메뉴 건너뛰기




Volumn 12, Issue 14, 1996, Pages 1305-1313

Characterization of CD4-gp120 activation intermediates during human immunodeficiency virus type 1 syncytium formation

Author keywords

[No Author keywords available]

Indexed keywords

CD4 ANTIGEN; GLYCOPROTEIN GP 120;

EID: 0029793719     PISSN: 08892229     EISSN: None     Source Type: Journal    
DOI: 10.1089/aid.1996.12.1305     Document Type: Article
Times cited : (14)

References (87)
  • 4
    • 0022546877 scopus 로고
    • AIDS retrovirus induced cytopathology: Giant cell formation and involvement of CD4 antigen
    • Lifson JD, Reyes GR, McGrath MG, Stein BS, and Engleman EG: AIDS retrovirus induced cytopathology: Giant cell formation and involvement of CD4 antigen. Science 1986;232:1123-1127.
    • (1986) Science , vol.232 , pp. 1123-1127
    • Lifson, J.D.1    Reyes, G.R.2    McGrath, M.G.3    Stein, B.S.4    Engleman, E.G.5
  • 6
    • 0026555903 scopus 로고
    • HIV interactions with CD4: A continuum of conformations and consequences
    • Eiden LE, and Lifson JD: HIV interactions with CD4: A continuum of conformations and consequences. Immunol Today 1992;13:201-206.
    • (1992) Immunol Today , vol.13 , pp. 201-206
    • Eiden, L.E.1    Lifson, J.D.2
  • 7
    • 0027055318 scopus 로고
    • Synergistic interaction between ligands binding to the CD4 binding site and V3 domain of human immunodeficiency virus type 1 gp120
    • McKeating JA, Cordell J, Dean CJ, and Balfe P: Synergistic interaction between ligands binding to the CD4 binding site and V3 domain of human immunodeficiency virus type 1 gp120. Virology 1992;191:732-742.
    • (1992) Virology , vol.191 , pp. 732-742
    • McKeating, J.A.1    Cordell, J.2    Dean, C.J.3    Balfe, P.4
  • 8
    • 0025866185 scopus 로고
    • Conformational changes induced in the human immunodeficiency virus envelope glycoprotein by soluble CD4 binding
    • Sattentau QJ, and Moore JP: 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
  • 9
    • 85027646578 scopus 로고
    • Receptor-mediated activation events in HIV/SIV viral entry
    • Koff W, Wong-Staal F, and Kennedy RC (Eds.). Marcel Dekker, New York
    • Allan JS: Receptor-mediated activation events in HIV/SIV viral entry. In: AIDS Research Review, Vol. 2. Koff W, Wong-Staal F, and Kennedy RC (Eds.). Marcel Dekker, New York, 1991, pp. 133-156.
    • (1991) AIDS Research Review , vol.2 , pp. 133-156
    • Allan, J.S.1
  • 11
    • 0026656502 scopus 로고
    • Human immunodeficiency virus type 2 infection and fusion CD4-negative human cell lines: Induction and enhancement by soluble CD4
    • Clapham PR, McKnight A, and Weiss RA: Human immunodeficiency virus type 2 infection and fusion CD4-negative human cell lines: induction and enhancement by soluble CD4. J Virol 1992;66:3531-3537.
    • (1992) J Virol , vol.66 , pp. 3531-3537
    • Clapham, P.R.1    McKnight, A.2    Weiss, R.A.3
  • 12
    • 0025066098 scopus 로고
    • CD4-immunoadhesin, but not recombinant soluble CD4, blocks syncytium formation by human immunodeficiency virus type 2-infected lymphoid cells
    • Sekigawa I, Chamow SM, Groopman JE, and Byrn RA: CD4-immunoadhesin, but not recombinant soluble CD4, blocks syncytium formation by human immunodeficiency virus type 2-infected lymphoid cells. J Virol 1990;64:5194-5198.
    • (1990) J Virol , vol.64 , pp. 5194-5198
    • Sekigawa, I.1    Chamow, S.M.2    Groopman, J.E.3    Byrn, R.A.4
  • 15
    • 0025297179 scopus 로고
    • Characterization of the fusion domain of the human immunodeficiency virus type 1 envelope glycoprotein gp41
    • Freed EO, Myers DJ, and Risser R: Characterization of the fusion domain of the human immunodeficiency virus type 1 envelope glycoprotein gp41. Proc Natl Acad Sci USA 1990;87:4650-4654.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4650-4654
    • Freed, E.O.1    Myers, D.J.2    Risser, R.3
  • 16
    • 0023954154 scopus 로고
    • Human immunodeficiency virus infection of CD4-bearing cells occurs by a pH-independent mechanism
    • McClure MO, Marsh M, and Weiss RA: Human immunodeficiency virus infection of CD4-bearing cells occurs by a pH-independent mechanism. EMBO J 1988;7:513-518.
    • (1988) EMBO J , vol.7 , pp. 513-518
    • McClure, M.O.1    Marsh, M.2    Weiss, R.A.3
  • 17
    • 0023737388 scopus 로고
    • Quantitative measurement of fusion between human immunodeficiency virus and cultured cells using membrane fluorescence dequenching
    • Sinangil F, Loyter A, and Volsky DJ: Quantitative measurement of fusion between human immunodeficiency virus and cultured cells using membrane fluorescence dequenching. FEBS Lett 1988;239:88-92.
