메뉴 건너뛰기




Volumn 2, Issue 5, 2010, Pages 1069-1105

HIV-1 entry, inhibitors, and resistance

Author keywords

CCR5; Envelope; Gp120; Gp41; HIV 1; Maraviroc; V3 loop; Vicriviroc

Indexed keywords

4 [(4 BROMOPHENYL)(ETHOXYIMINO)METHYL] 1' [(2,4 DIMETHYL 3 PYRIDINYL)CARBONYL] 4' METHYL 1,4' BIPIPERIDINE; 4 [1 [(2,4 DIMETHYL 3 PYRIDINYL)CARBONYL] 4 METHYL 4 PIPERIDINYL] 2 METHYL 1 [1 [4 (TRIFLUOROMETHYL)PHENYL]ETHYL]PIPERAZINE; 8 [4 (2 BUTOXYETHOXY)PHENYL] 1,2,3,4 TETRAHYDRO 1 ISOBUTYL N [4 (1 PROPYL 1H IMIDAZOL 5 YLMETHYLSULFINYL)PHENYL] 1 BENZAZOCINE 5 CARBOXAMIDE; ABACAVIR; AMPRENAVIR; APLAVIROC; ATAZANAVIR; DARUNAVIR; DELAVIRDINE; DIDANOSINE; EFAVIRENZ; EMTRICITABINE; ENFUVIRTIDE; ETRAVIRINE; FOSAMPRENAVIR; INDINAVIR; LAMIVUDINE; MARAVIROC; NELFINAVIR; NEVIRAPINE; RALTEGRAVIR; RITONAVIR; SAQUINAVIR; STAVUDINE; TENOFOVIR DISOPROXIL; TIPRANAVIR; UNCLASSIFIED DRUG; UNINDEXED DRUG; VICRIVIROC; VILEAD; ZALCITABINE; ZIDOVUDINE;

EID: 79952085104     PISSN: None     EISSN: 19994915     Source Type: Journal    
DOI: 10.3390/v2051069     Document Type: Review
Times cited : (56)

References (168)
  • 1
    • 0029075130 scopus 로고
    • Lower in vivo mutation rate of human immunodeficiency virus type 1 than that predicted from the fidelity of purified reverse transcriptase
    • Mansky, L.M.; Temin, H.M. Lower in vivo mutation rate of human immunodeficiency virus type 1 than that predicted from the fidelity of purified reverse transcriptase. J. Virol. 1995, 69, 5087-5094.
    • (1995) J. Virol , vol.69 , pp. 5087-5094
    • Mansky, L.M.1    Temin, H.M.2
  • 3
    • 79952091797 scopus 로고    scopus 로고
    • U.S. Food and Drug Administration, accessed December 3, 2009
    • U.S. Food and Drug Administration. Approved HIV-1 Antiretrovirals. http://www.fda.gov (accessed December 3, 2009).
    • Approved HIV-1 Antiretrovirals
  • 5
    • 0033012398 scopus 로고    scopus 로고
    • Chemokine receptors as HIV-1 coreceptors: Roles in viral entry, tropism, and disease
    • Berger, E.A.; Murphy, P.M.; Farber, J.M. 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
  • 6
    • 0023644926 scopus 로고
    • pH-independent HIV entry into CD4-positive T cells via virus envelope fusion to the plasma membrane
    • Stein, B.S.; Gowda, S.D.; Lifson, J.D.; Penhallow, R.C.; Bensch, K.G.; Engleman, E.G. pH-independent HIV entry into CD4-positive T cells via virus envelope fusion to the plasma membrane. Cell 1987, 49, 659-668.
    • (1987) Cell , vol.49 , pp. 659-668
    • Stein, B.S.1    Gowda, S.D.2    Lifson, J.D.3    Penhallow, R.C.4    Bensch, K.G.5    Engleman, E.G.6
  • 7
    • 65249139458 scopus 로고    scopus 로고
    • HIV enters cells via endocytosis and dynamin-dependent fusion with endosomes
    • Miyauchi, K.; Kim, Y.; Latinovic, O.; Morozov, V.; Melikyan, G.B. HIV enters cells via endocytosis and dynamin-dependent fusion with endosomes. Cell 2009, 137, 433-444.
    • (2009) Cell , vol.137 , pp. 433-444
    • Miyauchi, K.1    Kim, Y.2    Latinovic, O.3    Morozov, V.4    Melikyan, G.B.5
  • 8
    • 13744252968 scopus 로고    scopus 로고
    • Involvement of clathrin-mediated endocytosis in human immunodeficiency virus type 1 entry
    • Daecke, J.; Fackler, O.T.; Dittmar, M.T.; Krausslich, H.G. Involvement of clathrin-mediated endocytosis in human immunodeficiency virus type 1 entry. J. Virol. 2005, 79, 1581-1594.
    • (2005) J. Virol , vol.79 , pp. 1581-1594
    • Daecke, J.1    Fackler, O.T.2    Dittmar, M.T.3    Krausslich, H.G.4
  • 9
    • 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, 1884-1888.
    • (1998) Science , vol.280 , pp. 1884-1888
    • Wyatt, R.1    Sodroski, J.2
  • 10
    • 0027157736 scopus 로고
    • Folding and assembly of viral membrane proteins
    • Doms, R.W.; Lamb, R.A.; Rose, J.K.; Helenius, A. Folding and assembly of viral membrane proteins. Virology 1993, 193, 545-562.
    • (1993) Virology , vol.193 , pp. 545-562
    • Doms, R.W.1    Lamb, R.A.2    Rose, J.K.3    Helenius, A.4
  • 11
    • 0026029621 scopus 로고
    • Folding, interaction with GRP78-BiP, assembly, and transport of the human immunodeficiency virus type 1 envelope protein
    • Earl, P.L.; Moss, B.; Doms, R.W. Folding, interaction with GRP78-BiP, assembly, and transport of the human immunodeficiency virus type 1 envelope protein. J. Virol. 1991, 65, 2047-2055.
    • (1991) J. Virol , vol.65 , pp. 2047-2055
    • Earl, P.L.1    Moss, B.2    Doms, R.W.3
  • 12
    • 0034634728 scopus 로고    scopus 로고
    • Maturation of HIV envelope glycoprotein precursors by cellular endoproteases
    • Moulard, M.; Decroly, E. Maturation of HIV envelope glycoprotein precursors by cellular endoproteases. Biochim. Biophys. Acta 2000, 1469, 121-132.
    • (2000) Biochim. Biophys. Acta , vol.1469 , pp. 121-132
    • Moulard, M.1    Decroly, E.2
  • 13
    • 0037381269 scopus 로고    scopus 로고
    • The structural biology of type I viral membrane fusion
    • Colman, P.M.; Lawrence, M.C. The structural biology of type I viral membrane fusion. Nat. Rev. Mol. Cell Biol. 2003, 4, 309-319.
    • (2003) Nat. Rev. Mol. Cell Biol , vol.4 , pp. 309-319
    • Colman, P.M.1    Lawrence, M.C.2
  • 14
    • 0022978934 scopus 로고
    • Binding of the human retrovirus HTLV-III/LAV/ARV/HIV to the CD4 (T4) molecule: Conformation dependence, epitope mapping, antibody inhibition, and potential for idiotypic mimicry
    • McDougal, J.S.; Nicholson, J.K.; Cross, G.D.; Cort, S.P.; Kennedy, M.S.; Mawle, A.C. Binding of the human retrovirus HTLV-III/LAV/ARV/HIV to the CD4 (T4) molecule: conformation dependence, epitope mapping, antibody inhibition, and potential for idiotypic mimicry. J. Immunol. 1986, 137, 2937-2944.
