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Volumn 281, Issue , 2003, Pages 1-27

HIV-1 entry and its inhibition

Author keywords

[No Author keywords available]

Indexed keywords

1,1' [1,4 PHENYLENEBIS(METHYLENE)]BIS(1,4,8,11 TETRAAZACYCLOTETRADECANE); ALPHA N ACETYLNONA DEXTRO ARGININE AMIDE; CD4 ANTIGEN; CHEMOKINE RECEPTOR; CHEMOKINE RECEPTOR CCR5; CHEMOKINE RECEPTOR CCR5 INHIBITOR; CHEMOKINE RECEPTOR CXCR4; ENFUVIRTIDE; GLYCOPROTEIN GP 120; GLYCOPROTEIN GP 41; N [4 [[[6,7 DIHYDRO 2 (4 METHYLPHENYL) 5H BENZOCYCLOHEPTEN 8 YL]CARBONYL]AMINO]BENZYL] N,N DIMETHYL 2H TETRAHYDROPYRAN 4 AMINIUM CHLORIDE; SCH C; T 1249; T 22; UNCLASSIFIED DRUG; VIRUS ENVELOPE PROTEIN;

EID: 0041663569     PISSN: 0070217X     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-3-642-19012-4_1     Document Type: Review
Times cited : (103)

References (140)
  • 1
    • 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, CC, Feng, Y, Kennedy, PE, Murphy, PM, and Berger, EA (1996) CC CKR5: a RANTES, MIP-1alpha, MIP-1beta receptor as a fusion cofactor for macrophage-tropic HIV-1, Science 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
  • 3
    • 0032954383 scopus 로고    scopus 로고
    • T134, a small-molecule CXCR4 inhibitor, has no cross-drug resistance with AMD3100, a CXCR4 antagonist with a different structure
    • Arakaki, R, Tamamura, H, Premanathan, M, Kanbara, K, Ramanan, S, Mochizuki, K, Baba, M, Fujii, N, and Nakashima, H (1999) T134, a small-molecule CXCR4 inhibitor, has no cross-drug resistance with AMD3100, a CXCR4 antagonist with a different structure, J Virol 73: 1719-1723
    • (1999) J Virol , vol.73 , pp. 1719-1723
    • Arakaki, R.1    Tamamura, H.2    Premanathan, M.3    Kanbara, K.4    Ramanan, S.5    Mochizuki, K.6    Baba, M.7    Fujii, N.8    Nakashima, H.9
  • 5
    • 0025886458 scopus 로고
    • Resistance of primary isolates of human immunodeficiency virus type 1 to soluble CD4 is independent of CD4-gp120 binding affinity
    • Ashkenazi, A, Smith, DH, Marsters, SA, Riddle, L, Gregory, TJ, Ho, DD, and Capon, DJ (1991) Resistance of primary isolates of human immunodeficiency virus type 1 to soluble CD4 is independent of CD4-gp120 binding affinity, Proc Natl Acad Sci USA 88: 7056-7060
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 7056-7060
    • Ashkenazi, A.1    Smith, D.H.2    Marsters, S.A.3    Riddle, L.4    Gregory, T.J.5    Ho, D.D.6    Capon, D.J.7
  • 7
    • 0033106334 scopus 로고    scopus 로고
    • Structural basis for paramyxovirus-mediated membrane fusion
    • Baker, KA, Dutch, RE, Lamb, RA, and Jardetzky, TS (1999) Structural basis for paramyxovirus-mediated membrane fusion, Mol Cell 3: 309-19
    • (1999) Mol Cell , vol.3 , pp. 309-319
    • Baker, K.A.1    Dutch, R.E.2    Lamb, R.A.3    Jardetzky, T.S.4
  • 8
    • 0036721331 scopus 로고    scopus 로고
    • Quantitative expression and virus transmission analysis of DC-SIGN on monocyte-derived dendritic cells
    • Baribaud, F, Pohlmann, S, Leslie, G, Mortari, F, and Doms, RW (2002) Quantitative expression and virus transmission analysis of DC-SIGN on monocyte-derived dendritic cells, J Virol 76: 9135-42
    • (2002) J Virol , vol.76 , pp. 9135-9142
    • Baribaud, F.1    Pohlmann, S.2    Leslie, G.3    Mortari, F.4    Doms, R.W.5
  • 10
    • 0035911220 scopus 로고    scopus 로고
    • A dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin (DC-SIGN)-related protein is highly expressed on human liver sinusoidal endothelial cells and promotes HIV-1 infection
    • Bashirova, AA, Geijtenbeek, TB, van Duijnhoven, GC, van Vliet, SJ, Eilering, JB, Martin, MP, Wu, L, Martin, TD, Viebig, N, Knolle, PA, et al. (2001) A dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin (DC-SIGN)-related protein is highly expressed on human liver sinusoidal endothelial cells and promotes HIV-1 infection, J Exp Med 193: 671-8
    • (2001) J Exp Med , vol.193 , pp. 671-678
    • Bashirova, A.A.1    Geijtenbeek, T.B.2    Van Duijnhoven, G.C.3    Van Vliet, S.J.4    Eilering, J.B.5    Martin, M.P.6    Wu, L.7    Martin, T.D.8    Viebig, N.9    Knolle, P.A.10
  • 11
    • 0036838693 scopus 로고    scopus 로고
    • Identification of conserved and variable structures in the human immunodeficiency virus gp120 glycoprotein of importance for CXCR4 binding
    • Basmaciogullari, S, Babcock, GJ, Van Ryk, D, Wojtowicz, W, and Sodroski, J (2002) Identification of conserved and variable structures in the human immunodeficiency virus gp120 glycoprotein of importance for CXCR4 binding, J Virol 76: 10791-800
    • (2002) J Virol , vol.76 , pp. 10791-10800
    • Basmaciogullari, S.1    Babcock, G.J.2    Van Ryk, D.3    Wojtowicz, W.4    Sodroski, J.5
  • 13
    • 0033012398 scopus 로고    scopus 로고
    • Chemokine receptors as HIV-1 coreceptors: Roles in viral entry, tropism, and disease
    • Berger, EA, Murphy, PM, and Farber, JM (1999) Chemokine receptors as HIV-1 coreceptors: roles in viral entry, tropism, and disease, Annu Rev Immunol 17: 657-700
    • (1999) Annu Rev Immunol , vol.17 , pp. 657-700
    • Berger, E.A.1    Murphy, P.M.2    Farber, J.M.3
  • 16