    • (1988) FEBS Lett , vol.239 , pp. 88-92
    • Sinangil, F.1    Loyter, A.2    Volsky, D.J.3
  • 18
    • 0023644926 scopus 로고
    • pH-independent HIV entry into CD4-positive T cells via virus envelope fusion to the plasma membrane
    • Stein BS, Gowda SD, Lifson JD, Penhallow RC, Bensch KG, and Engleman EG: 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
  • 19
    • 0026543977 scopus 로고
    • Kinetics of soluble CD4 binding to cells expressing human immunodeficiency virus type 1 envelope glycoprotein
    • Dimitrov DS, Hillman K, Manischewitz J, Blumenthal R, and Golding H: Kinetics of soluble CD4 binding to cells expressing human immunodeficiency virus type 1 envelope glycoprotein. J Virol 1992;66:132-138.
    • (1992) J Virol , vol.66 , pp. 132-138
    • Dimitrov, D.S.1    Hillman, K.2    Manischewitz, J.3    Blumenthal, R.4    Golding, H.5
  • 20
    • 0026650992 scopus 로고
    • The human immunodeficiency virus gp120 binding site on CD4: Delineation by quantitative equilibrium and kinetic binding studies of mutants in conjunction with a high-resolution CD4 atomic structure
    • Moebius U, Clayton LK, Abraham S, Harrison SC, and Reinherz EL: The human immunodeficiency virus gp120 binding site on CD4: Delineation by quantitative equilibrium and kinetic binding studies of mutants in conjunction with a high-resolution CD4 atomic structure. J Exp Med 1992;76:507-517.
    • (1992) J Exp Med , vol.76 , pp. 507-517
    • Moebius, U.1    Clayton, L.K.2    Abraham, S.3    Harrison, S.C.4    Reinherz, E.L.5
  • 21
    • 0026625843 scopus 로고
    • Thermodynamic and kinetic analysis of sCD4 binding to HIV-1 virions and of gp120 dissociation
    • Moore JP, Klasse PJ: Thermodynamic and kinetic analysis of sCD4 binding to HIV-1 virions and of gp120 dissociation. AIDS Res Hum Retroviruses 1992;8:443-449.
    • (1992) AIDS Res Hum Retroviruses , vol.8 , pp. 443-449
    • Moore, J.P.1    Klasse, P.J.2
  • 22
    • 0026095929 scopus 로고
    • Effects of changes in gp120-CD4 binding affinity on human immunodeficiency virus type 1 envelope glycoprotein function and soluble CD4 sensitivity
    • Thali M, Olshevsky U, Furman C, Gabuzda D, Li J, and Sodroski J: Effects of changes in gp120-CD4 binding affinity on human immunodeficiency virus type 1 envelope glycoprotein function and soluble CD4 sensitivity. J Virol 1991;65:5007-5012.
    • (1991) J Virol , vol.65 , pp. 5007-5012
    • Thali, M.1    Olshevsky, U.2    Furman, C.3    Gabuzda, D.4    Li, J.5    Sodroski, J.6
  • 23
    • 0027173841 scopus 로고
    • Physicochemical dissociation of CD4-mediated syncytium formation and shedding of human immunodeficiency virus type 1 gp120
    • Fu Y-K, Hart TK, Jonak ZL, and Bugelski PJ: Physicochemical dissociation of CD4-mediated syncytium formation and shedding of human immunodeficiency virus type 1 gp120. J Virol 1993;67:3818-3825.
    • (1993) J Virol , vol.67 , pp. 3818-3825
    • Fu, Y.-K.1    Hart, T.K.2    Jonak, Z.L.3    Bugelski, P.J.4
  • 24
    • 0026611792 scopus 로고
    • Temperature enhancement of syncytium formation by HIV and Sendai virus
    • Kinchington D, Barker W, Galpin S, and Apostolov K: Temperature enhancement of syncytium formation by HIV and Sendai virus. J Med Virol 1992;36:44-48.
    • (1992) J Med Virol , vol.36 , pp. 44-48
    • Kinchington, D.1    Barker, W.2    Galpin, S.3    Apostolov, K.4
  • 25
    • 0026572801 scopus 로고
    • Kinetics of HIV-1 interactions with sCD4 and CD4+ cells: Implications for inhibition of virus infection and initial steps of virus entry into cells
    • Dimitrov DS, Willey RS, Martin MA, and Blumenthal R: Kinetics of HIV-1 interactions with sCD4 and CD4+ cells: Implications for inhibition of virus infection and initial steps of virus entry into cells. Virology 1992;187:398-406.
    • (1992) Virology , vol.187 , pp. 398-406
    • Dimitrov, D.S.1    Willey, R.S.2    Martin, M.A.3    Blumenthal, R.4
  • 27
    • 0025782806 scopus 로고
    • A highly selected panel of anti-CD4 antibodies fails to induce anti-idiotypic antisera mediating human immunodeficiency virus neutralization
    • Healey DG, Dianda L, Buck D, Schroeder K, Truneh A, Sattentau QJ, and Beverley PCL: A highly selected panel of anti-CD4 antibodies fails to induce anti-idiotypic antisera mediating human immunodeficiency virus neutralization. Eur J Immunol 1991;21: 1491-1498.