    • (1986) J. Immunol , vol.137 , pp. 2937-2944
    • McDougal, J.S.1    Nicholson, J.K.2    Cross, G.D.3    Cort, S.P.4    Kennedy, M.S.5    Mawle, A.C.6
  • 16
    • 0030986787 scopus 로고    scopus 로고
    • HIV-1-induced cell fusion is mediated by multiple regions within both the viral envelope and the CCR-5 co-receptor
    • Bieniasz, P.D.; Fridell, R.A.; Aramori, I.; Ferguson, S.S.; Caron, M.G.; Cullen, B.R. HIV-1-induced cell fusion is mediated by multiple regions within both the viral envelope and the CCR-5 co-receptor. EMBO J. 1997, 16, 2599-2609.
    • (1997) EMBO J , vol.16 , pp. 2599-2609
    • Bieniasz, P.D.1    Fridell, R.A.2    Aramori, I.3    Ferguson, S.S.4    Caron, M.G.5    Cullen, B.R.6
  • 17
    • 0032543307 scopus 로고    scopus 로고
    • Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
    • Kwong, P.D.; Wyatt, R.; Robinson, J.; Sweet, R.W.; Sodroski, J.; Hendrickson, W.A. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 1998, 393, 648-659.
    • (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
  • 18
    • 0034690683 scopus 로고    scopus 로고
    • Fine definition of a conserved CCR5-binding region on the human immunodeficiency virus type 1 glycoprotein 120
    • Rizzuto, C.; Sodroski, J. Fine definition of a conserved CCR5-binding region on the human immunodeficiency virus type 1 glycoprotein 120. AIDS Res. Hum. Retroviruses 2000, 16, 741-749.
    • (2000) AIDS Res. Hum. Retroviruses , vol.16 , pp. 741-749
    • Rizzuto, C.1    Sodroski, J.2
  • 19
    • 0025866185 scopus 로고
    • Conformational changes induced in the human immunodeficiency virus envelope glycoprotein by soluble CD4 binding
    • Sattentau, Q.J.; Moore, J.P. Conformational changes induced in the human immunodeficiency virus envelope glycoprotein by soluble CD4 binding. J. Exp. Med. 1991, 174, 407-415.
    • (1991) J. Exp. Med , vol.174 , pp. 407-415
    • Sattentau, Q.J.1    Moore, J.P.2
  • 21
    • 0023669119 scopus 로고
    • Detection of a fusion peptide sequence in the transmembrane protein of human immunodeficiency virus
    • Gallaher, W.R. Detection of a fusion peptide sequence in the transmembrane protein of human immunodeficiency virus. Cell 1987, 50, 327-328.
    • (1987) Cell , vol.50 , pp. 327-328
    • Gallaher, W.R.1
  • 22
    • 0024564217 scopus 로고
    • Hydrophobic binding of the ectodomain of influenza hemagglutinin to membranes occurs through the fusion peptide
    • Harter, C.; James, P.; Bachi, T.; Semenza, G.; Brunner, J. Hydrophobic binding of the ectodomain of influenza hemagglutinin to membranes occurs through the fusion peptide. J. Biol. Chem. 1989, 264, 6459-6464.
    • (1989) J. Biol. Chem , vol.264 , pp. 6459-6464
    • Harter, C.1    James, P.2    Bachi, T.3    Semenza, G.4    Brunner, J.5
  • 23
    • 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, G.B.; Markosyan, R.M.; Hemmati, H.; Delmedico, M.K.; Lambert, D.M.; Cohen, F.S. 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, 413-423.
    • (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
  • 25
    • 0029878665 scopus 로고    scopus 로고
    • The ectodomain of HIV-1 env subunit gp41 forms a soluble, alpha-helical, rod-like oligomer in the absence of gp120 and the N-terminal fusion peptide
    • Weissenhorn, W.; Wharton, S.A.; Calder, L.J.; Earl, P.L.; Moss, B.; Aliprandis, E.; Skehel, J.J.; Wiley, D.C. The ectodomain of HIV-1 env subunit gp41 forms a soluble, alpha-helical, rod-like oligomer in the absence of gp120 and the N-terminal fusion peptide. EMBO J. 1996, 15, 1507-1514.
    • (1996) EMBO J , vol.15 , pp. 1507-1514
    • Weissenhorn, W.1    Wharton, S.A.2    Calder, L.J.3    Earl, P.L.4    Moss, B.5    Aliprandis, E.6    Skehel, J.J.7    Wiley, D.C.8
  • 26
    • 0025678671 scopus 로고
    • Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins
    • Chambers, P.; Pringle, C.R.; Easton, A.J. Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins. J. Gen. Virol. 1990, 71, 3075-3080.
    • (1990) J. Gen. Virol , vol.71 , pp. 3075-3080
    • Chambers, P.1    Pringle, C.R.2    Easton, A.J.3
  • 27
    • 0025010813 scopus 로고
    • Retroviral envelope glycoproteins contain a leucine zipper-like repeat
    • Delwart, E.L.; Mosialos, G.; Gilmore, T. Retroviral envelope glycoproteins contain a leucine zipper-like repeat. AIDS Res. Hum. Retroviruses 1990, 6, 703-706.
    • (1990) AIDS Res. Hum. Retroviruses , vol.6 , pp. 703-706
    • Delwart, E.L.1    Mosialos, G.2    Gilmore, T.3
  • 29
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan, D.C.; Fass, D.; Berger, J.M.; Kim, P.S. Core structure of gp41 from the HIV envelope glycoprotein. Cell 1997, 89, 263-273.
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 31
    • 0023580063 scopus 로고
    • Blocking of HIV-1 infectivity by a soluble, secreted form of the CD4 antigen
    • Smith, D.H.; Byrn, R.A.; Marsters, S.A.; Gregory, T.; Groopman, J.E.; Capon, D.J. Blocking of HIV-1 infectivity by a soluble, secreted form of the CD4 antigen. Science 1987, 238, 1704-1707.
    • (1987) Science , vol.238 , pp. 1704-1707
    • Smith, D.H.1    Byrn, R.A.2    Marsters, S.A.3    Gregory, T.4    Groopman, J.E.5    Capon, D.J.6
  • 33
    • 0023867450 scopus 로고
    • Soluble CD4 molecules neutralize human immunodeficiency virus type 1
    • Traunecker, A.; Luke, W.; Karjalainen, K. Soluble CD4 molecules neutralize human immunodeficiency virus type 1. Nature 1988, 331, 84-86.
    • (1988) Nature , vol.331 , pp. 84-86
    • Traunecker, A.1    Luke, W.2    Karjalainen, K.3
  • 36
    • 0024561088 scopus 로고
    • Effect of recombinant soluble CD4 in rhesus monkeys infected with simian immunodeficiency virus of macaques
    • Watanabe, M.; Reimann, K.A.; DeLong, P.A.; Liu, T.; Fisher, R.A.; Letvin, N.L. Effect of recombinant soluble CD4 in rhesus monkeys infected with simian immunodeficiency virus of macaques. Nature 1989, 337, 267-270.