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough, PA, Hughson, FM, Skehel, JJ, and Wiley, DC (1994) Structure of influenza haemagglutinin at the pH of membrane fusion, Nature 371: 37-43
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 17
    • 0034699898 scopus 로고    scopus 로고
    • Adverse effects of antiretroviral therapy
    • Carr, A, and Cooper, DA (2000) Adverse effects of antiretroviral therapy, Lancet 356: 1423-30
    • (2000) Lancet , vol.356 , pp. 1423-1430
    • Carr, A.1    Cooper, D.A.2
  • 18
    • 0033583977 scopus 로고    scopus 로고
    • Diagnosis, prediction, and natural course of HIV-1 protease-inhibitor-associated lipodystrophy, hyperlipidaemia, and diabetes mellitus: A cohort study
    • Carr, A, Samaras, K, Thorisdottir, A, Kaufmann, GR, Chisholm, DJ, and Cooper, DA (1999) Diagnosis, prediction, and natural course of HIV-1 protease-inhibitor-associated lipodystrophy, hyperlipidaemia, and diabetes mellitus: a cohort study, Lancet 353: 2093-9
    • (1999) Lancet , vol.353 , pp. 2093-2099
    • Carr, A.1    Samaras, K.2    Thorisdottir, A.3    Kaufmann, G.R.4    Chisholm, D.J.5    Cooper, D.A.6
  • 19
    • 0025678671 scopus 로고
    • Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins
    • Chambers, P, Pringle, CR, and Easton, AJ (1990) Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins, J Gen Virol 71: 3075-80
    • (1990) J Gen Virol , vol.71 , pp. 3075-3080
    • Chambers, P.1    Pringle, C.R.2    Easton, A.J.3
  • 20
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan, DC, Fass, D, Berger, JM, and Kim, PS (1997) Core structure of gp41 from the HIV envelope glycoprotein, Cell 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
  • 22
    • 0023748691 scopus 로고
    • Substitution of murine for human CD4 residues identifies amino acids critical for HIV-gp120 binding
    • Clayton, LK, Hussey, RE, Steinbrich, R, Ramachandran, H, Husain, Y, and Reinherz, EL (1988) Substitution of murine for human CD4 residues identifies amino acids critical for HIV-gp120 binding, Nature 335: 363-6
    • (1988) Nature , vol.335 , pp. 363-366
    • Clayton, L.K.1    Hussey, R.E.2    Steinbrich, R.3    Ramachandran, H.4    Husain, Y.5    Reinherz, E.L.6
  • 23
    • 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, AL, Garzino-Demo, A, Arya, SK, Gallo, RC, and Lusso, P (1995) Identification of RANTES, MIP-1 alpha, and MIP-1 beta as the major HIV-suppressive factors produced by CD8+ T cells, Science 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
  • 24
    • 0025016076 scopus 로고
    • High concentrations of recombinant soluble CD4 are required to neutralize primary human immunodeficiency virus type 1 isolates
    • Daar, ES, Li, XL, Moudgil, T, and Ho, DD (1990) High concentrations of recombinant soluble CD4 are required to neutralize primary human immunodeficiency virus type 1 isolates, Proc Natl Acad Sci USA 87: 6574-6578
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 6574-6578
    • Daar, E.S.1    Li, X.L.2    Moudgil, T.3    Ho, D.D.4
  • 29
    • 0025010813 scopus 로고
    • Retroviral envelope glycoproteins contain a "leucine zipper"-like repeat
    • Delwart, EL, Mosialos, G, and Gilmore, T (1990) Retroviral envelope glycoproteins contain a "leucine zipper"-like repeat, AIDS Res Hum Retroviruses 6: 703-6
    • (1990) AIDS Res Hum Retroviruses , vol.6 , pp. 703-706
    • Delwart, E.L.1    Mosialos, G.2    Gilmore, T.3
  • 31
    • 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, CA, Decker, JM, Sfakianos, JN, Wu, X, O'Brien, WA, Ratner, L, Kappes, JC, Shaw, GM, and Hunter, E (2000) 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 74: 8358-67
    • (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
  • 32
    • 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, Zhang, Z, O'Brien, WA, Ratner, L, Shaw, GM, and Hunter, E (2001) 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 75: 8605-14
    • (2001) J Virol , vol.75 , pp. 8605-8614
    • Derdeyn, C.A.1    Decker, J.M.2    Sfakianos, J.N.3    Zhang, Z.4    O'Brien, W.A.5    Ratner, L.6    Shaw, G.M.7    Hunter, E.8
  • 33
    • 0034715519 scopus 로고    scopus 로고
    • Beyond receptor expression: The influence of receptor conformation, density, and affinity in HIV-1 infection
    • Doms, RW (2000) Beyond receptor expression: the influence of receptor conformation, density, and affinity in HIV-1 infection, Virology 276: 229-237
    • (2000) Virology , vol.276 , pp. 229-237
    • Doms, R.W.1
  • 34
    • 0030770546 scopus 로고    scopus 로고
    • Unwelcomed guests with master keys: How HIV uses chemokine receptors for cellular entry
    • Doms, RW, and Peiper, SC (1997) Unwelcomed guests with master keys: how HIV uses chemokine receptors for cellular entry, Virology 235: 179-90
    • (1997) Virology , vol.235 , pp. 179-190
    • Doms, R.W.1    Peiper, S.C.2
  • 38
    • 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, Smyth, RJ, Samson, M, Peiper, SC, Parmentier, M, Collman, RG, and Doms, RW (1996) 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 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
  • 41
    • 0031985314 scopus 로고    scopus 로고