    • (1991) Eur J Immunol , vol.21 , pp. 1491-1498
    • Healey, D.G.1    Dianda, L.2    Buck, D.3    Schroeder, K.4    Truneh, A.5    Sattentau, Q.J.6    Beverley, P.C.L.7
  • 28
    • 0026047529 scopus 로고
    • A region in domain 1 of CD4 distinct from the primary gp120 binding site is involved in HIV infection and virus-mediated fusion
    • Truneh A, Buck D, Cassatt DR, Juszczak R, Kassis S, Ryu SE, Healey D, Sweet R, and Sattentau Q: A region in domain 1 of CD4 distinct from the primary gp120 binding site is involved in HIV infection and virus-mediated fusion. J Biol Chem 1991;266: 5942-5948.
    • (1991) J Biol Chem , vol.266 , pp. 5942-5948
    • Truneh, A.1    Buck, D.2    Cassatt, D.R.3    Juszczak, R.4    Kassis, S.5    Ryu, S.E.6    Healey, D.7    Sweet, R.8    Sattentau, Q.9
  • 29
    • 14744294919 scopus 로고
    • "Primatization" of recombinant antibodies for immunotherapy of human diseases: A macaque/human chimeric antibody against human CD4
    • Newman R, Alberts J, Anderson D, Camer K, Heard C, Norton F, Raab R, Reff M, Shuey S, and Hanna N: "Primatization" of recombinant antibodies for immunotherapy of human diseases: A macaque/human chimeric antibody against human CD4. Biotechnology 1992;10:1455-1460.
    • (1992) Biotechnology , vol.10 , pp. 1455-1460
    • Newman, R.1    Alberts, J.2    Anderson, D.3    Camer, K.4    Heard, C.5    Norton, F.6    Raab, R.7    Reff, M.8    Shuey, S.9    Hanna, N.10
  • 31
    • 0027404892 scopus 로고
    • Calcium ions are required for cell fusion mediated by the CD4-human immunodeficiency virus type 1 envelope glycoprotein interaction
    • Dimitrov DS, Broder CC, Berger EA, and Blumenthal R: Calcium ions are required for cell fusion mediated by the CD4-human immunodeficiency virus type 1 envelope glycoprotein interaction. J Virol 1993;67:1647-1652.
    • (1993) J Virol , vol.67 , pp. 1647-1652
    • Dimitrov, D.S.1    Broder, C.C.2    Berger, E.A.3    Blumenthal, R.4
  • 33
    • 0023651341 scopus 로고
    • Delineation of a region of the human immunodeficiency virus type 1 gp120 glycoprotein critical for interaction with the CD4 receptor
    • Lasky LA, Nakamura G, Smith DH, Fennie C, Shimasaki C, Patzer E, Berman P, Gregory T, and Capon DJ: Delineation of a region of the human immunodeficiency virus type 1 gp120 glycoprotein critical for interaction with the CD4 receptor. Cell 1987; 50:975-985.
    • (1987) Cell , vol.50 , pp. 975-985
    • Lasky, L.A.1    Nakamura, G.2    Smith, D.H.3    Fennie, C.4    Shimasaki, C.5    Patzer, E.6    Berman, P.7    Gregory, T.8    Capon, D.J.9
  • 34
    • 0028177807 scopus 로고
    • Structures of an HIV and MHC binding fragment from human CD4 as refined in two crystal lattices
    • Ryu SE, Truneh A, Sweet RW, and Hendrickson WA: Structures of an HIV and MHC binding fragment from human CD4 as refined in two crystal lattices. Structure 1994;2:59-74.
    • (1994) Structure , vol.2 , pp. 59-74
    • Ryu, S.E.1    Truneh, A.2    Sweet, R.W.3    Hendrickson, W.A.4
  • 35
    • 0026714751 scopus 로고
    • Analysis of HIV-induced autoantibodies to cryptic epitopes on human CD4
    • Callahan LN, Roderiquez G, Mallinson M, and Norcross MA: Analysis of HIV-induced autoantibodies to cryptic epitopes on human CD4. J Immunol 1992;149:2194-2202.
    • (1992) J Immunol , vol.149 , pp. 2194-2202
    • Callahan, L.N.1    Roderiquez, G.2    Mallinson, M.3    Norcross, M.A.4
  • 37
    • 0027488547 scopus 로고
    • Conformational changes induced in the envelope glycoproieins of the human and simian immunodeficiency viruses by soluble receptor binding
    • Sattentau QJ, Moore JP, Vignaux F, Traincard F, and Poignard P: Conformational changes induced in the envelope glycoproieins of the human and simian immunodeficiency viruses by soluble receptor binding. J Virol 1993;67:7383-7393.
    • (1993) J Virol , vol.67 , pp. 7383-7393
    • Sattentau, Q.J.1    Moore, J.P.2    Vignaux, F.3    Traincard, F.4    Poignard, P.5
  • 38
    • 0026729485 scopus 로고
    • Localized conformational changes in the N-terminal domain of CD4 identified in competitive binding assay of monoclonal antibodies and HIV-1 envelope glycoprotein
    • Walker L, Wilks D, O'Brien J, Habeshaw J, and Dalgleish A: Localized conformational changes in the N-terminal domain of CD4 identified in competitive binding assay of monoclonal antibodies and HIV-1 envelope glycoprotein. AIDS Res Hum Retroviruses 1992;8:1083-1090.
