메뉴 건너뛰기




Volumn 14, Issue 5, 1998, Pages 385-392

Efficacy of fusion peptide homologs in blocking cell lysis and HIV- induced fusion

Author keywords

[No Author keywords available]

Indexed keywords

APOLIPOPROTEIN A1; GLYCOPROTEIN GP 41; HYBRID PROTEIN; PHENYLALANINE;

EID: 0032549632     PISSN: 08892229     EISSN: None     Source Type: Journal    
DOI: 10.1089/aid.1998.14.385     Document Type: Article
Times cited : (10)

References (34)
  • 4
    • 0024316282 scopus 로고
    • A syncytia assay for human immunodeficiency virus type-I (HIV-I) envelope protein and its use in studying HIV-I mutations
    • Felser J, Klimkait T, and Silver J: A syncytia assay for human immunodeficiency virus type-I (HIV-I) envelope protein and its use in studying HIV-I mutations. Virology 1989;170:566-570.
    • (1989) Virology , vol.170 , pp. 566-570
    • Felser, J.1    Klimkait, T.2    Silver, J.3
  • 5
    • 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
  • 6
    • 0025050505 scopus 로고
    • Phospholipid interactions of synthetic peptides representing the N-terminus of HIV-gp41
    • Rafalski M, Lear JD, and DeGrado WF: Phospholipid interactions of synthetic peptides representing the N-terminus of HIV-gp41. Biochemistry 1990;9:7917-7922.
    • (1990) Biochemistry , vol.9 , pp. 7917-7922
    • Rafalski, M.1    Lear, J.D.2    DeGrado, W.F.3
  • 7
    • 0344021513 scopus 로고
    • Interaction of the HIV-1 fusion peptide with phospholipid vesicles: Different structural requirements for fusion and leakage
    • Nieva JL, Nir S, Muga A, Goni FM, and Wilschut J: Interaction of the HIV-1 fusion peptide with phospholipid vesicles: Different structural requirements for fusion and leakage. Biochemistry 1994;29:7917-7922.
    • (1994) Biochemistry , vol.29 , pp. 7917-7922
    • Nieva, J.L.1    Nir, S.2    Muga, A.3    Goni, F.M.4    Wilschut, J.5
  • 12
    • 0026743982 scopus 로고
    • The amino terminal peptide of HIV-1 glycoprotein 41 interacts with human erythrocyte membranes: Peptide confermation, 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 confermation, 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
  • 14
    • 0003803058 scopus 로고
    • Hafner K, Lehn J-M, Rees CW, von Raqué Schleyer P, Trost BM, and Zahradnik R, eds.. Springer-Verlag, Berlin
    • Bodanszky M and Bodanszky A: In: The Practice of Peptide Synthesis. (Hafner K, Lehn J-M, Rees CW, von Raqué Schleyer P, Trost BM, and Zahradnik R, eds.). Springer-Verlag, Berlin, 1984, p. 125.
    • (1984) The Practice of Peptide Synthesis , pp. 125
    • Bodanszky, M.1    Bodanszky, A.2
  • 15
    • 0027600318 scopus 로고
    • A gentle method for linking TRIS to amino acids and peptides
    • Whittaker RG, Hayes PJ, and Bender VJ: A gentle method for linking TRIS to amino acids and peptides. Peptide Res 1993;6: 125-128.
    • (1993) Peptide Res , vol.6 , pp. 125-128
    • Whittaker, R.G.1    Hayes, P.J.2    Bender, V.J.3
  • 16
    • 0018369993 scopus 로고
    • Lipid asymmetry in membranes
    • Op den Kamp JF: Lipid asymmetry in membranes. Annu Rev Biochem 1979;48:47-71.
    • (1979) Annu Rev Biochem , vol.48 , pp. 47-71
    • Op Den Kamp, J.F.1
  • 17
    • 0019802745 scopus 로고
    • Type C virus particles in a cord T-cell line derived by cocultivating normal cord leukocytes and human leukaemic T-cells