    • Spontaneous mutations in the env gene of the human immunodeficiency virus type 1 NDK isolate are associated with a CD4-independent entry phenotype
    • Dumonceaux, J, Nisole, S, Chanel, C, Quivet, L, Amara, A, Baleux, F, Briand, P, and Hazan, U (1998) Spontaneous mutations in the env gene of the human immunodeficiency virus type 1 NDK isolate are associated with a CD4-independent entry phenotype, J Virol 72: 512-519
    • (1998) J Virol , vol.72 , pp. 512-519
    • Dumonceaux, J.1    Nisole, S.2    Chanel, C.3    Quivet, L.4    Amara, A.5    Baleux, F.6    Briand, P.7    Hazan, U.8
  • 42
    • 0033214895 scopus 로고    scopus 로고
    • Inhibiting HIV-1 entry: Discovery of D-peptide inhibitors that target the gp41 coiled-coil pocket
    • Eckert, DM, Malashkevich, VN, Hong, LH, Carr, PA, and Kim, PS (1999) Inhibiting HIV-1 entry: discovery of D-peptide inhibitors that target the gp41 coiled-coil pocket, Cell 99: 103-15
    • (1999) Cell , vol.99 , pp. 103-115
    • Eckert, D.M.1    Malashkevich, V.N.2    Hong, L.H.3    Carr, P.A.4    Kim, P.S.5
  • 44
    • 0035035296 scopus 로고    scopus 로고
    • Relationships between CD4 independence, neutralization sensitivity, and exposure of a CD4-induced epitope in a human immunodeficiency virus type 1 envelope protein
    • Edwards, TG, Hoffman, TL, Baribaud, F, Wyss, S, LaBranche, CC, Romano, J, Adkinson, J, Sharron, M, Hoxie, JA, and Doms, RW (2001) Relationships between CD4 independence, neutralization sensitivity, and exposure of a CD4-induced epitope in a human immunodeficiency virus type 1 envelope protein, J Virol 75: 5230-5239
    • (2001) J Virol , vol.75 , pp. 5230-5239
    • Edwards, T.G.1    Hoffman, T.L.2    Baribaud, F.3    Wyss, S.4    LaBranche, C.C.5    Romano, J.6    Adkinson, J.7    Sharron, M.8    Hoxie, J.A.9    Doms, R.W.10
  • 46
    • 0033059948 scopus 로고    scopus 로고
    • Shift of clinical human immunodeficiency virus type 1 isolates from X4 to R5 and prevention of emergence of the syncytium-inducing phenotype by blockade of CXCR4
    • Este, JA, Cabrera, C, Blanco, J, Gutierrez, A, Bridger, G, Henson, G, Clotet, B, Schols, D, and De Clercq, E (1999) Shift of clinical human immunodeficiency virus type 1 isolates from X4 to R5 and prevention of emergence of the syncytium-inducing phenotype by blockade of CXCR4, J Virol 73: 5577-85
    • (1999) J Virol , vol.73 , pp. 5577-5585
    • Este, J.A.1    Cabrera, C.2    Blanco, J.3    Gutierrez, A.4    Bridger, G.5    Henson, G.6    Clotet, B.7    Schols, D.8    De Clercq, E.9
  • 47
    • 0029556891 scopus 로고
    • Dissection of a retrovirus envelope protein reveals structural similarity to influenza hemagglutinin
    • Fass, D, and Kim, PS (1995) Dissection of a retrovirus envelope protein reveals structural similarity to influenza hemagglutinin, Curr Biol 5: 1377-83
    • (1995) Curr Biol , vol.5 , pp. 1377-1383
    • Fass, D.1    Kim, P.S.2
  • 48
    • 0035824446 scopus 로고    scopus 로고
    • Structural basis for selective recognition of oligosaccharides by DC-SIGN and DC-SIGNR
    • Feinberg, H, Mitchell, DA, Drickamer, K, and Weis, WI (2001) Structural basis for selective recognition of oligosaccharides by DC-SIGN and DC-SIGNR, Science 294: 2163-6
    • (2001) Science , vol.294 , pp. 2163-2166
    • Feinberg, H.1    Mitchell, D.A.2    Drickamer, K.3    Weis, W.I.4
  • 49
    • 0030002637 scopus 로고    scopus 로고
    • HIV-1 entry cofactor: Functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor
    • Feng, Y, Broder, CC, Kennedy, PE, and Berger, EA (1996) HIV-1 entry cofactor: functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor, Science 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
  • 51
    • 0036184630 scopus 로고    scopus 로고
    • Infectious and whole inactivated simian immunodeficiency viruses interact similarly with primate dendritic cells (DCs): Differential intracellular fate of virions in mature and immature DCs
    • Frank, I, Piatak, M, Jr., Stoessel, H, Romani, N, Bonnyay, D, Lifson, JD, and Pope, M (2002) Infectious and whole inactivated simian immunodeficiency viruses interact similarly with primate dendritic cells (DCs): differential intracellular fate of virions in mature and immature DCs, J Virol 76: 2936-51
    • (2002) J Virol , vol.76 , pp. 2936-2951
    • Frank, I.1    Piatak M., Jr.2    Stoessel, H.3    Romani, N.4    Bonnyay, D.5    Lifson, J.D.6    Pope, M.7
  • 52
    • 0028851288 scopus 로고
    • Temperature dependence of cell-cell fusion induced by the envelope glycoprotein of human immunodeficiency virus type I
    • Frey, S, Marsh, M, Gunther, S, Pelchen-Matthews, A, Stephens, P, Ortlepp, S, and Stegmann, T (1995) Temperature dependence of cell-cell fusion induced by the envelope glycoprotein of human immunodeficiency virus type I, J Virol 69: 1462-1472
    • (1995) J Virol , vol.69 , pp. 1462-1472
    • Frey, S.1    Marsh, M.2    Gunther, S.3    Pelchen-Matthews, A.4    Stephens, P.5    Ortlepp, S.6    Stegmann, T.7
  • 53
    • 0031959601 scopus 로고    scopus 로고
    • Capture of an early fusion-active conformation of HIV-1 gp41