    • (1992) AIDS Res Hum Retroviruses , vol.8 , pp. 1083-1090
    • Walker, L.1    Wilks, D.2    O'Brien, J.3    Habeshaw, J.4    Dalgleish, A.5
  • 39
    • 0027236481 scopus 로고
    • Identification of a neutralizing epitope conformationally affected by the attachment of CD4 to gp120
    • Kang CY, Hariharan K, Posner MR, and Nara P: Identification of a neutralizing epitope conformationally affected by the attachment of CD4 to gp120. J Immunol 1993;151:449-457.
    • (1993) J Immunol , vol.151 , pp. 449-457
    • Kang, C.Y.1    Hariharan, K.2    Posner, M.R.3    Nara, P.4
  • 41
    • 0027261552 scopus 로고
    • Conformational changes affecting the V3 and CD4-binding domains of human immunodeficiency virus type 1 gp120 associated with env processing and with binding of ligands to these sites
    • Pinter A, Honnen WJ, and Tilley SA: Conformational changes affecting the V3 and CD4-binding domains of human immunodeficiency virus type 1 gp120 associated with env processing and with binding of ligands to these sites. J Virol 1993;67:5692-5697.
    • (1993) J Virol , vol.67 , pp. 5692-5697
    • Pinter, A.1    Honnen, W.J.2    Tilley, S.A.3
  • 42
    • 0028017515 scopus 로고
    • Inhibitors of the conformational switch involved in CD4 binding and by the env glycoprotein from human immunodeficiency virus type 1
    • Reed J, and Kinzel V: Inhibitors of the conformational switch involved in CD4 binding and by the env glycoprotein from human immunodeficiency virus type 1. Biochemistry 1994;33: 10993-10998.
    • (1994) Biochemistry , vol.33 , pp. 10993-10998
    • Reed, J.1    Kinzel, V.2
  • 43
    • 0027256814 scopus 로고
    • Characterization of conserved human immunodeficiency virus type 1 gp120 neutralization epitopes exposed upon gp120-CD4 binding
    • Thali M, Moore JP, Furman C, Charles M, Ho DD, Robinson J, and Sodroski J: Characterization of conserved human immunodeficiency virus type 1 gp120 neutralization epitopes exposed upon gp120-CD4 binding. J Virol 1992;67:3978-3988.
    • (1992) J Virol , vol.67 , pp. 3978-3988
    • Thali, M.1    Moore, J.P.2    Furman, C.3    Charles, M.4    Ho, D.D.5    Robinson, J.6    Sodroski, J.7
  • 44
    • 0023371134 scopus 로고
    • Effects of mutations in three domains of the vesicular stomatitis viral glycoprotein on its lateral diffusion in the plasma membrane
    • Scullion BF, Hou Y, Puddington L, Rose JK, and Jacobson K: Effects of mutations in three domains of the vesicular stomatitis viral glycoprotein on its lateral diffusion in the plasma membrane. J Cell Biol 1987;105:69-75.
    • (1987) J Cell Biol , vol.105 , pp. 69-75
    • Scullion, B.F.1    Hou, Y.2    Puddington, L.3    Rose, J.K.4    Jacobson, K.5
  • 45
    • 0026528045 scopus 로고
    • Tracking of cell surface receptors by fluorescence digital imaging microscopy using a charge-coupled device camera. Low-density lipoprotein and influenza virus receptor mobility at 4°C
    • Anderson CM, Georgiou GN, Morrison IEG, Stevenson GYW, and Cherry RJ: Tracking of cell surface receptors by fluorescence digital imaging microscopy using a charge-coupled device camera. Low-density lipoprotein and influenza virus receptor mobility at 4°C. J Cell Sci 1992;101:415-125.
    • (1992) J Cell Sci , vol.101 , pp. 415-1125
    • Anderson, C.M.1    Georgiou, G.N.2    Morrison, I.E.G.3    Stevenson, G.Y.W.4    Cherry, R.J.5
  • 46
    • 0022371883 scopus 로고    scopus 로고
    • The activation of the human neutrophil respiratory burst occurs only at temperatures above 17°C: Evidence that activation requires membrane fusion
    • Manara FS, and Schneider DL: The activation of the human neutrophil respiratory burst occurs only at temperatures above 17°C: Evidence that activation requires membrane fusion. Biochem Biophys Res Commun 132:696-701.
    • Biochem Biophys Res Commun , vol.132 , pp. 696-701
    • Manara, F.S.1    Schneider, D.L.2
  • 47
    • 0019256559 scopus 로고
    • Adsorptive endocytosis of Semliki Forest virus
    • 1980
    • Marsh M, and Helenius A: 1980. Adsorptive endocytosis of Semliki Forest virus. J Mol Biol 1980;142:439-454.
    • (1980) J Mol Biol , vol.142 , pp. 439-454
    • Marsh, M.1    Helenius, A.2
  • 49
    • 0025998524 scopus 로고
    • A novel membrane bound serine esterase in human T4(+)-lymphocytes is a binding protein of envelope glycoprotein gp120 of HIV-1
    • Kido H, Fukutomi A, and Katunuma N: A novel membrane bound serine esterase in human T4(+)-lymphocytes is a binding protein of envelope glycoprotein gp120 of HIV-1. Biomed Biochim Acta 1991;50:781-789.
