypic resistance of HIV-1 to the fusion inhibitor T-20 in long-term infected patients
    • Zollner B, Feucht HH, Schroter M, et al. Primary genotypic resistance of HIV-1 to the fusion inhibitor T-20 in long-term infected patients. AIDS 2001; 15: 935-6
    • (2001) AIDS , vol.15 , pp. 935-936
    • Zollner, B.1    Feucht, H.H.2    Schroter, M.3
  • 184
    • 0038078724 scopus 로고    scopus 로고
    • Uncommon mutations at residue positions critical for enfuvirtide (T-20) resistance in enfuvirtide-naive patients infected with subtype B and non-B HIV-1 strains
    • Roman F, Gonzales D, Lambert C, et al. Uncommon mutations at residue positions critical for enfuvirtide (T-20) resistance in enfuvirtide-naive patients infected with subtype B and non-B HIV-1 strains. J Acquir Immune Defic Syndr 2003; 33: 134-9
    • (2003) J Acquir Immune Defic Syndr , vol.33 , pp. 134-139
    • Roman, F.1    Gonzales, D.2    Lambert, C.3
  • 185
    • 0036090585 scopus 로고    scopus 로고
    • Emergence of resistant human immunodeficiency virus type 1 in patients receiving fusion inhibitor (T-20) monotherapy
    • Wei X, Decker JM, Liu H, et al. Emergence of resistant human immunodeficiency virus type 1 in patients receiving fusion inhibitor (T-20) monotherapy. Antimicrob Agents Chemother 2002; 46: 1896-905
    • (2002) Antimicrob Agents Chemother , vol.46 , pp. 1896-1905
    • Wei, X.1    Decker, J.M.2    Liu, H.3
  • 186
    • 4444310448 scopus 로고    scopus 로고
    • Characterization of determinants of genotypic and phenotypic resistance to enfuvirtide in baseline and on-treatment HIV-1 isolates
    • Sista PR, Melby T, Davison D, et al. Characterization of determinants of genotypic and phenotypic resistance to enfuvirtide in baseline and on-treatment HIV-1 isolates. AIDS 2004; 18: 1787-94
    • (2004) AIDS , vol.18 , pp. 1787-1794
    • Sista, P.R.1    Melby, T.2    Davison, D.3
  • 187
    • 3342981347 scopus 로고    scopus 로고
    • Evolution of genotypic and phenotypic resistance to enfuvirtide in HIV-infected patients experiencing prolonged virologic failure
    • Poveda E, Rodes B, Labernardiere JL, et al. Evolution of genotypic and phenotypic resistance to enfuvirtide in HIV-infected patients experiencing prolonged virologic failure. J Med Virol 2004; 74: 21-8
    • (2004) J Med Virol , vol.74 , pp. 21-28
    • Poveda, E.1    Rodes, B.2    Labernardiere, J.L.3
  • 188
    • 4444375658 scopus 로고    scopus 로고
    • Resistance to enfuvirtide, the first HIV fusion inhibitor
    • Greenberg ML, Cammack N. Resistance to enfuvirtide, the first HIV fusion inhibitor. J Antimicrob Chemother 2004; 54: 333-40
    • (2004) J Antimicrob Chemother , vol.54 , pp. 333-340
    • Greenberg, M.L.1    Cammack, N.2
  • 189
    • 3042687460 scopus 로고    scopus 로고
    • Characterization of genotypic determinants in HR-1 and HR-2 gp41 domains in individuals with persistent HIV viraemia under T-20
    • Marcelin AG, Reynes J, Yerly S, et al. Characterization of genotypic determinants in HR-1 and HR-2 gp41 domains in individuals with persistent HIV viraemia under T-20. AIDS 2004; 18: 1340-2
    • (2004) AIDS , vol.18 , pp. 1340-1342
    • Marcelin, A.G.1    Reynes, J.2    Yerly, S.3
  • 190
    • 3142779320 scopus 로고    scopus 로고
    • Determinants of human immunodeficiency virus type 1 baseline susceptibility to the fusion inhibitors enfuvirtide and T-649 reside outside the peptide interaction site