    • (1989) Nature , vol.337 , pp. 267-270
    • Watanabe, M.1    Reimann, K.A.2    Delong, P.A.3    Liu, T.4    Fisher, R.A.5    Letvin, N.L.6
  • 37
    • 0025093595 scopus 로고
    • Recombinant soluble CD4 therapy in patients with the acquired immunodeficiency syndrome (AIDS) and AIDS-related complex. A phase I-II escalating dosage trial
    • Schooley, R.T.; Merigan, T.C.; Gaut, P.; Hirsch, M.S.; Holodniy, M.; Flynn, T.; Liu, S.; Byington, R.E.; Henochowicz, S.; Gubish, E. Recombinant soluble CD4 therapy in patients with the acquired immunodeficiency syndrome (AIDS) and AIDS-related complex. A phase I-II escalating dosage trial. Ann. Intern. Med. 1990, 112, 247-253.
    • (1990) Ann. Intern. Med , vol.112 , pp. 247-253
    • Schooley, R.T.1    Merigan, T.C.2    Gaut, P.3    Hirsch, M.S.4    Holodniy, M.5    Flynn, T.6    Liu, S.7    Byington, R.E.8    Henochowicz, S.9    Gubish, E.10
  • 38
    • 0024549563 scopus 로고
    • Highly efficient neutralization of HIV with recombinant CD4-immunoglobulin molecules
    • Traunecker, A.; Schneider, J.; Kiefer, H.; Karjalainen, K. Highly efficient neutralization of HIV with recombinant CD4-immunoglobulin molecules. Nature 1989, 339, 68-70.
    • (1989) Nature , vol.339 , pp. 68-70
    • Traunecker, A.1    Schneider, J.2    Kiefer, H.3    Karjalainen, K.4
  • 39
    • 0025016076 scopus 로고
    • High concentrations of recombinant soluble CD4 are required to neutralize primary human immunodeficiency virus type 1 isolates
    • Daar, E.S.; Li, X.L.; Moudgil, T.; Ho, D.D. High concentrations of recombinant soluble CD4 are required to neutralize primary human immunodeficiency virus type 1 isolates. Proc. Natl. Acad. Sci. U.S.A 1990, 87, 6574-6578.
    • (1990) Proc. Natl. Acad. Sci. U.S.A , vol.87 , pp. 6574-6578
    • Daar, E.S.1    Li, X.L.2    Moudgil, T.3    Ho, D.D.4
  • 43
    • 0025351001 scopus 로고
    • CD8+ T cells inhibit HIV replication in naturally infected CD4+ T cells. Evidence for a soluble inhibitor
    • Brinchmann, J.E.; Gaudernack, G.; Vartdal, F. CD8+ T cells inhibit HIV replication in naturally infected CD4+ T cells. Evidence for a soluble inhibitor. J. Immunol. 1990, 144, 2961-2966.
    • (1990) J. Immunol , vol.144 , pp. 2961-2966
    • Brinchmann, J.E.1    Gaudernack, G.2    Vartdal, F.3
  • 44
    • 0029417004 scopus 로고
    • Identification of RANTES, MIP-1 alpha, and MIP-1 beta as the major HIV-suppressive factors produced by CD8+ T cells
    • Cocchi, F.; DeVico, A.L.; Garzino-Demo, A.; Arya, S.K.; Gallo, R.C.; Lusso, P. Identification of RANTES, MIP-1 alpha, and MIP-1 beta as the major HIV-suppressive factors produced by CD8+ T cells. Science 1995, 270, 1811-1815.
    • (1995) Science , vol.270 , pp. 1811-1815
    • Cocchi, F.1    Devico, A.L.2    Garzino-Demo, A.3    Arya, S.K.4    Gallo, R.C.5    Lusso, P.6
  • 46
    • 0030002637 scopus 로고    scopus 로고
    • HIV-1 entry cofactor: Functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor
    • Feng, Y.; Broder, C.C.; Kennedy, P.E.; Berger, E.A. HIV-1 entry cofactor: functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor. Science 1996, 272, 872-877.
    • (1996) Science , vol.272 , pp. 872-877
    • Feng, Y.1    Broder, C.C.2    Kennedy, P.E.3    Berger, E.A.4
  • 48
  • 49
    • 0030018156 scopus 로고    scopus 로고
    • CC CKR5: A RANTES, MIP-1alpha, MIP-1beta receptor as a fusion cofactor for macrophage-tropic HIV-1
    • Alkhatib, G.; Combadiere, C.; Broder, C.C.; Feng, Y.; Kennedy, P.E.; Murphy, P.M.; Berger, E.A. CC CKR5: a RANTES, MIP-1alpha, MIP-1beta receptor as a fusion cofactor for macrophage-tropic HIV-1. Science 1996, 272, 1955-1958.
    • (1996) Science , vol.272 , pp. 1955-1958
    • Alkhatib, G.1    Combadiere, C.2    Broder, C.C.3    Feng, Y.4    Kennedy, P.E.5    Murphy, P.M.6    Berger, E.A.7
  • 53
    • 1842331564 scopus 로고    scopus 로고
    • Envelope glycoproteins from human immunodeficiency virus types 1 and 2 and simian immunodeficiency virus can use human CCR5 as a coreceptor for viral entry and make direct CD4-dependent interactions with this chemokine receptor
    • Hill, C.M.; Deng, H.; Unutmaz, D.; Kewalramani, V.N.; Bastiani, L.; Gorny, M.K.; Zolla-Pazner, S.; Littman, D.R. Envelope glycoproteins from human immunodeficiency virus types 1 and 2 and simian immunodeficiency virus can use human CCR5 as a coreceptor for viral entry and make direct CD4-dependent interactions with this chemokine receptor. J. Virol. 1997, 71, 6296-6304.
    • (1997) J. Virol , vol.71 , pp. 6296-6304
    • Hill, C.M.1    Deng, H.2    Unutmaz, D.3    Kewalramani, V.N.4    Bastiani, L.5    Gorny, M.K.6    Zolla-Pazner, S.7    Littman, D.R.8
  • 54
    • 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, B.J.; Rucker, J.; Yi, Y.; Smyth, R.J.; Samson, M.; Peiper, S.C.; Parmentier, M.; Collman, R.G.; Doms, R.W. 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, 1149-1158.
    • (1996) Cell , vol.85 , pp. 1149-1158
    • Doranz, B.J.1    Rucker, J.2    Yi, Y.3    Smyth, R.J.4    Samson, M.5    Peiper, S.C.6    Parmentier, M.7    Collman, R.G.8    Doms, R.W.9
  • 58
    • 0031008794 scopus 로고    scopus 로고
    • STRL33, A novel chemokine receptor-like protein, functions as a fusion cofactor for both macrophage-tropic and T cell line-tropic HIV-1
    • Liao, F.; Alkhatib, G.; Peden, K.W.; Sharma, G.; Berger, E.A.; Farber, J.M. STRL33, A novel chemokine receptor-like protein, functions as a fusion cofactor for both macrophage-tropic and T cell line-tropic HIV-1. J. Exp. Med. 1997, 185, 2015-2023.
    • (1997) J. Exp. Med , vol.185 , pp. 2015-2023
    • Liao, F.1    Alkhatib, G.2    Peden, K.W.3    Sharma, G.4    Berger, E.A.5    Farber, J.M.6
  • 60
    • 0031575431 scopus 로고    scopus 로고
    • Change in coreceptor use correlates with disease progression in HIV-1--infected individuals
    • Connor, R.I.; Sheridan, K.E.; Ceradini, D.; Choe, S.; Landau, N.R. Change in coreceptor use correlates with disease progression in HIV-1--infected individuals. J. Exp. Med. 1997, 185, 621-628.