    • (1991) Biomed Biochim Acta , vol.50 , pp. 781-789
    • Kido, H.1    Fukutomi, A.2    Katunuma, N.3
  • 50
    • 0028103736 scopus 로고
    • Conformational rearrangements required of the V3 loop of HIV-1 gp120 for proteolytic cleavage and infection
    • Johnson ME, Lin Z, Padmanabhan K, Tulinsky A, and Kahn M: Conformational rearrangements required of the V3 loop of HIV-1 gp120 for proteolytic cleavage and infection. FEBS Lett 1994;337:4-8.
    • (1994) FEBS Lett , vol.337 , pp. 4-8
    • Johnson, M.E.1    Lin, Z.2    Padmanabhan, K.3    Tulinsky, A.4    Kahn, M.5
  • 51
    • 0027471180 scopus 로고
    • Human immunodeficiency virus Type 1 envelope gp120 is cleaved after incubation with recombinant soluble CD4
    • Werner A, and Levy JA: Human immunodeficiency virus Type 1 envelope gp120 is cleaved after incubation with recombinant soluble CD4. J Virol 1990;67:2566-2574.
    • (1990) J Virol , vol.67 , pp. 2566-2574
    • Werner, A.1    Levy, J.A.2
  • 52
    • 0027283312 scopus 로고
    • The block to HIV-1 envelope glycoprotein-mediated membrane fusion in animal cells expressing human CD4 can be overcome by a human cell component(s)
    • Broder CC, Dimitrov DS, Blumenthal R, and Berger EA: The block to HIV-1 envelope glycoprotein-mediated membrane fusion in animal cells expressing human CD4 can be overcome by a human cell component(s). Virology 1993;193:483-491.
    • (1993) Virology , vol.193 , pp. 483-491
    • Broder, C.C.1    Dimitrov, D.S.2    Blumenthal, R.3    Berger, E.A.4
  • 53
    • 0026709705 scopus 로고
    • Inhibition of HIV infection by a novel CD4 domain 2 specific antibody. Dissecting the basis for its inhibitory effect on HIV-induced cell fusion
    • Burkly LC, Olson D, Shapiro R, Winkler G, Rosa JJ, Thomas DW, Williams C, and Chisolm P: Inhibition of HIV infection by a novel CD4 domain 2 specific antibody. Dissecting the basis for its inhibitory effect on HIV-induced cell fusion. J Immunol 1992; 149:1779-1787.
    • (1992) J Immunol , vol.149 , pp. 1779-1787
    • Burkly, L.C.1    Olson, D.2    Shapiro, R.3    Winkler, G.4    Rosa, J.J.5    Thomas, D.W.6    Williams, C.7    Chisolm, P.8
  • 54
    • 0028180240 scopus 로고
    • Adhesion mediated by intracellular adhesion molecule 1 attenuates the potency of antibodies that block HIV-1 gp160-dependent syncytium formation
    • Berman PW, and Nakamura GR: Adhesion mediated by intracellular adhesion molecule 1 attenuates the potency of antibodies that block HIV-1 gp160-dependent syncytium formation. AIDS Res Hum Retroviruses 1994;10:585-593.
    • (1994) AIDS Res Hum Retroviruses , vol.10 , pp. 585-593
    • Berman, P.W.1    Nakamura, G.R.2
  • 55
    • 0027968631 scopus 로고
    • Intercellular adhesion molecules (ICAM)-1 ICAM-2 and ICAM-3 function as counter-receptors for lymphocytes function molecule 1 in human immunodeficiency virus-mediated syncytia formation
    • Butini L, De Fougerolles AR, Vaccarezza M, Graziosi C, Cohen DI, Montroni M, Springer TA, Pantaleo G, and Fauci AS: Intercellular adhesion molecules (ICAM)-1 ICAM-2 and ICAM-3 function as counter-receptors for lymphocytes function molecule 1 in human immunodeficiency virus-mediated syncytia formation. Eur J Immunol 1994;24:2191-2195.
    • (1994) Eur J Immunol , vol.24 , pp. 2191-2195
    • Butini, L.1    De Fougerolles, A.R.2    Vaccarezza, M.3    Graziosi, C.4    Cohen, D.I.5    Montroni, M.6    Springer, T.A.7    Pantaleo, G.8    Fauci, A.S.9
  • 56
    • 0026673995 scopus 로고
    • LFA-1 adhesion molecules are not involved in the early stages of HIV-1 env-mediated cell membrane fusion
    • Golding H, Dimitrov DS, and Blumenthal R: LFA-1 adhesion molecules are not involved in the early stages of HIV-1 env-mediated cell membrane fusion. AIDS Res Hum Retroviruses 1992;8: 1593-1598.
    • (1992) AIDS Res Hum Retroviruses , vol.8 , pp. 1593-1598
    • Golding, H.1    Dimitrov, D.S.2    Blumenthal, R.3
  • 57
    • 0025835141 scopus 로고
    • Functional epitope analysis of the human CD11a/CD18 molecule (LFA-1, lymphocyte function associates antigen 1) involved in HIV-1-induced syncytium formation
    • Vermot-Desroches C, Rigal D, Escaich S, Bernaud J, Pichoud C, Lamelin JP, and Trepo C: Functional epitope analysis of the human CD11a/CD18 molecule (LFA-1, lymphocyte function associates antigen 1) involved in HIV-1-induced syncytium formation. Scand J Imrnunol 1991;34:461-470.