    • Furuta, RA, Wild, CT, Weng, Y, and Weiss, CD (1998) Capture of an early fusion-active conformation of HIV-1 gp41, Nat Struct Biol 5: 276-9
    • (1998) Nat Struct Biol , vol.5 , pp. 276-279
    • Furuta, R.A.1    Wild, C.T.2    Weng, Y.3    Weiss, C.D.4
  • 55
    • 0035900003 scopus 로고    scopus 로고
    • HIV-1 gp41 six-helix bundle formation occurs rapidly after the engagement of gp120 by CXCR4 in the HIV-1 Env-mediated fusion process
    • Gallo, SA, Puri, A, and Blumenthal, R (2001) HIV-1 gp41 six-helix bundle formation occurs rapidly after the engagement of gp120 by CXCR4 in the HIV-1 Env-mediated fusion process, Biochemistry (Mosc) 40: 12231-6
    • (2001) Biochemistry (Mosc) , vol.40 , pp. 12231-12236
    • Gallo, S.A.1    Puri, A.2    Blumenthal, R.3
  • 56
    • 0029875107 scopus 로고    scopus 로고
    • Effective ex vivo neutralization of human immunodeficiency virus type 1 in plasma by recombinant immunoglobulin molecules
    • Gauduin, MC, Allaway, GP, Maddon, PJ, Barbas, CF 3rd, Burton, DR, and Koup, RA (1996) Effective ex vivo neutralization of human immunodeficiency virus type 1 in plasma by recombinant immunoglobulin molecules, J Virol 70: 2586-92
    • (1996) J Virol , vol.70 , pp. 2586-2592
    • Gauduin, M.C.1    Allaway, G.P.2    Maddon, P.J.3    Barbas C.F. III4    Burton, D.R.5    Koup, R.A.6
  • 57
    • 0031900546 scopus 로고    scopus 로고
    • CD4-immunoglobulin G2 protects Hu-PBL-SCID mice against challenge by primary human immunodeficiency virus type 1 isolates
    • Gauduin, MC, Allaway, GP, Olson, WC, Weir, R, Maddon, PJ, and Koup, RA (1998) CD4-immunoglobulin G2 protects Hu-PBL-SCID mice against challenge by primary human immunodeficiency virus type 1 isolates, J Virol 72: 3475-8
    • (1998) J Virol , vol.72 , pp. 3475-3478
    • Gauduin, M.C.1    Allaway, G.P.2    Olson, W.C.3    Weir, R.4    Maddon, P.J.5    Koup, R.A.6
  • 61
    • 0442268112 scopus 로고    scopus 로고
    • A controlled trial of two nucleoside analogues plus indinavir in persons with human immunodeficiency virus infection and CD4 cell counts of 200 per cubic millimeter or less
    • AIDS Clinical Trials Group 320 Study Team
    • Hammer, SM, Squires, KE, Hughes, MD, Grimes, JM, Demeter, LM, Currier, JS, Eron, JJ, Jr., Feinberg, JE, Balfour, HH, Jr., Deyton, LR, et al. (1997) A controlled trial of two nucleoside analogues plus indinavir in persons with human immunodeficiency virus infection and CD4 cell counts of 200 per cubic millimeter or less. AIDS Clinical Trials Group 320 Study Team, N Engl J Med 337: 725-33
    • (1997) N Engl J Med , vol.337 , pp. 725-733
    • Hammer, S.M.1    Squires, K.E.2    Hughes, M.D.3    Grimes, J.M.4    Demeter, L.M.5    Currier, J.S.6    Eron J.J., Jr.7    Feinberg, J.E.8    Balfour H.H., Jr.9    Deyton, L.R.10
  • 63
    • 0033032389 scopus 로고    scopus 로고
    • Dendritic cell-T-cell interactions support coreceptor-independent human immunodeficiency virus type 1 transmission in the human genital tract
    • Hladik, F, Lentz, G, Akridge, RE, Peterson, G, Kelley, H, McElroy, A, and McElrath, MJ (1999) Dendritic cell-T-cell interactions support coreceptor-independent human immunodeficiency virus type 1 transmission in the human genital tract, J Virol 73: 5833-42
    • (1999) J Virol , vol.73 , pp. 5833-5842
    • Hladik, F.1    Lentz, G.2    Akridge, R.E.3    Peterson, G.4    Kelley, H.5    McElroy, A.6    McElrath, M.J.7
  • 69
    • 0036148171 scopus 로고    scopus 로고
    • Segregation of CD4 and CXCR4 into distinct lipid microdomains in T lymphocytes suggests a mechanism for membrane destabilization by human immunodeficiency virus
    • Kozak, SL, Heard, JM, and Kabat, D (2002) Segregation of CD4 and CXCR4 into distinct lipid microdomains in T lymphocytes suggests a mechanism for membrane destabilization by human immunodeficiency virus, J Virol 76: 1802-15
    • (2002) J Virol , vol.76 , pp. 1802-1815
    • Kozak, S.L.1    Heard, J.M.2    Kabat, D.3
  • 70
    • 0033941573 scopus 로고    scopus 로고
    • Cooperation of multiple CCR5 coreceptors is required for infections by human immunodeficiency virus type 1
    • Kuhmann, SE, Platt, EJ, Kozak, SL, and Kabat, D (2000) Cooperation of multiple CCR5 coreceptors is required for infections by human immunodeficiency virus type 1, J Virol 74: 7005-15
    • (2000) J Virol , vol.74 , pp. 7005-7015
    • Kuhmann, S.E.1    Platt, E.J.2    Kozak, S.L.3    Kabat, D.4
  • 71
    • 0036172314 scopus 로고    scopus 로고
    • DC-SIGN-mediated internalization of HIV is required for trans-enhancement of T cell infection
    • Kwon, DS, Gregorio, G, Bitton, N, Hendrickson, WA, and Littman, DR (2002) DC-SIGN-mediated internalization of HIV is required for trans-enhancement of T cell infection, Immunity 16: 135-44
    • (2002) Immunity , vol.16 , pp. 135-144
    • Kwon, D.S.1    Gregorio, G.2    Bitton, N.3    Hendrickson, W.A.4    Littman, D.R.5
  • 72
    • 0032543307 scopus 로고    scopus 로고
    • Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
    • Kwong, PD, Wyatt, R, Robinson, J, Sweet, RW, Sodroski, J, and Hendrickson, WA (1998) Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody, Nature 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