    • (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
  • 61
    • 0023896246 scopus 로고
    • Differential syncytium-inducing capacity of human immunodeficiency virus isolates: Frequent detection of syncytium-inducing isolates in patients with acquired immunodeficiency syndrome (AIDS) and AIDS-related complex
    • Tersmette, M.; de Goede, R.E.; Al, B.J.; Winkel, I.N.; Gruters, R.A.; Cuypers, H.T.; Huisman, H.G.; Miedema, F. Differential syncytium-inducing capacity of human immunodeficiency virus isolates: frequent detection of syncytium-inducing isolates in patients with acquired immunodeficiency syndrome (AIDS) and AIDS-related complex. J. Virol. 1988, 62, 2026-2032.
    • (1988) J. Virol , vol.62 , pp. 2026-2032
    • Tersmette, M.1    de Goede, R.E.2    Al, B.J.3    Winkel, I.N.4    Gruters, R.A.5    Cuypers, H.T.6    Huisman, H.G.7    Miedema, F.8
  • 62
    • 0026600926 scopus 로고
    • Biological phenotype of human immunodeficiency virus type 1 clones at different stages of infection: Progression of disease is associated with a shift from monocytotropic to T-cell-tropic virus population
    • Schuitemaker, H.; Koot, M.; Kootstra, N.A.; Dercksen, M.W.; de Goede, R.E.; van Steenwijk, R.P.; Lange, J.M.; Schattenkerk, J.K.; Miedema, F.; Tersmette, M. Biological phenotype of human immunodeficiency virus type 1 clones at different stages of infection: progression of disease is associated with a shift from monocytotropic to T-cell-tropic virus population. J. Virol. 1992, 66, 1354-1360.
    • (1992) J. Virol , vol.66 , pp. 1354-1360
    • Schuitemaker, H.1    Koot, M.2    Kootstra, N.A.3    Dercksen, M.W.4    de Goede, R.E.5    van Steenwijk, R.P.6    Lange, J.M.7    Schattenkerk, J.K.8    Miedema, F.9    Tersmette, M.10
  • 63
  • 66
    • 0031041571 scopus 로고    scopus 로고
    • The role of viral phenotype and CCR-5 gene defects in HIV-1 transmission and disease progression
    • Michael, N.L.; Chang, G.; Louie, L.G.; Mascola, J.R.; Dondero, D.; Birx, D.L.; Sheppard, H.W. The role of viral phenotype and CCR-5 gene defects in HIV-1 transmission and disease progression. Nat. Med. 1997, 3, 338-340.
    • (1997) Nat. Med , vol.3 , pp. 338-340
    • Michael, N.L.1    Chang, G.2    Louie, L.G.3    Mascola, J.R.4    Dondero, D.5    Birx, D.L.6    Sheppard, H.W.7
  • 71
    • 0032511573 scopus 로고    scopus 로고
    • CCR5 promoter polymorphism and HIV-1 disease progression. Multicenter AIDS Cohort Study (MACS)
    • McDermott, D.H.; Zimmerman, P.A.; Guignard, F.; Kleeberger, C.A.; Leitman, S.F.; Murphy, P.M. CCR5 promoter polymorphism and HIV-1 disease progression. Multicenter AIDS Cohort Study (MACS). Lancet 1998, 352, 866-870.
    • (1998) Lancet , vol.352 , pp. 866-870
    • McDermott, D.H.1    Zimmerman, P.A.2    Guignard, F.3    Kleeberger, C.A.4    Leitman, S.F.5    Murphy, P.M.6
  • 72
    • 0035282641 scopus 로고    scopus 로고
    • Polymorphisms in the CCR5 promoter region influence disease progression in perinatally human immunodeficiency virus type 1-infected children
    • Ometto, L.; Bertorelle, R.; Mainardi, M.; Zanchetta, M.; Tognazzo, S.; Rampon, O.; Ruga, E.; Chieco-Bianchi, L.; De, R.A. Polymorphisms in the CCR5 promoter region influence disease progression in perinatally human immunodeficiency virus type 1-infected children. J. Infect. Dis. 2001, 183, 814-818.
    • (2001) J. Infect. Dis , vol.183 , pp. 814-818
    • Ometto, L.1    Bertorelle, R.2    Mainardi, M.3    Zanchetta, M.4    Tognazzo, S.5    Rampon, O.6    Ruga, E.7    Chieco-Bianchi, L.8    De, R.A.9
  • 76
    • 0346365289 scopus 로고    scopus 로고
    • Intrapatient alterations in the human immunodeficiency virus type 1 gp120 V1V2 and V3 regions differentially modulate coreceptor usage, virus inhibition by CC/CXC chemokines, soluble CD4, and the b12 and 2G12 monoclonal antibodies
    • Nabatov, A.A.; Pollakis, G.; Linnemann, T.; Kliphius, A.; Chalaby, M.I.; Paxton, W.A. Intrapatient alterations in the human immunodeficiency virus type 1 gp120 V1V2 and V3 regions differentially modulate coreceptor usage, virus inhibition by CC/CXC chemokines, soluble CD4, and the b12 and 2G12 monoclonal antibodies. J. Virol. 2004, 78, 524-530.
    • (2004) J. Virol , vol.78 , pp. 524-530
    • Nabatov, A.A.1    Pollakis, G.2    Linnemann, T.3    Kliphius, A.4    Chalaby, M.I.5    Paxton, W.A.6
  • 78
    • 0030920235 scopus 로고    scopus 로고
    • Multiple extracellular domains of CCR-5 contribute to human immunodeficiency virus type 1 entry and fusion
    • Picard, L.; Simmons, G.; Power, C.A.; Meyer, A.; Weiss, R.A.; Clapham, P.R. Multiple extracellular domains of CCR-5 contribute to human immunodeficiency virus type 1 entry and fusion. J. Virol. 1997, 71, 5003-5011.
    • (1997) J. Virol , vol.71 , pp. 5003-5011
    • Picard, L.1    Simmons, G.2    Power, C.A.3    Meyer, A.4    Weiss, R.A.5    Clapham, P.R.6
  • 79
    • 0036333648 scopus 로고    scopus 로고
    • The crown and stem of the V3 loop play distinct roles in human immunodeficiency virus type 1 envelope glycoprotein interactions with the CCR5 coreceptor
    • Cormier, E.G.; Dragic, T. The crown and stem of the V3 loop play distinct roles in human immunodeficiency virus type 1 envelope glycoprotein interactions with the CCR5 coreceptor. J. Virol. 2002, 76, 8953-8957.
    • (2002) J. Virol , vol.76 , pp. 8953-8957
    • Cormier, E.G.1    Dragic, T.2
  • 82
    • 0036258990 scopus 로고    scopus 로고
    • G protein-coupled receptor allosterism and complexing
    • Christopoulos, A.; Kenakin, T. G protein-coupled receptor allosterism and complexing. Pharmacol. Rev. 2002, 54, 323-374.
    • (2002) Pharmacol. Rev , vol.54 , pp. 323-374
    • Christopoulos, A.1    Kenakin, T.2
  • 86
    • 0037144581 scopus 로고    scopus 로고
    • Constitutive agonist-independent CCR5 oligomerization and antibody-mediated clustering occurring at physiological levels of receptors
    • Issafras, H.; Angers, S.; Bulenger, S.; Blanpain, C.; Parmentier, M.; Labbe-Jullie, C.; Bouvier, M.; Marullo, S. Constitutive agonist-independent CCR5 oligomerization and antibody-mediated clustering occurring at physiological levels of receptors. J. Biol. Chem. 2002, 277, 34666-34673.