    • (1991) Scand J Imrnunol , vol.34 , pp. 461-470
    • Vermot-Desroches, C.1    Rigal, D.2    Escaich, S.3    Bernaud, J.4    Pichoud, C.5    Lamelin, J.P.6    Trepo, C.7
  • 58
    • 0026318326 scopus 로고
    • HIV-induced syncytia formation requires the formation of conjugates between virus-infected and uninfected T-cells in vitro
    • Busso M, Thornwaite J, and Resnick L: HIV-induced syncytia formation requires the formation of conjugates between virus-infected and uninfected T-cells in vitro. AIDS 1991;5:1425-1432.
    • (1991) AIDS , vol.5 , pp. 1425-1432
    • Busso, M.1    Thornwaite, J.2    Resnick, L.3
  • 59
    • 0028095165 scopus 로고
    • The prevention of cell adhesion and the cell-to-cell spread of HIV-1 in vitro by the alpha-glucosidase 1 inhibitor, 6-O-butanoyl catanospermine (MDL 28574)
    • Bridges CG, Brennan TM, Taylor DL, McPherson M, and Tyms AS: The prevention of cell adhesion and the cell-to-cell spread of HIV-1 in vitro by the alpha-glucosidase 1 inhibitor, 6-O-butanoyl catanospermine (MDL 28574). Antiviral Res 1994;25:169-175.
    • (1994) Antiviral Res , vol.25 , pp. 169-175
    • Bridges, C.G.1    Brennan, T.M.2    Taylor, D.L.3    McPherson, M.4    Tyms, A.S.5
  • 60
    • 0027993531 scopus 로고
    • Factors involved in the entry of human immunodeficiency virus type 1 into permissive cells: Lack of evidence of a role for CD26
    • Lazaro I, Naniche D, Signoret N, Bernard AM, Marguet D, Klantmann D, Dragic T, Alizon M, and Sattentau Q: Factors involved in the entry of human immunodeficiency virus type 1 into permissive cells: Lack of evidence of a role for CD26. J Virol 1994;68:6535-6546.
    • (1994) J Virol , vol.68 , pp. 6535-6546
    • Lazaro, I.1    Naniche, D.2    Signoret, N.3    Bernard, A.M.4    Marguet, D.5    Klantmann, D.6    Dragic, T.7    Alizon, M.8    Sattentau, Q.9
  • 61
    • 0025342405 scopus 로고
    • Effects of an engineered disulfide bond on the folding of T4 lysozyme at low temperatures
    • Anderson WD, Fink AL, Perry LJ, and Wetzel R: Effects of an engineered disulfide bond on the folding of T4 lysozyme at low temperatures. Biochemistry 1990;29:3331-3337.
    • (1990) Biochemistry , vol.29 , pp. 3331-3337
    • Anderson, W.D.1    Fink, A.L.2    Perry, L.J.3    Wetzel, R.4
  • 62
    • 0021840415 scopus 로고
    • Temperature dependence of the rate constants of the Escherichia coli RNA polymerase-lambda PR promoter interaction. Assignment of the kinetics steps corresponding to protein conformational changes and DNA opening
    • Roe JH, Burgess RR, and Record MT Jr: Temperature dependence of the rate constants of the Escherichia coli RNA polymerase-lambda PR promoter interaction. Assignment of the kinetics steps corresponding to protein conformational changes and DNA opening. J Mol Biol 1985;184:441-453.
    • (1985) J Mol Biol , vol.184 , pp. 441-453
    • Roe, J.H.1    Burgess, R.R.2    Record Jr., M.T.3
  • 63
    • 0022511857 scopus 로고
    • Agonist induced isomerization of the alpha 1-adrenergic receptor: Kinetic analysis using broken-cell and solubilized preparations
    • Schwarz KR, Lanier SM, Sena LM, Carter EA, Graham RM, and Homey CJ: Agonist induced isomerization of the alpha 1-adrenergic receptor: Kinetic analysis using broken-cell and solubilized preparations. Biochemistry 1986;25:2697-2702.
    • (1986) Biochemistry , vol.25 , pp. 2697-2702
    • Schwarz, K.R.1    Lanier, S.M.2    Sena, L.M.3    Carter, E.A.4    Graham, R.M.5    Homey, C.J.6
  • 64
    • 0024970988 scopus 로고
    • Conformational stability and mechanism of folding of ribonucleasee T1
    • Thomson JA, Shirley BA, Grimsley GR, and Pace CN: Conformational stability and mechanism of folding of ribonucleasee T1. J Biol Chem 1989;264:11614-11620.
    • (1989) J Biol Chem , vol.264 , pp. 11614-11620
    • Thomson, J.A.1    Shirley, B.A.2    Grimsley, G.R.3    Pace, C.N.4
  • 65
    • 0024314434 scopus 로고
    • Conformation and stability of Sendai virus fusion protein
    • Barnes JA: Conformation and stability of Sendai virus fusion protein. Int J Biol Macromol 1989;11:130-136.