  • 75
    • 0025315836 scopus 로고
    • HIV requires multiple gp120 molecules for CD4-mediated infection
    • Layne, SP, Merges, MJ, Dembo, M, Spouge, JL, and Nara, PL (1990) HIV requires multiple gp120 molecules for CD4-mediated infection, Nature 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
  • 77
    • 0033609149 scopus 로고    scopus 로고
    • Quantification of CD4, CCR5, and CXCR4 levels on lymphocyte subsets, dendritic cells, and differentially conditioned monocyte-derived macrophages
    • Lee, B, Sharron, M, Montaner, LJ, Weissman, D, and Doms, RW (1999) Quantification of CD4, CCR5, and CXCR4 levels on lymphocyte subsets, dendritic cells, and differentially conditioned monocyte-derived macrophages, Proc Natl Acad Sci USA 96: 5215-5220
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 5215-5220
    • Lee, B.1    Sharron, M.2    Montaner, L.J.3    Weissman, D.4    Doms, R.W.5
  • 80
    • 0028834461 scopus 로고
    • A trimeric structural domain of the HIV-1 transmembrane glycoprotein
    • Lu, M, Blacklow, SC, and Kim, PS (1995) A trimeric structural domain of the HIV-1 transmembrane glycoprotein, Nat Struct Biol 2: 1075-1082
    • (1995) Nat Struct Biol , vol.2 , pp. 1075-1082
    • Lu, M.1    Blacklow, S.C.2    Kim, P.S.3
  • 81
    • 0023028190 scopus 로고
    • The T4 gene encodes the AIDS virus receptor and is expressed in the immune system and the brain
    • Maddon, PJ, Dalgleish, AG, McDougal, JS, Clapham, PR, Weiss, RA, and Axel, R (1986) The T4 gene encodes the AIDS virus receptor and is expressed in the immune system and the brain, Cell 47: 333-348
    • (1986) Cell , vol.47 , pp. 333-348
    • Maddon, P.J.1    Dalgleish, A.G.2    McDougal, J.S.3    Clapham, P.R.4    Weiss, R.A.5    Axel, R.6
  • 82
    • 0035860744 scopus 로고    scopus 로고
    • Novel low molecular weight spirodiketopiperazine derivatives potently inhibit R5 HIV-1 infection through their antagonistic effects on CCR5
    • Maeda, K, Yoshimura, K, Shibayama, S, Habashita, H, Tada, H, Sagawa, K, Miyakawa, T, Aoki, M, Fukushima, D, and Mitsuya, H (2001) Novel low molecular weight spirodiketopiperazine derivatives potently inhibit R5 HIV-1 infection through their antagonistic effects on CCR5, J Biol Chem 276: 35194-200
    • (2001) J Biol Chem , vol.276 , pp. 35194-35200
    • Maeda, K.1    Yoshimura, K.2    Shibayama, S.3    Habashita, H.4    Tada, H.5    Sagawa, K.6    Miyakawa, T.7    Aoki, M.8    Fukushima, D.9    Mitsuya, H.10
  • 84
    • 0022587282 scopus 로고
    • Binding of HTLV-III/LAV to T4+ T cells by a complex of the 110 K viral protein and the T4 molecule
    • McDougal, JS, Kennedy, MS, Sligh, JM, Cort, SP, Mawle, A, and Nicholson, JK (1986) Binding of HTLV-III/LAV to T4+ T cells by a complex of the 110 K viral protein and the T4 molecule, Science 231: 382-385
    • (1986) Science , vol.231 , pp. 382-385
    • McDougal, J.S.1    Kennedy, M.S.2    Sligh, J.M.3    Cort, S.P.4    Mawle, A.5    Nicholson, J.K.6
  • 85
    • 0034675886 scopus 로고    scopus 로고
    • Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion
    • Melikyan, GB, Markosyan, RM, Hemmati, H, Delmedico, MK, Lambert, DM, and Cohen, FS (2000) Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion, J Cell Biol 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
  • 86
    • 0035800757 scopus 로고    scopus 로고
    • A novel mechanism of carbohydrate recognition by the C-type lectins DC-SIGN and DC-SIGNR. Subunit organization and binding to multivalent ligands
    • Mitchell, DA, Fadden, AJ, and Drickamer, K (2001) A novel mechanism of carbohydrate recognition by the C-type lectins DC-SIGN and DC-SIGNR. Subunit organization and binding to multivalent ligands, J Biol Chem 276: 28939-45
    • (2001) J Biol Chem , vol.276 , pp. 28939-28945
    • Mitchell, D.A.1    Fadden, A.J.2    Drickamer, K.3
  • 87
    • 0024273639 scopus 로고
    • Binding region for human immunodeficiency virus (HIV) and epitopes for HIV-blocking monoclonal antibodies of the CD4 molecule defined by site-directed mutagenesis
    • Mizukami, T, Fuerst, TR, Berger, EA, and Moss, B (1988) Binding region for human immunodeficiency virus (HIV) and epitopes for HIV-blocking monoclonal antibodies of the CD4 molecule defined by site-directed mutagenesis, Proc Natl Acad Sci U S A 85: 9273-7
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 9273-9277
    • Mizukami, T.1    Fuerst, T.R.2    Berger, E.A.3    Moss, B.4
  • 88
    • 0025374887 scopus 로고
    • Diversity of oligosaccharide structures on the envelope glycoprotein gp120 of human immunodeficiency virus 1 from the lymphoblastoid cell line H9. Presence of complex-type oligosaccharides with bisecting N-acetylglucosamine residues
    • Mizuochi, T, Matthews, TJ, Kato, M, Hamako, J, Titani, K, Solomon, J, and Feizi, T (1990) Diversity of oligosaccharide structures on the envelope glycoprotein gp120 of human immunodeficiency virus 1 from the lymphoblastoid cell line H9. Presence of complex-type oligosaccharides with bisecting N-acetylglucosamine residues, J Biol Chem 265: 8519-24
    • (1990) J Biol Chem , vol.265 , pp. 8519-8524