    • (2002) J. Biol. Chem , vol.277 , pp. 34666-34673
    • Issafras, H.1    Angers, S.2    Bulenger, S.3    Blanpain, C.4    Parmentier, M.5    Labbe-Jullie, C.6    Bouvier, M.7    Marullo, S.8
  • 89
    • 0032483021 scopus 로고    scopus 로고
    • Crystal structure of the simian immunodeficiency virus (SIV) gp41 core: Conserved helical interactions underlie the broad inhibitory activity of gp41 peptides
    • Malashkevich, V.N.; Chan, D.C.; Chutkowski, C.T.; Kim, P.S. Crystal structure of the simian immunodeficiency virus (SIV) gp41 core: conserved helical interactions underlie the broad inhibitory activity of gp41 peptides. Proc. Natl. Acad. Sci. U.S.A 1998, 95, 9134-9139.
    • (1998) Proc. Natl. Acad. Sci. U.S.A , vol.95 , pp. 9134-9139
    • Malashkevich, V.N.1    Chan, D.C.2    Chutkowski, C.T.3    Kim, P.S.4
  • 90
    • 0032529672 scopus 로고    scopus 로고
    • A core trimer of the paramyxovirus fusion protein: Parallels to influenza virus hemagglutinin and HIV-1 gp41
    • Joshi, S.B.; Dutch, R.E.; Lamb, R.A. A core trimer of the paramyxovirus fusion protein: parallels to influenza virus hemagglutinin and HIV-1 gp41. Virology 1998, 248, 20-34.
    • (1998) Virology , vol.248 , pp. 20-34
    • Joshi, S.B.1    Dutch, R.E.2    Lamb, R.A.3
  • 91
    • 0026465468 scopus 로고
    • A synthetic peptide inhibitor of human immunodeficiency virus replication: Correlation between solution structure and viral inhibition
    • Wild, C.; Oas, T.; McDanal, C.; Bolognesi, D.; Matthews, T. A synthetic peptide inhibitor of human immunodeficiency virus replication: correlation between solution structure and viral inhibition. Proc. Natl. Acad. Sci. U.S.A 1992, 89, 10537-10541.
    • (1992) Proc. Natl. Acad. Sci. U.S.A , vol.89 , pp. 10537-10541
    • Wild, C.1    Oas, T.2    McDanal, C.3    Bolognesi, D.4    Matthews, T.5
  • 94
    • 0031883832 scopus 로고    scopus 로고
    • Determinants of human immunodeficiency virus type 1 resistance to gp41-derived inhibitory peptides
    • Rimsky, L.T.; Shugars, D.C.; Matthews, T.J. Determinants of human immunodeficiency virus type 1 resistance to gp41-derived inhibitory peptides. J. Virol. 1998, 72, 986-993.
    • (1998) J. Virol , vol.72 , pp. 986-993
    • Rimsky, L.T.1    Shugars, D.C.2    Matthews, T.J.3
  • 96
    • 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.; Greenberg, M.; Kuritzkes, D.R. Relative replicative fitness of human immunodeficiency virus type 1 mutants resistant to enfuvirtide (T-20). J. Virol. 2004, 78, 4628-4637.
    • (2004) J. Virol , vol.78 , pp. 4628-4637
    • Lu, J.1    Sista, P.2    Giguel, F.3    Greenberg, M.4    Kuritzkes, D.R.5
  • 97
    • 16244380203 scopus 로고    scopus 로고
    • Enfuvirtide resistance mutations: Impact on human immunodeficiency virus envelope function, entry inhibitor sensitivity, and virus neutralization
    • Reeves, J.D.; Lee, F.H.; Miamidian, J.L.; Jabara, C.B.; Juntilla, M.M.; Doms, R.W. Enfuvirtide resistance mutations: impact on human immunodeficiency virus envelope function, entry inhibitor sensitivity, and virus neutralization. J. Virol. 2005, 79, 4991-4999.
    • (2005) J. Virol , vol.79 , pp. 4991-4999
    • Reeves, J.D.1    Lee, F.H.2    Miamidian, J.L.3    Jabara, C.B.4    Juntilla, M.M.5    Doms, R.W.6
  • 98
    • 33947417638 scopus 로고    scopus 로고
    • Clinical resistance to enfuvirtide does not affect susceptibility of human immunodeficiency virus type 1 to other classes of entry inhibitors
    • Ray, N.; Harrison, J.E.; Blackburn, L.A.; Martin, J.N.; Deeks, S.G.; Doms, R.W. Clinical resistance to enfuvirtide does not affect susceptibility of human immunodeficiency virus type 1 to other classes of entry inhibitors. J. Virol. 2007, 81, 3240-3250.
    • (2007) J. Virol , vol.81 , pp. 3240-3250
    • Ray, N.1    Harrison, J.E.2    Blackburn, L.A.3    Martin, J.N.4    Deeks, S.G.5    Doms, R.W.6
  • 99
    • 7644236011 scopus 로고    scopus 로고
    • Emergence of a drug-dependent human immunodeficiency virus type 1 variant during therapy with the T20 fusion inhibitor
    • Baldwin, C.E.; Sanders, R.W.; Deng, Y.; Jurriaans, S.; Lange, J.M.; Lu, M.; Berkhout, B. Emergence of a drug-dependent human immunodeficiency virus type 1 variant during therapy with the T20 fusion inhibitor. J. Virol. 2004, 78, 12428-12437.
    • (2004) J. Virol , vol.78 , pp. 12428-12437
    • Baldwin, C.E.1    Sanders, R.W.2    Deng, Y.3    Jurriaans, S.4    Lange, J.M.5    Lu, M.6    Berkhout, B.7
  • 101
    • 0033856458 scopus 로고    scopus 로고
    • Sensitivity of human immunodeficiency virus type 1 to the fusion inhibitor T-20 is modulated by coreceptor specificity defined by the V3 loop of gp120
    • Derdeyn, C.A.; Decker, J.M.; Sfakianos, J.N.; Wu, X.; O'Brien, W.A.; Ratner, L.; Kappes, J.C.; Shaw, G.M.; Hunter, E. Sensitivity of human immunodeficiency virus type 1 to the fusion inhibitor T-20 is modulated by coreceptor specificity defined by the V3 loop of gp120. J. Virol. 2000, 74, 8358-8367.
    • (2000) J. Virol , vol.74 , pp. 8358-8367
    • Derdeyn, C.A.1    Decker, J.M.2    Sfakianos, J.N.3    Wu, X.4    O'Brien, W.A.5    Ratner, L.6    Kappes, J.C.7    Shaw, G.M.8    Hunter, E.9
  • 103
    • 2342514225 scopus 로고    scopus 로고
    • Impact of mutations in the coreceptor binding site on human immunodeficiency virus type 1 fusion, infection, and entry inhibitor sensitivity
    • Reeves, J.D.; Miamidian, J.L.; Biscone, M.J.; Lee, F.H.; Ahmad, N.; Pierson, T.C.; Doms, R.W. Impact of mutations in the coreceptor binding site on human immunodeficiency virus type 1 fusion, infection, and entry inhibitor sensitivity. J. Virol. 2004, 78, 5476-5485.