    • Miyoshi I, Kubonishi I, Yoshimoto S, Akagi T, Ohtsuki Y, Shiraishi Y, Nagata K, and Himuna Y: Type C virus particles in a cord T-cell line derived by cocultivating normal cord leukocytes and human leukaemic T-cells. Nature (London) 1981;294:770-771.
    • (1981) Nature (London) , vol.294 , pp. 770-771
    • Miyoshi, I.1    Kubonishi, I.2    Yoshimoto, S.3    Akagi, T.4    Ohtsuki, Y.5    Shiraishi, Y.6    Nagata, K.7    Himuna, Y.8
  • 18
    • 0025124112 scopus 로고
    • Kinetics of HIV-1 replication and intracellular accumulation of particles in HTLV-1 transformed cells
    • Kieman R, Marshall J, Bowers R, Doherty RR, and McPhee DA: Kinetics of HIV-1 replication and intracellular accumulation of particles in HTLV-1 transformed cells. AIDS Res Hum Retroviruses 1990;6:743-752.
    • (1990) AIDS Res Hum Retroviruses , vol.6 , pp. 743-752
    • Kieman, R.1    Marshall, J.2    Bowers, R.3    Doherty, R.R.4    McPhee, D.A.5
  • 19
    • 0023692399 scopus 로고
    • Quantitation of infectious human immunodeficiency virus using a modified plaque forming assay
    • Kiernan RE, McPhee DA, and Doherty RR: Quantitation of infectious human immunodeficiency virus using a modified plaque forming assay. J Virol Methods 1988;22:303-308.
    • (1988) J Virol Methods , vol.22 , pp. 303-308
    • Kiernan, R.E.1    McPhee, D.A.2    Doherty, R.R.3
  • 20
    • 0026581293 scopus 로고
    • Synthesis of human immunodeficiency virus DNA in a cell-to-cell transmission model
    • Li P and Burrell C: Synthesis of human immunodeficiency virus DNA in a cell-to-cell transmission model. AIDS Res Hum Retroviruses 1992;8:253-259.
    • (1992) AIDS Res Hum Retroviruses , vol.8 , pp. 253-259
    • Li, P.1    Burrell, C.2
  • 21
    • 0024595042 scopus 로고
    • Re-examination and further development of a precise and rapid dye method for measuring cell growth/cell killing
    • Hansen MB, Nielson SE, and Berg K: Re-examination and further development of a precise and rapid dye method for measuring cell growth/cell killing. J Immunol Methods 1989;119:203-210.
    • (1989) J Immunol Methods , vol.119 , pp. 203-210
    • Hansen, M.B.1    Nielson, S.E.2    Berg, K.3
  • 22
    • 0001587762 scopus 로고
    • Inhibition of the in vitro infectivity and cytopathic effect of human T-lymphotrophic virus type III/ lymphadenopathy-associated virus (HTLV-III/LAV) by 2′,3′-dideoxynucleosides
    • Mitsuya H and Broder S: Inhibition of the in vitro infectivity and cytopathic effect of human T-lymphotrophic virus type III/ lymphadenopathy-associated virus (HTLV-III/LAV) by 2′,3′-dideoxynucleosides. Proc Natl Acad Sci USA 1986;83:1911-1915.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 1911-1915
    • Mitsuya, H.1    Broder, S.2
  • 24
    • 0023930757 scopus 로고
    • In vitro mutagenesis identifies a region within the envelope gene of the human immunodeficiency virus that is critical for infectivity
    • Willey RL, Smith DH, Lasky LA, Theodore TS, Earl PL, Moss B, Capon DJ, and Martin MA: In vitro mutagenesis identifies a region within the envelope gene of the human immunodeficiency virus that is critical for infectivity. J Virol 1988;62:139-147.
    • (1988) J Virol , vol.62 , pp. 139-147
    • Willey, R.L.1    Smith, D.H.2    Lasky, L.A.3    Theodore, T.S.4    Earl, P.L.5    Moss, B.6    Capon, D.J.7    Martin, M.A.8
  • 25