    • (1989) Int J Biol Macromol , vol.11 , pp. 130-136
    • Barnes, J.A.1
  • 66
    • 0028915080 scopus 로고
    • Identification of a membrane fusion domain and an oligomerization domain in the baculovirus GP64 envelope fusion protein
    • Monsma SA, and Blissard GW: Identification of a membrane fusion domain and an oligomerization domain in the baculovirus GP64 envelope fusion protein. J Virol 1995;69:2583-2595.
    • (1995) J Virol , vol.69 , pp. 2583-2595
    • Monsma, S.A.1    Blissard, G.W.2
  • 67
    • 0025940737 scopus 로고
    • A Golgi retention signal in a membrane-spanning domain of corona virus El protein
    • Swift AM, and Chamer CE: A Golgi retention signal in a membrane-spanning domain of corona virus El protein. J Cell Biol 1991;115:19-30.
    • (1991) J Cell Biol , vol.115 , pp. 19-30
    • Swift, A.M.1    Chamer, C.E.2
  • 68
    • 0025369546 scopus 로고
    • Conformation of membrane fusion-active 20-residue peptides with or without lipid bilayers. Implication of alpha-helix formation for membrane fusion
    • Takahashi S: Conformation of membrane fusion-active 20-residue peptides with or without lipid bilayers. Implication of alpha-helix formation for membrane fusion. Biochemistry 1990;29: 6257-6264.
    • (1990) Biochemistry , vol.29 , pp. 6257-6264
    • Takahashi, S.1
  • 69
    • 0026743982 scopus 로고
    • The amino-terminal peptide of HIV-1 glycoprotein 41 interacts with human erythrocyte membranes: Peptide conformation, orientation and aggregation
    • Gordon LM, Curtain CC, Zhong YC, Kirkpatrick A, Mobley PW, and Waring AJ: The amino-terminal peptide of HIV-1 glycoprotein 41 interacts with human erythrocyte membranes: peptide conformation, orientation and aggregation. Biochim Biophys Acta 1992;1139:257-274.
    • (1992) Biochim Biophys Acta , vol.1139 , pp. 257-274
    • Gordon, L.M.1    Curtain, C.C.2    Zhong, Y.C.3    Kirkpatrick, A.4    Mobley, P.W.5    Waring, A.J.6
  • 71
    • 0028813111 scopus 로고
    • Determinants of human immunodeficiency virus type 1 envelope glycoprotein oligomeric structure
    • Poumbourios P, el Ahmar W, McPhee DA, and Kemp BE: Determinants of human immunodeficiency virus type 1 envelope glycoprotein oligomeric structure. J Virol 1995;69:1209-1218.
    • (1995) J Virol , vol.69 , pp. 1209-1218
    • Poumbourios, P.1    El Ahmar, W.2    McPhee, D.A.3    Kemp, B.E.4
  • 73
    • 0026505142 scopus 로고
    • Fusogenic segments of bovine leukemia virus and simian immunodeficiency virus are interchangeable and mediated fusion by means of oblique insertion in the lipid bilayer of their target cells
    • Voneche V, Portelle D, Kettmann R, Willems L, Limbach K, Paoletti E, Ruysschaert JM, Burny A, and Brasseur R: Fusogenic segments of bovine leukemia virus and simian immunodeficiency virus are interchangeable and mediated fusion by means of oblique insertion in the lipid bilayer of their target cells. Proc Natl Acad Sci USA 1992;89:3810-3814.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 3810-3814
    • Voneche, V.1    Portelle, D.2    Kettmann, R.3    Willems, L.4    Limbach, K.5    Paoletti, E.6    Ruysschaert, J.M.7    Burny, A.8    Brasseur, R.9
  • 74
    • 0026570397 scopus 로고
    • Evidence that the stalk of Drosophila kinesin heavy chain is an alpha-helical coiled coil
    • de Cuevas M, Tao T, and Goldstein LS: Evidence that the stalk of Drosophila kinesin heavy chain is an alpha-helical coiled coil. J Cell Biol 1992;116:957-965.
    • (1992) J Cell Biol , vol.116 , pp. 957-965
    • De Cuevas, M.1    Tao, T.2    Goldstein, L.S.3
  • 75
    • 0027146350 scopus 로고
    • Conformation of thymosin beta 4 in water determined by NMR spectroscopy
    • Czisch M, Schleicher M, Harger S, Voelter W, and Holak TA: Conformation of thymosin beta 4 in water determined by NMR spectroscopy. Eur J Biochem 1993;218:335-344.
    • (1993) Eur J Biochem , vol.218 , pp. 335-344
    • Czisch, M.1    Schleicher, M.2    Harger, S.3    Voelter, W.4    Holak, T.A.5
  • 76
    • 0028351682 scopus 로고
    • Conformation-dependent platelet adhesion to collagen involving integrin alpha 2 beta 1-mediated and other mechanisms: Multiple alpha 2 beta 1-recognition sites in collagen type 1
    • Morton LF, Peachey AR, Zijenah LS, Godall AH, Humphries MJ, and Barnes MJ: Conformation-dependent platelet adhesion to collagen involving integrin alpha 2 beta 1-mediated and other mechanisms: multiple alpha 2 beta 1-recognition sites in collagen type 1. Biochem J 1994;299:791-797.