    • (2004) J. Virol , vol.78 , pp. 5476-5485
    • Reeves, J.D.1    Miamidian, J.L.2    Biscone, M.J.3    Lee, F.H.4    Ahmad, N.5    Pierson, T.C.6    Doms, R.W.7
  • 106
    • 33744492607 scopus 로고    scopus 로고
    • Synergistic in vitro antiretroviral activity of a humanized monoclonal anti-CD4 antibody (TNX-355) and enfuvirtide (T-20)
    • Zhang, X.Q.; Sorensen, M.; Fung, M.; Scoohley, R.T. Synergistic in vitro antiretroviral activity of a humanized monoclonal anti-CD4 antibody (TNX-355) and enfuvirtide (T-20). Antimicrob. Agents Chemother. 2006, 50, 2231-2233.
    • (2006) Antimicrob. Agents Chemother , vol.50 , pp. 2231-2233
    • Zhang, X.Q.1    Sorensen, M.2    Fung, M.3    Scoohley, R.T.4
  • 107
    • 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, K.A.; Thompson, D.A.; Rosenfield, S.I.; Maddon, P.J.; Dragic, T.; Olson, W.C. 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, 1121-1125.
    • (2001) J. Infect. Dis , vol.183 , pp. 1121-1125
    • Nagashima, K.A.1    Thompson, D.A.2    Rosenfield, S.I.3    Maddon, P.J.4    Dragic, T.5    Olson, W.C.6
  • 109
    • 0034671725 scopus 로고    scopus 로고
    • Aminooxypentane addition to the chemokine macrophage inflammatory protein-1alpha P increases receptor affinities and HIV inhibition
    • Townson, J.R.; Graham, G.J.; Landau, N.R.; Rasala, B.; Nibbs, R.J. Aminooxypentane addition to the chemokine macrophage inflammatory protein-1alpha P increases receptor affinities and HIV inhibition. J. Biol. Chem. 2000, 275, 39254-39261.
    • (2000) J. Biol. Chem , vol.275 , pp. 39254-39261
    • Townson, J.R.1    Graham, G.J.2    Landau, N.R.3    Rasala, B.4    Nibbs, R.J.5
  • 110
    • 0037799237 scopus 로고    scopus 로고
    • The core domain of chemokines binds CCR5 extracellular domains while their amino terminus interacts with the transmembrane helix bundle
    • Blanpain, C.; Doranz, B.J.; Bondue, A.; Govaerts, C.; De, L.A.; Vassart, G.; Doms, R.W.; Proudfoot, A.; Parmentier, M. The core domain of chemokines binds CCR5 extracellular domains while their amino terminus interacts with the transmembrane helix bundle. J. Biol. Chem. 2003, 278, 5179-5187.
    • (2003) J. Biol. Chem , vol.278 , pp. 5179-5187
    • Blanpain, C.1    Doranz, B.J.2    Bondue, A.3    Govaerts, C.4    De, L.A.5    Vassart, G.6    Doms, R.W.7    Proudfoot, A.8    Parmentier, M.9
  • 113
    • 0030745286 scopus 로고    scopus 로고
    • HIV coreceptor downregulation as antiviral principle: SDF-1alpha-dependent internalization of the chemokine receptor CXCR4 contributes to inhibition of HIV replication
    • Amara, A.; Gall, S.L.; Schwartz, O.; Salamero, J.; Montes, M.; Loetscher, P.; Baggiolini, M.; Virelizier, J.L.; Arenzana-Seisdedos, F. HIV coreceptor downregulation as antiviral principle: SDF-1alpha-dependent internalization of the chemokine receptor CXCR4 contributes to inhibition of HIV replication. J. Exp. Med. 1997, 186, 139-146.
    • (1997) J. Exp. Med , vol.186 , pp. 139-146
    • Amara, A.1    Gall, S.L.2    Schwartz, O.3    Salamero, J.4    Montes, M.5    Loetscher, P.6    Baggiolini, M.7    Virelizier, J.L.8    Arenzana-Seisdedos, F.9
  • 115
    • 0037053373 scopus 로고    scopus 로고
    • Association of chemokine-mediated block to HIV entry with coreceptor internalization
    • Brandt, S.M.; Mariani, R.; Holland, A.U.; Hope, T.J.; Landau, N.R. Association of chemokine-mediated block to HIV entry with coreceptor internalization. J. Biol. Chem. 2002, 277, 17291-17299.
    • (2002) J. Biol. Chem , vol.277 , pp. 17291-17299
    • Brandt, S.M.1    Mariani, R.2    Holland, A.U.3    Hope, T.J.4    Landau, N.R.5
  • 122
    • 0032889517 scopus 로고    scopus 로고
    • Enhancement of human immunodeficiency virus type 1 infection by the CC-chemokine RANTES is independent of the mechanism of virus-cell fusion
    • Gordon, C.J.; Muesing, M.A.; Proudfoot, A.E.; Power, C.A.; Moore, J.P.; Trkola, A. Enhancement of human immunodeficiency virus type 1 infection by the CC-chemokine RANTES is independent of the mechanism of virus-cell fusion. J. Virol. 1999, 73, 684-694.
    • (1999) J. Virol , vol.73 , pp. 684-694
    • Gordon, C.J.1    Muesing, M.A.2    Proudfoot, A.E.3    Power, C.A.4    Moore, J.P.5    Trkola, A.6
  • 123
    • 0042237921 scopus 로고    scopus 로고
    • RANTES (CCL5) uses the proteoglycan CD44 as an auxiliary receptor to mediate cellular activation signals and HIV-1 enhancement
    • Roscic-Mrkic, B.; Fischer, M.; Leemann, C.; Manrique, A.; Gordon, C.J.; Moore, J.P.; Proudfoot, A.E.; Trkola, A. RANTES (CCL5) uses the proteoglycan CD44 as an auxiliary receptor to mediate cellular activation signals and HIV-1 enhancement. Blood 2003, 102, 1169-1177.
    • (2003) Blood , vol.102 , pp. 1169-1177
    • Roscic-Mrkic, B.1    Fischer, M.2    Leemann, C.3    Manrique, A.4    Gordon, C.J.5    Moore, J.P.6    Proudfoot, A.E.7    Trkola, A.8
  • 127
    • 28644432424 scopus 로고    scopus 로고
    • Protection of macaques from vaginal SHIV challenge by an orally delivered CCR5 inhibitor
    • Veazey, R.S.; Springer, M.S.; Marx, P.A.; Dufour, J.; Klasse, P.J.; Moore, J.P. Protection of macaques from vaginal SHIV challenge by an orally delivered CCR5 inhibitor. Nat. Med. 2005, 11, 1293-1294.
    • (2005) Nat. Med , vol.11 , pp. 1293-1294
    • Veazey, R.S.1    Springer, M.S.2    Marx, P.A.3    Dufour, J.4    Klasse, P.J.5    Moore, J.P.6
  • 129
  • 133
    • 33745581733 scopus 로고    scopus 로고
    • GlaxoSmithKline ends aplaviroc trials
    • Crabb, C. GlaxoSmithKline ends aplaviroc trials. AIDS 2006, 20, 641.
    • (2006) AIDS , vol.20 , pp. 641
    • Crabb, C.1
  • 134
    • 20644453529 scopus 로고    scopus 로고
    • Generation and properties of a human immunodeficiency virus type 1 isolate resistant to the small molecule CCR5 inhibitor, SCH-417690 (SCH-D)
    • Marozsan, A.J.; Kuhmann, S.E.; Morgan, T.; Herrera, C.; Rivera-Troche, E.; Xu, S.; Baroudy, B. M.; Strizki, J.; Moore, J.P. Generation and properties of a human immunodeficiency virus type 1 isolate resistant to the small molecule CCR5 inhibitor, SCH-417690 (SCH-D). Virology 2005, 338, 182-199.