    • Mizuochi, T.1    Matthews, T.J.2    Kato, M.3    Hamako, J.4    Titani, K.5    Solomon, J.6    Feizi, T.7
  • 89
    • 0027168953 scopus 로고
    • Adaptation of two primary human immunodeficiency virus type 1 isolates to growth in transformed T cell lines correlates with alterations in the responses of their envelope glycoproteins to soluble CD4
    • Moore, JP, Burkly, LC, Connor, RI, Cao, Y, Tizard, R, Ho, DD, and Fisher, RA (1993) Adaptation of two primary human immunodeficiency virus type 1 isolates to growth in transformed T cell lines correlates with alterations in the responses of their envelope glycoproteins to soluble CD4, AIDS Res Hum Retroviruses 9: 529-539
    • (1993) AIDS Res Hum Retroviruses , vol.9 , pp. 529-539
    • Moore, J.P.1    Burkly, L.C.2    Connor, R.I.3    Cao, Y.4    Tizard, R.5    Ho, D.D.6    Fisher, R.A.7
  • 90
    • 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, DE, Picchio, GR, Gulizia, RJ, Sabbe, R, Poignard, P, Picard, L, Offord, RE, Thompson, DA, and Wilken, J (1999) 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 73: 3544-50
    • (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
  • 91
    • 0038065763 scopus 로고    scopus 로고
    • Dilation of the human immunodeficiency virus-1 envelope glycoprotein fusion pore revealed by the inhibitory action of a synthetic peptide from gp41
    • Munoz-Barroso, I, Durell, S, Sakaguchi, K, Appella, E, and Blumenthal, R (1998) 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 140: 315-323
    • (1998) J Cell Biol , vol.140 , pp. 315-323
    • Munoz-Barroso, I.1    Durell, S.2    Sakaguchi, K.3    Appella, E.4    Blumenthal, R.5
  • 95
    • 0026625277 scopus 로고
    • Anti-human immunodeficiency virus activity of a novel synthetic peptide, T22 ([Tyr-5,12, Lys-7]polyphemusin II): A possible inhibitor of virus-cell fusion
    • Nakashima, H, Masuda, M, Murakami, T, Koyanagi, Y, Matsumoto, A, Fujii, N, and Yamamoto, N (1992) Anti-human immunodeficiency virus activity of a novel synthetic peptide, T22 ([Tyr-5,12, Lys-7]polyphemusin II): a possible inhibitor of virus-cell fusion, Antimicrob Agents Chemother 36: 1249-55
    • (1992) Antimicrob Agents Chemother , vol.36 , pp. 1249-1255
    • Nakashima, H.1    Masuda, M.2    Murakami, T.3    Koyanagi, Y.4    Matsumoto, A.5    Fujii, N.6    Yamamoto, N.7
  • 96
    • 0024044173 scopus 로고
    • Genetic analysis of monoclonal antibody and HIV binding sites on the human lymphocyte antigen CD4
    • Peterson, A, and Seed, B (1988) Genetic analysis of monoclonal antibody and HIV binding sites on the human lymphocyte antigen CD4, Cell 54: 65-72
    • (1988) Cell , vol.54 , pp. 65-72
    • Peterson, A.1    Seed, B.2
  • 97
    • 0035202075 scopus 로고    scopus 로고
    • Adaptive mutations in the V3 loop of gp120 enhance fusogenicity of human immunodeficiency virus type 1 and enable use of a CCR5 coreceptor that lacks the amino-terminal sulfated region
    • Platt, EJ, Kuhmann, SE, Rose, PP, and Kabat, D (2001) Adaptive mutations in the V3 loop of gp120 enhance fusogenicity of human immunodeficiency virus type 1 and enable use of a CCR5 coreceptor that lacks the amino-terminal sulfated region, J Virol 75: 12266-78
    • (2001) J Virol , vol.75 , pp. 12266-12278
    • Platt, E.J.1    Kuhmann, S.E.2    Rose, P.P.3    Kabat, D.4
  • 98
    • 0035655108 scopus 로고    scopus 로고
    • DC-SIGN and DC-SIGNR: Helping hands for HIV
    • Pohlmann, S, Baribaud, F, and Doms, RW (2001a) DC-SIGN and DC-SIGNR: helping hands for HIV, Trends Immunol 22: 643-646
    • (2001) Trends Immunol , vol.22 , pp. 643-646
    • Pohlmann, S.1    Baribaud, F.2    Doms, R.W.3
  • 101
  • 103
    • 0033120514 scopus 로고    scopus 로고
    • Chemokine receptor responses on T cells are achieved through regulation of both receptor expression and signaling
    • Rabin, RL, Park, MK, Liao, F, Swofford, R, Stephany, D, and Farber, JM (1999) Chemokine receptor responses on T cells are achieved through regulation of both receptor expression and signaling, J Immunol 162: 3840-50
    • (1999) J Immunol , vol.162 , pp. 3840-3850
    • Rabin, R.L.1    Park, M.K.2    Liao, F.3    Swofford, R.4    Stephany, D.5    Farber, J.M.6
  • 105
    • 0032856713 scopus 로고    scopus 로고
    • Primary human immunodeficiency virus type 2 (HIV-2) isolates infect CD4-negative cells via CCR5 and CXCR4: Comparison with HIV-1 and simian immunodeficiency virus and relevance to cell tropism in vivo
    • Reeves, JD, Hibbitts, S, Simmons, G, McKnight, Azevedo-Pereira, JM, Moniz-Pereira, J, and Clapham, PR (1999) Primary human immunodeficiency virus type 2 (HIV-2) isolates infect CD4-negative cells via CCR5 and CXCR4: Comparison with HIV-1 and simian immunodeficiency virus and relevance to cell tropism in vivo, J Virol 73: 7795-7804
    • (1999) J Virol , vol.73 , pp. 7795-7804
    • Reeves, J.D.1    Hibbitts, S.2    Simmons, G.3    McKnight4    Azevedo-Pereira, J.M.5    Moniz-Pereira, J.6    Clapham, P.R.7
  • 107
    • 0031015211 scopus 로고    scopus 로고
    • The CD4-independent tropism of human immunodeficiency virus type 2 involves several regions of the envelope protein and correlates with a reduced activation threshold for envelope-mediated fusion