    • (1994) Biochem J , vol.299 , pp. 791-797
    • Morton, L.F.1    Peachey, A.R.2    Zijenah, L.S.3    Godall, A.H.4    Humphries, M.J.5    Barnes, M.J.6
  • 77
    • 0022497957 scopus 로고
    • Kinetics and extent of fusion between Sendai virus and erythrocyte ghosts: Application of a mass action kinetic model
    • Nir S, Klappe K, and Hoekstra D: Kinetics and extent of fusion between Sendai virus and erythrocyte ghosts: Application of a mass action kinetic model. Biochemistry 1986;25:2155-2166.
    • (1986) Biochemistry , vol.25 , pp. 2155-2166
    • Nir, S.1    Klappe, K.2    Hoekstra, D.3
  • 79
    • 0025913151 scopus 로고
    • Stimulation of glycoprotein gp120 dissociation from the envelope glycoprotein complex of human immunodeficiency virus type 1 by soluble CD4 and CD4 peptide derivatives: Implications for the role of the complementarity-determining region 3-like region in membrane fusion
    • Berger EA, Lifson JD, and Eiden LE: Stimulation of glycoprotein gp120 dissociation from the envelope glycoprotein complex of human immunodeficiency virus type 1 by soluble CD4 and CD4 peptide derivatives: Implications for the role of the complementarity-determining region 3-like region in membrane fusion. Proc Natl Acad Sci USA 1991;88:8082-8086.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 8082-8086
    • Berger, E.A.1    Lifson, J.D.2    Eiden, L.E.3
  • 80
    • 0026011315 scopus 로고
    • Binding of soluble CD4 proteins to human immunodeficiency virus type 1 and infected cells induces release of envelope glycoprotein gp120
    • Hart TK, Kirsh R, Ellens H, Sweet RW, Lambert DM, Petteway SR, Leary J, and Bugelski PJ: Binding of soluble CD4 proteins to human immunodeficiency virus type 1 and infected cells induces release of envelope glycoprotein gp120. Proc Natl Acad Sci USA 1991;88:2189-2193.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 2189-2193
    • Hart, T.K.1    Kirsh, R.2    Ellens, H.3    Sweet, R.W.4    Lambert, D.M.5    Petteway, S.R.6    Leary, J.7    Bugelski, P.J.8
  • 82
    • 0025572710 scopus 로고
    • Dissociation of gp120 from HIV-1 virions induced by soluble CD4
    • Moore JP, McKeating JA, Weiss RA, and Sattentau QJ: Dissociation of gp120 from HIV-1 virions induced by soluble CD4. Science 1990;250:1139-1142.
    • (1990) Science , vol.250 , pp. 1139-1142
    • Moore, J.P.1    McKeating, J.A.2    Weiss, R.A.3    Sattentau, Q.J.4
  • 83
    • 0026786630 scopus 로고
    • High level of surface CD4 prevents stable human immunodeficiency virus infection of T-cell transfectants
    • Marshall WL, Diamond DC, Kowalski MM, and Finberg RW: High level of surface CD4 prevents stable human immunodeficiency virus infection of T-cell transfectants. J Virol 1992;66: 5492-5499.
    • (1992) J Virol , vol.66 , pp. 5492-5499
    • Marshall, W.L.1    Diamond, D.C.2    Kowalski, M.M.3    Finberg, R.W.4
  • 84
    • 0026792879 scopus 로고
    • Lack of correlation between soluble CD4-induced shedding of the human immunodeficiency virus type 1 exterior envelope glycoprotein and subsequent membrane fusion events
    • Thali M, Furman C, Helseth E, Repke H, and Sodroski J: Lack of correlation between soluble CD4-induced shedding of the human immunodeficiency virus type 1 exterior envelope glycoprotein and subsequent membrane fusion events. J Virol 1992;66:5516-5524.
    • (1992) J Virol , vol.66 , pp. 5516-5524
    • Thali, M.1    Furman, C.2    Helseth, E.3    Repke, H.4    Sodroski, J.5
  • 85
    • 0028851288 scopus 로고
    • Temperature dependence of cell-cell fusion by the envelope glycoprotein of human immunodeficiency virus type 1
    • Frey S, Marsh M, Gunther S, Pelchen-Matthews A, Stevens P, Ortlepp S, and Stegman T: Temperature dependence of cell-cell fusion by the envelope glycoprotein of human immunodeficiency virus type 1. J Virol 1995;69:1462-1472.
    • (1995) J Virol , vol.69 , pp. 1462-1472
    • Frey, S.1    Marsh, M.2    Gunther, S.3    Pelchen-Matthews, A.4    Stevens, P.5    Ortlepp, S.6    Stegman, T.7
  • 86
    • 0026611884 scopus 로고
    • Kinetic modeling of Sendai virus fusion with PC-12 cells. Effect of pH and temperature on fusion and viral inactivation
    • Pedroso de Lima MC, Ramalho-Santos J, Martins MF, Pato de Carvalho A, Bairs V, and Nir S: Kinetic modeling of Sendai virus fusion with PC-12 cells. Effect of pH and temperature on fusion and viral inactivation. Eur J Biochem 1992;205:181-186.
    • (1992) Eur J Biochem , vol.205 , pp. 181-186
    • Pedroso De Lima, M.C.1    Ramalho-Santos, J.2    Martins, M.F.3    Pato De Carvalho, A.4    Bairs, V.5    Nir, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.