    • (2005) Virology , vol.338 , pp. 182-199
    • Marozsan, A.J.1    Kuhmann, S.E.2    Morgan, T.3    Herrera, C.4    Rivera-Troche, E.5    Xu, S.6    Baroudy, B.M.7    Strizki, J.8    Moore, J.P.9
  • 136
    • 33847237614 scopus 로고    scopus 로고
    • Reduced maximal inhibition in phenotypic susceptibility assays indicates that viral strains resistant to the CCR5 antagonist maraviroc utilize inhibitor-bound receptor for entry
    • Westby, M.; Smith-Burchnell, C.; Mori, J.; Lewis, M.; Mosley, M.; Stockdale, M.; Dorr, P.; Ciaramella, G.; Perros, M. Reduced maximal inhibition in phenotypic susceptibility assays indicates that viral strains resistant to the CCR5 antagonist maraviroc utilize inhibitor-bound receptor for entry. J. Virol. 2007, 81, 2359-2371.
    • (2007) J. Virol , vol.81 , pp. 2359-2371
    • Westby, M.1    Smith-Burchnell, C.2    Mori, J.3    Lewis, M.4    Mosley, M.5    Stockdale, M.6    Dorr, P.7    Ciaramella, G.8    Perros, M.9
  • 137
    • 33846574670 scopus 로고    scopus 로고
    • Isolation and characterization of human immunodeficiency virus type 1 resistant to the small-molecule CCR5 antagonist TAK-652
    • Baba, M.; Miyake, H.; Wang, X.; Okamoto, M.; Takashima, K. Isolation and characterization of human immunodeficiency virus type 1 resistant to the small-molecule CCR5 antagonist TAK-652. Antimicrob. Agents Chemother. 2007, 51, 707-715.
    • (2007) Antimicrob. Agents Chemother , vol.51 , pp. 707-715
    • Baba, M.1    Miyake, H.2    Wang, X.3    Okamoto, M.4    Takashima, K.5
  • 138
    • 33646443202 scopus 로고    scopus 로고
    • Emergence of CXCR4-using human immunodeficiency virus type 1 (HIV-1) variants in a minority of HIV-1-infected patients following treatment with the CCR5 antagonist maraviroc is from a pretreatment CXCR4-using virus reservoir
    • Westby, M.; Lewis, M.; Whitcomb, J.; Youle, M.; Pozniak, A.L.; James, I.T.; Jenkins, T.M.; Perros, M.; van der Ryst, E. Emergence of CXCR4-using human immunodeficiency virus type 1 (HIV-1) variants in a minority of HIV-1-infected patients following treatment with the CCR5 antagonist maraviroc is from a pretreatment CXCR4-using virus reservoir. J. Virol. 2006, 80, 4909-4920.
    • (2006) J. Virol , vol.80 , pp. 4909-4920
    • Westby, M.1    Lewis, M.2    Whitcomb, J.3    Youle, M.4    Pozniak, A.L.5    James, I.T.6    Jenkins, T.M.7    Perros, M.8    van der Ryst, E.9
  • 142
    • 65349147003 scopus 로고    scopus 로고
    • Selection of a simian-human immunodeficiency virus strain resistant to a vaginal microbicide in macaques
    • Dudley, D.M.; Wentzel, J.L.; Lalonde, M.S.; Veazey, R.S.; Arts, E.J. Selection of a simian-human immunodeficiency virus strain resistant to a vaginal microbicide in macaques. J. Virol. 2009, 83, 5067-5076.
    • (2009) J. Virol , vol.83 , pp. 5067-5076
    • Dudley, D.M.1    Wentzel, J.L.2    Lalonde, M.S.3    Veazey, R.S.4    Arts, E.J.5
  • 144
    • 34047271098 scopus 로고    scopus 로고
    • HIV-1 clones resistant to a small molecule CCR5 inhibitor use the inhibitor-bound form of CCR5 for entry
    • Pugach, P.; Marozsan, A.J.; Ketas, T.J.; Landes, E.L.; Moore, J.P.; Kuhmann, S.E. HIV-1 clones resistant to a small molecule CCR5 inhibitor use the inhibitor-bound form of CCR5 for entry. Virology 2007, 361, 212-228.
    • (2007) Virology , vol.361 , pp. 212-228
    • Pugach, P.1    Marozsan, A.J.2    Ketas, T.J.3    Landes, E.L.4    Moore, J.P.5    Kuhmann, S.E.6
  • 145
    • 65249151382 scopus 로고    scopus 로고
    • Resistance to CCR5 inhibitors caused by sequence changes in the fusion peptide of HIV-1 gp41
    • Anastassopoulou, C.G.; Ketas, T.J.; Klasse, P.J.; Moore, J.P. Resistance to CCR5 inhibitors caused by sequence changes in the fusion peptide of HIV-1 gp41. Proc. Natl. Acad. Sci. U.S.A 2009, 106, 5318-5323.
    • (2009) Proc. Natl. Acad. Sci. U.S.A , vol.106 , pp. 5318-5323
    • Anastassopoulou, C.G.1    Ketas, T.J.2    Klasse, P.J.3    Moore, J.P.4
  • 146
    • 40849085150 scopus 로고    scopus 로고
    • Mapping resistance to the CCR5 co-receptor antagonist vicriviroc using heterologous chimeric HIV-1 envelope genes reveals key determinants in the C2-V5 domain of gp120
    • Ogert, R.A.; Wojcik, L.; Buontempo, C.; Ba, L.; Buontempo, P.; Ralston, R.; Strizki, J.; Howe, J.A. Mapping resistance to the CCR5 co-receptor antagonist vicriviroc using heterologous chimeric HIV-1 envelope genes reveals key determinants in the C2-V5 domain of gp120. Virology 2008, 373, 387-399.
    • (2008) Virology , vol.373 , pp. 387-399
    • Ogert, R.A.1    Wojcik, L.2    Buontempo, C.3    Ba, L.4    Buontempo, P.5    Ralston, R.6    Strizki, J.7    Howe, J.A.8
  • 149
  • 150
    • 33747045164 scopus 로고    scopus 로고
    • An anti-CCR5 monoclonal antibody and small molecule CCR5 antagonists synergize by inhibiting different stages of human immunodeficiency virus type 1 entry
    • Safarian, D.; Carnec, X.; Tsamis, F.; Kajumo, F.; Dragic, T. An anti-CCR5 monoclonal antibody and small molecule CCR5 antagonists synergize by inhibiting different stages of human immunodeficiency virus type 1 entry. Virology 2006, 352, 477-484.
    • (2006) Virology , vol.352 , pp. 477-484
    • Safarian, D.1    Carnec, X.2    Tsamis, F.3    Kajumo, F.4    Dragic, T.5
  • 152
    • 15244356599 scopus 로고    scopus 로고
    • Kinetic factors control efficiencies of cell entry, efficacies of entry inhibitors, and mechanisms of adaptation of human immunodeficiency virus
    • Platt, E.J.; Durnin, J.P.; Kabat, D. Kinetic factors control efficiencies of cell entry, efficacies of entry inhibitors, and mechanisms of adaptation of human immunodeficiency virus. J. Virol. 2005, 79, 4347-4356.