    • Heil ML, Decker JM, Sfakianos JN, et al. Determinants of human immunodeficiency virus type 1 baseline susceptibility to the fusion inhibitors enfuvirtide and T-649 reside outside the peptide interaction site. J Virol 2004; 78: 7582-9
    • (2004) J Virol , vol.78 , pp. 7582-7589
    • Heil, M.L.1    Decker, J.M.2    Sfakianos, J.N.3
  • 191
    • 4344685387 scopus 로고    scopus 로고
    • Genotype and phenotype patterns of human immunodeficiency virus type 1 resistance to enfuvirtide during long-term treatment
    • Menzo S, Castagna A, Monachetti A, et al. Genotype and phenotype patterns of human immunodeficiency virus type 1 resistance to enfuvirtide during long-term treatment. Antimicrob Agents Chemother 2004; 48: 3253-9
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 3253-3259
    • Menzo, S.1    Castagna, A.2    Monachetti, A.3
  • 192
    • 3042799046 scopus 로고    scopus 로고
    • Relative replicative fitness of human immunodeficiency virus type 1 mutants resistant to enfuvirtide (T-20)
    • Lu J, Sista P, Giguel F, et al. Relative replicative fitness of human immunodeficiency virus type 1 mutants resistant to enfuvirtide (T-20). J Virol 2004; 78: 4628-37
    • (2004) J Virol , vol.78 , pp. 4628-4637
    • Lu, J.1    Sista, P.2    Giguel, F.3
  • 193
    • 4344613594 scopus 로고    scopus 로고
    • Susceptibility of HIV type 1 to the fusion inhibitor T-20 is reduced on insertion of host intercellular adhesion molecule 1 in the virus membrane
    • Beausejour Y, Tremblay MJ. Susceptibility of HIV type 1 to the fusion inhibitor T-20 is reduced on insertion of host intercellular adhesion molecule 1 in the virus membrane. J Infect Dis 2004; 190: 894-902
    • (2004) J Infect Dis , vol.190 , pp. 894-902
    • Beausejour, Y.1    Tremblay, M.J.2
  • 194
    • 2942596050 scopus 로고    scopus 로고
    • Clinical management of treatment-experienced, HIV-infected patients with the fusion inhibitor enfuvirtide: Consensus recommendations
    • Clotet B, Raffi F, Cooper D, et al. Clinical management of treatment-experienced, HIV-infected patients with the fusion inhibitor enfuvirtide: consensus recommendations. AIDS 2004; 18: 1137-46
    • (2004) AIDS , vol.18 , pp. 1137-1146
    • Clotet, B.1    Raffi, F.2    Cooper, D.3
  • 195
    • 12144290487 scopus 로고    scopus 로고
    • Short-term safety and antiretroviral activity of T-1249, a second-generation fusion inhibitor of HIV
    • Eron JJ, Gulick RM, Bartlett JA, et al. Short-term safety and antiretroviral activity of T-1249, a second-generation fusion inhibitor of HIV. J Infect Dis 2004; 189: 1075-83
    • (2004) J Infect Dis , vol.189 , pp. 1075-1083
    • Eron, J.J.1    Gulick, R.M.2    Bartlett, J.A.3
  • 196
    • 20144386372 scopus 로고    scopus 로고
    • T-1249 retains potent antiretroviral activity in patients who had experienced virological failure while on an enfuvirtide-containing treatment regimen
    • Lalezari JP, Bellos NC, Sathasivan K, et al. T-1249 retains potent antiretroviral activity in patients who had experienced virological failure while on an enfuvirtide-containing treatment regimen. J Infect Dis 2005; 191: 1153-63
    • (2005) J Infect Dis , vol.191 , pp. 1153-1163
    • Lalezari, J.P.1    Bellos, N.C.2    Sathasivan, K.3
  • 197
    • 2342550183 scopus 로고    scopus 로고
    • Discontinuation of the clinical development of fusion inhibitor T-1249
    • Martin-Carbonero L. Discontinuation of the clinical development of fusion inhibitor T-1249. AIDS Rev 2004; 6: 61
    • (2004) AIDS Rev , vol.6 , pp. 61
    • Martin-Carbonero, L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.