    • Reeves, JD, and Schulz, TF (1997) The CD4-independent tropism of human immunodeficiency virus type 2 involves several regions of the envelope protein and correlates with a reduced activation threshold for envelope-mediated fusion, J Virol 71: 1453-1465
    • (1997) J Virol , vol.71 , pp. 1453-1465
    • Reeves, J.D.1    Schulz, T.F.2
  • 108
    • 0035912249 scopus 로고    scopus 로고
    • HIV chemotherapy
    • Richman, DD (2001) HIV chemotherapy, Nature 410: 995-1001
    • (2001) Nature , vol.410 , pp. 995-1001
    • Richman, D.D.1
  • 109
    • 0031883832 scopus 로고    scopus 로고
    • Determinants of human immunodeficiency virus type 1 resistance to gp41-derived inhibitory peptides
    • Rimsky, LT, Shugars, DC, and Matthews, TJ (1998) Determinants of human immunodeficiency virus type 1 resistance to gp41-derived inhibitory peptides, J Virol 72: 986-993
    • (1998) J Virol , vol.72 , pp. 986-993
    • Rimsky, L.T.1    Shugars, D.C.2    Matthews, T.J.3
  • 111
    • 0035793406 scopus 로고    scopus 로고
    • Protein design of an HIV-1 entry inhibitor
    • Root, MJ, Kay, MS, and Kim, PS (2001) Protein design of an HIV-1 entry inhibitor, Science 291: 884-8
    • (2001) Science , vol.291 , pp. 884-888
    • Root, M.J.1    Kay, M.S.2    Kim, P.S.3
  • 112
    • 0033396957 scopus 로고    scopus 로고
    • Fat distribution and metabolic changes in patients with HIV infection
    • Safrin, S, and Grunfeld, C (1999) Fat distribution and metabolic changes in patients with HIV infection, AIDS 13: 2493-505
    • (1999) AIDS , vol.13 , pp. 2493-2505
    • Safrin, S.1    Grunfeld, C.2
  • 114
    • 0025866185 scopus 로고
    • Conformational changes induced in the human immunodeficiency virus envelope glycoprotein by soluble CD4 binding
    • Sattentau, QJ, and Moore, JP (1991) Conformational changes induced in the human immunodeficiency virus envelope glycoprotein by soluble CD4 binding, J Exp Med 174: 407-415
    • (1991) J Exp Med , vol.174 , pp. 407-415
    • Sattentau, Q.J.1    Moore, J.P.2
  • 115
    • 0028999803 scopus 로고
    • Human immunodeficiency virus type 1 neutralization is determined by epitope exposure on the gp120 oligomer
    • Sattentau, QJ, and Moore, JP (1995) Human immunodeficiency virus type 1 neutralization is determined by epitope exposure on the gp120 oligomer, J Exp Med 182: 185-196
    • (1995) J Exp Med , vol.182 , pp. 185-196
    • Sattentau, Q.J.1    Moore, J.P.2
  • 117
    • 0030830661 scopus 로고    scopus 로고
    • Inhibition of T-tropic HIV strains by selective antagonization of the chemokine receptor CXCR4
    • Schols, D, Struyf, S, Van Damme, J, Este, JA, Henson, G, and De Clercq, E (1997) Inhibition of T-tropic HIV strains by selective antagonization of the chemokine receptor CXCR4, J Exp Med 186: 1383-1388
    • (1997) J Exp Med , vol.186 , pp. 1383-1388
    • Schols, D.1    Struyf, S.2    Van Damme, J.3    Este, J.A.4    Henson, G.5    De Clercq, E.6
  • 118
    • 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, Fletcher, CV, Wara, D, Rathore, M, Church, J, DeVille, J, Fenton, T, Graham, B, et al. (2000) 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 182: 1774-9
    • (2000) J Infect Dis , vol.182 , pp. 1774-1779
    • Shearer, W.T.1    Israel, R.J.2    Starr, S.3    Fletcher, C.V.4    Wara, D.5    Rathore, M.6    Church, J.7    DeVille, J.8    Fenton, T.9    Graham, B.10
  • 119
  • 120
    • 0034598903 scopus 로고    scopus 로고
    • DC-SIGN: A guide to some mysteries of dendritic cells
    • Steinman, RM (2000) DC-SIGN: a guide to some mysteries of dendritic cells, Cell 100: 491-4
    • (2000) Cell , vol.100 , pp. 491-494
    • Steinman, R.M.1
  • 121
    • 0035940445 scopus 로고    scopus 로고
    • SCH-C (SCH 351125), an orally bioavailable, small molecule antagonist of the chemokine receptor CCR5, is a potent inhibitor of HIV-1 infection in vitro and in vivo
    • Strizki, JM, Xu, S, Wagner, NE, Wojcik, L, Liu, J, Hou, Y, Endres, M, Palani, A, Shapiro, S, Clader, JW, et al. (2001) SCH-C (SCH 351125), an orally bioavailable, small molecule antagonist of the chemokine receptor CCR5, is a potent inhibitor of HIV-1 infection in vitro and in vivo, Proc Natl Acad Sci U S A 98: 12718-23
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 12718-12723
    • Strizki, J.M.1    Xu, S.2    Wagner, N.E.3    Wojcik, L.4    Liu, J.5    Hou, Y.6    Endres, M.7    Palani, A.8    Shapiro, S.9    Clader, J.W.10
  • 124
    • 0023867450 scopus 로고
    • Soluble CD4 molecules neutralize human immunodeficiency virus type 1
    • Traunecker, A, Luke, W, and Karjalainen, K (1988) Soluble CD4 molecules neutralize human immunodeficiency virus type 1, Nature 331: 84-86
    • (1988) Nature , vol.331 , pp. 84-86
    • Traunecker, A.1    Luke, W.2    Karjalainen, K.3
  • 125
    • 0031812844 scopus 로고    scopus 로고
    • The acquisition of host-encoded proteins by nascent HIV-1
    • Tremblay, MJ, Fortin, JF, and Cantin, R (1998) The acquisition of host-encoded proteins by nascent HIV-1, Immunol Today 19: 346-51
    • (1998) Immunol Today , vol.19 , pp. 346-351