    • (2005) J. Virol , vol.79 , pp. 4347-4356
    • Platt, E.J.1    Durnin, J.P.2    Kabat, D.3
  • 153
    • 23844479503 scopus 로고    scopus 로고
    • Ternary complex formation of human immunodeficiency virus type 1 Env, CD4, and chemokine receptor captured as an intermediate of membrane fusion
    • Mkrtchyan, S.R.; Markosyan, R.M.; Eadon, M.T.; Moore, J.P.; Melikyan, G.B.; Cohen, F.S. Ternary complex formation of human immunodeficiency virus type 1 Env, CD4, and chemokine receptor captured as an intermediate of membrane fusion. J. Virol. 2005, 79, 11161-11169.
    • (2005) J. Virol , vol.79 , pp. 11161-11169
    • Mkrtchyan, S.R.1    Markosyan, R.M.2    Eadon, M.T.3    Moore, J.P.4    Melikyan, G.B.5    Cohen, F.S.6
  • 154
    • 0032924183 scopus 로고    scopus 로고
    • Highly potent RANTES analogues either prevent CCR5-using human immunodeficiency virus type 1 infection in vivo or rapidly select for CXCR4-using variants
    • Mosier, D.E.; Picchio, G.R.; Gulizia, R.J.; Sabbe, R.; Poignard, P.; Picard, L.; Offord, R.E.; Thompson, D.A.; Wilken, J. Highly potent RANTES analogues either prevent CCR5-using human immunodeficiency virus type 1 infection in vivo or rapidly select for CXCR4-using variants. J. Virol. 1999, 73, 3544-3550.
    • (1999) J. Virol , vol.73 , pp. 3544-3550
    • Mosier, D.E.1    Picchio, G.R.2    Gulizia, R.J.3    Sabbe, R.4    Poignard, P.5    Picard, L.6    Offord, R.E.7    Thompson, D.A.8    Wilken, J.9
  • 155
    • 34547115470 scopus 로고    scopus 로고
    • Natural variation in the V3 crown of human immunodeficiency virus type 1 affects replicative fitness and entry inhibitor sensitivity
    • Lobritz, M.A.; Marozsan, A.J.; Troyer, R.M.; Arts, E.J. Natural variation in the V3 crown of human immunodeficiency virus type 1 affects replicative fitness and entry inhibitor sensitivity. J. Virol. 2007, 81, 8258-8269.
    • (2007) J. Virol , vol.81 , pp. 8258-8269
    • Lobritz, M.A.1    Marozsan, A.J.2    Troyer, R.M.3    Arts, E.J.4
  • 157
    • 0141617472 scopus 로고    scopus 로고
    • Decreasing sensitivity to RANTES (regulated on activation, normally T cell-expressed and -secreted) neutralization of CC chemokine receptor 5-using, non-syncytium-inducing virus variants in the course of human immunodeficiency virus type 1 infection
    • Koning, F.A.; Kwa, D.; Boeser-Nunnink, B.; Dekker, J.; Vingerhoed, J.; Hiemstra, H.; Schuitemaker, H. Decreasing sensitivity to RANTES (regulated on activation, normally T cell-expressed and -secreted) neutralization of CC chemokine receptor 5-using, non-syncytium-inducing virus variants in the course of human immunodeficiency virus type 1 infection. J. Infect. Dis. 2003, 188, 864-872.
    • (2003) J. Infect. Dis , vol.188 , pp. 864-872
    • Koning, F.A.1    Kwa, D.2    Boeser-Nunnink, B.3    Dekker, J.4    Vingerhoed, J.5    Hiemstra, H.6    Schuitemaker, H.7
  • 158
    • 0033941573 scopus 로고    scopus 로고
    • Cooperation of multiple CCR5 coreceptors is required for infections by human immunodeficiency virus type 1
    • Kuhmann, S.E.; Platt, E.J.; Kozak, S.L.; Kabat, D. Cooperation of multiple CCR5 coreceptors is required for infections by human immunodeficiency virus type 1. J. Virol. 2000, 74, 7005-7015.
    • (2000) J. Virol , vol.74 , pp. 7005-7015
    • Kuhmann, S.E.1    Platt, E.J.2    Kozak, S.L.3    Kabat, D.4
  • 159
    • 25144500649 scopus 로고    scopus 로고
    • Stoichiometry of envelope glycoprotein trimers in the entry of human immunodeficiency virus type 1
    • Yang, X.; Kurteva, S.; Ren, X.; Lee, S.; Sodroski, J. Stoichiometry of envelope glycoprotein trimers in the entry of human immunodeficiency virus type 1. J. Virol. 2005, 79, 12132-12147.
    • (2005) J. Virol , vol.79 , pp. 12132-12147
    • Yang, X.1    Kurteva, S.2    Ren, X.3    Lee, S.4    Sodroski, J.5
  • 160
    • 33646185493 scopus 로고    scopus 로고
    • Subunit stoichiometry of human immunodeficiency virus type 1 envelope glycoprotein trimers during virus entry into host cells
    • Yang, X.; Kurteva, S.; Ren, X.; Lee, S.; Sodroski, J. Subunit stoichiometry of human immunodeficiency virus type 1 envelope glycoprotein trimers during virus entry into host cells. J. Virol. 2006, 80, 4388-4395.
    • (2006) J. Virol , vol.80 , pp. 4388-4395
    • Yang, X.1    Kurteva, S.2    Ren, X.3    Lee, S.4    Sodroski, J.5
  • 161
    • 0025315836 scopus 로고
    • HIV requires multiple gp120 molecules for CD4-mediated infection
    • Layne, S.P.; Merges, M.J.; Dembo, M.; Spouge, J.L.; Nara, P.L. HIV requires multiple gp120 molecules for CD4-mediated infection. Nature 1990, 346, 277-279.
    • (1990) Nature , vol.346 , pp. 277-279
    • Layne, S.P.1    Merges, M.J.2    Dembo, M.3    Spouge, J.L.4    Nara, P.L.5
  • 162
    • 33745833942 scopus 로고    scopus 로고
    • Dominant-negative effect of hetero-oligomerization on the function of the human immunodeficiency virus type 1 envelope glycoprotein complex
    • Herrera, C.; Klasse, P.J.; Kibler, C.W.; Michael, E.; Moore, J.P.; Beddows, S. Dominant-negative effect of hetero-oligomerization on the function of the human immunodeficiency virus type 1 envelope glycoprotein complex. Virology 2006, 351, 121-132.
    • (2006) Virology , vol.351 , pp. 121-132
    • Herrera, C.1    Klasse, P.J.2    Kibler, C.W.3    Michael, E.4    Moore, J.P.5    Beddows, S.6
  • 164
    • 18844372793 scopus 로고    scopus 로고
    • Differences in the fitness of two diverse wild-type human immunodeficiency virus type 1 isolates are related to the efficiency of cell binding and entry
    • Marozsan, A.J.; Moore, D.M.; Lobritz, M.A.; Fraundorf, E.; Abraha, A.; Reeves, J.D.; Arts, E.J. Differences in the fitness of two diverse wild-type human immunodeficiency virus type 1 isolates are related to the efficiency of cell binding and entry. J. Virol. 2005, 79, 7121-7134.
    • (2005) J. Virol , vol.79 , pp. 7121-7134
    • Marozsan, A.J.1    Moore, D.M.2    Lobritz, M.A.3    Fraundorf, E.4    Abraha, A.5    Reeves, J.D.6    Arts, E.J.7
  • 165
    • 0030747157 scopus 로고    scopus 로고
    • RNA virus mutations and fitness for survival
    • Domingo, E.; Holland, J.J. RNA virus mutations and fitness for survival. Annu. Rev. Microbiol. 1997, 51, 151-178.
    • (1997) Annu. Rev. Microbiol , vol.51 , pp. 151-178
    • Domingo, E.1    Holland, J.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.