    • Tremblay, M.J.1    Fortin, J.F.2    Cantin, R.3
  • 127
    • 0028865465 scopus 로고
    • Cross-clade neutralization of primary isolates of human immunodeficiency virus type 1 by human monoclonal antibodies and tetrameric CD4-IgG
    • Trkola, A, Pomales, AB, Yuan, H, Korber, B, Maddon, PJ, Allaway, GP, Katinger, H, Barbas, CF, 3rd, Burton, DR, Ho, DD, et al. (1995) Cross-clade neutralization of primary isolates of human immunodeficiency virus type 1 by human monoclonal antibodies and tetrameric CD4-IgG, J Virol 69: 6609-17
    • (1995) J Virol , vol.69 , pp. 6609-6617
    • Trkola, A.1    Pomales, A.B.2    Yuan, H.3    Korber, B.4    Maddon, P.J.5    Allaway, G.P.6    Katinger, H.7    Barbas C.F. III8    Burton, D.R.9    Ho, D.D.10
  • 129
    • 0033771310 scopus 로고    scopus 로고
    • Functional importance of the coiled-coil of the Ebola virus glycoprotein
    • Watanabe, S, Takada, A, Watanabe, T, Ito, H, Kida, H, and Kawaoka, Y (2000) Functional importance of the coiled-coil of the Ebola virus glycoprotein, J Virol 74: 10194-201
    • (2000) J Virol , vol.74 , pp. 10194-10201
    • Watanabe, S.1    Takada, A.2    Watanabe, T.3    Ito, H.4    Kida, H.5    Kawaoka, Y.6
  • 130
    • 0029864284 scopus 로고    scopus 로고
    • Studies of HIV-1 envelope glycoprotein-mediated fusion using a simple fluorescence assay
    • Weiss, CD, Barnett, SW, Cacalano, N, Killeen, N, Littman, DR, and White, JM (1996) Studies of HIV-1 envelope glycoprotein-mediated fusion using a simple fluorescence assay, AIDS 10: 241-6
    • (1996) AIDS , vol.10 , pp. 241-246
    • Weiss, C.D.1    Barnett, S.W.2    Cacalano, N.3    Killeen, N.4    Littman, D.R.5    White, J.M.6
  • 131
    • 0032568634 scopus 로고    scopus 로고
    • The central structural feature of the membrane fusion protein subunit from the Ebola virus glycoprotein is a long triple-stranded coiled coil
    • Weissenhorn, W, Calder, LJ, Wharton, SA, Skehel, JJ, and Wiley, DC (1998) The central structural feature of the membrane fusion protein subunit from the Ebola virus glycoprotein is a long triple-stranded coiled coil, Proc Natl Acad Sci USA 95: 6032-6
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6032-6036
    • Weissenhorn, W.1    Calder, L.J.2    Wharton, S.A.3    Skehel, J.J.4    Wiley, D.C.5
  • 134
    • 0027692502 scopus 로고
    • A synthetic peptide from HIV-1 gp41 is a potent inhibitor of virus-mediated cell-cell fusion
    • Wild, C, Greenwell, T, and Matthews, T (1993) A synthetic peptide from HIV-1 gp41 is a potent inhibitor of virus-mediated cell-cell fusion, AIDS Res Hum Retroviruses 9: 1051-1053
    • (1993) AIDS Res Hum Retroviruses , vol.9 , pp. 1051-1053
    • Wild, C.1    Greenwell, T.2    Matthews, T.3
  • 135
    • 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, and Matthews, T (1992) A synthetic peptide inhibitor of human immunodeficiency virus replication: correlation between solution structure and viral inhibition, Proc Natl Acad Sci USA 89: 10537-10541
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10537-10541
    • Wild, C.1    Oas, T.2    McDanal, C.3    Bolognesi, D.4    Matthews, T.5
  • 137
    • 0033612928 scopus 로고    scopus 로고
    • Transmission of antiretroviral-drug-resistant HIV-1 variants
    • Yerly, S, Kaiser, L, Race, E, Bru, JP, Clavel, F, and Perrin, L (1999) Transmission of antiretroviral-drug-resistant HIV-1 variants, Lancet 354: 729-33
    • (1999) Lancet , vol.354 , pp. 729-733
    • Yerly, S.1    Kaiser, L.2    Race, E.3    Bru, J.P.4    Clavel, F.5    Perrin, L.6
  • 138
    • 0033927570 scopus 로고    scopus 로고
    • Use of inhibitors to evaluate coreceptor usage by simian and simian/human immunodeficiency viruses and human immunodeficiency virus type 2 in primary cells
    • Zhang, Y, Lou, B, Lal, RB, Gettie, A, Marx, PA, and Moore, JP (2000) Use of inhibitors to evaluate coreceptor usage by simian and simian/human immunodeficiency viruses and human immunodeficiency virus type 2 in primary cells, J Virol 74: 6893-6910
    • (2000) J Virol , vol.74 , pp. 6893-6910
    • Zhang, Y.1    Lou, B.2    Lal, R.B.3    Gettie, A.4    Marx, P.A.5    Moore, J.P.6
  • 139
    • 0034984290 scopus 로고    scopus 로고
    • Structural flexibility and functional valence of CD4-IgG2 (PRO 542): Potential for cross-linking human immunodeficiency virus type 1 envelope spikes
    • Zhu, P, Olson, WC, and Roux, KH (2001) Structural flexibility and functional valence of CD4-IgG2 (PRO 542): potential for cross-linking human immunodeficiency virus type 1 envelope spikes, J Virol 75: 6682-6
    • (2001) J Virol , vol.75 , pp. 6682-6686
    • Zhu, P.1    Olson, W.C.2    Roux, K.H.3
  • 140
    • 0032507962 scopus 로고    scopus 로고
    • Function of the chemokine receptor CXCR4 in haematopoiesis and in cerebellar development
    • Zou, YR, Kottmann, AH, Kuroda, M, Taniuchi, I, and Littman, DR (1998) Function of the chemokine receptor CXCR4 in haematopoiesis and in cerebellar development, Nature 393: 595-599
    • (1998) Nature , vol.393 , pp. 595-599
    • Zou, Y.R.1    Kottmann, A.H.2    Kuroda, M.3    Taniuchi, I.4    Littman, D.R.5


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