    • 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: The T4 gene encodes the AIDS virus receptor and is expressed in the immune system and the brain. Cell 1986;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
  • 26
    • 0025095635 scopus 로고
    • Oligomeric structure of the human immunodeficiency virus type 1 envelope glycoprotein
    • Earl PL, Doms RW, and Moss B: Oligomeric structure of the human immunodeficiency virus type 1 envelope glycoprotein. Proc Natl Acad Sci USA 1990;87:648-652.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 648-652
    • Earl, P.L.1    Doms, R.W.2    Moss, B.3
  • 27
    • 0026713860 scopus 로고
    • Mutations in the leucine zipper of the human immunodeficiency virus type 1 transmembrane glycoprotein affect fusion and infectivity
    • Dubai JW, Roberts SJ, Brody B, and Hunter E: Mutations in the leucine zipper of the human immunodeficiency virus type 1 transmembrane glycoprotein affect fusion and infectivity. J Virol 1992;66:6616-6625.
    • (1992) J Virol , vol.66 , pp. 6616-6625
    • Dubai, J.W.1    Roberts, S.J.2    Brody, B.3    Hunter, E.4
  • 28
    • 0025186067 scopus 로고
    • Apolipoprotein A-1 and its amphipathic helix peptide analogues inhibit human immunodeficiency virus-induced syncytium formation
    • Owens RJ, Anantharamaiah GM, Kahlon JB, Srinivas RV, Compans RW, and Segrest JP: Apolipoprotein A-1 and its amphipathic helix peptide analogues inhibit human immunodeficiency virus-induced syncytium formation. J Clin Invest 1990;86:1142-1150.
    • (1990) J Clin Invest , vol.86 , pp. 1142-1150
    • Owens, R.J.1    Anantharamaiah, G.M.2    Kahlon, J.B.3    Srinivas, R.V.4    Compans, R.W.5    Segrest, J.P.6
  • 30
    • 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
  • 31
    • 0026670705 scopus 로고
    • Apolipoprotein A-1 interacts with the N-terminal fusogenic domains of SIV (simian immunodeficiency virus) gp32 and HIV (human immunodeficiency virus) gp41: Implications in viral entry
    • Martin I, Dubois M-C, Saermark T, and Ruysschaert J-M: Apolipoprotein A-1 interacts with the N-terminal fusogenic domains of SIV (simian immunodeficiency virus) gp32 and HIV (human immunodeficiency virus) gp41: Implications in viral entry. Biochim Biophys Res Commun 1992;186:95-101.
    • (1992) Biochim Biophys Res Commun , vol.186 , pp. 95-101
    • Martin, I.1    Dubois, M.-C.2    Saermark, T.3    Ruysschaert, J.-M.4
  • 32
    • 0028174543 scopus 로고
    • HIV-1 virion-cell interactions; an electrostatic model of pathogenicity and syncytium formation
    • Callahan L: HIV-1 virion-cell interactions; an electrostatic model of pathogenicity and syncytium formation. AIDS 1994;10: 231-233.
    • (1994) AIDS , vol.10 , pp. 231-233
    • Callahan, L.1
  • 33
    • 0025271999 scopus 로고
    • Dextran sulphate and other polyanionic anti-HIV compounds specifically interact with the viral gp120 glycoprotein expressed by T-cells infected with HIV-1
    • Schols D, Pauwels R, Desmyter J, and De Clerq E: Dextran sulphate and other polyanionic anti-HIV compounds specifically interact with the viral gp120 glycoprotein expressed by T-cells infected with HIV-1. Virology 1990;175:556-561.
    • (1990) Virology , vol.175 , pp. 556-561
    • Schols, D.1    Pauwels, R.2    Desmyter, J.3    De Clerq, E.4
  • 34
    • 0028834461 scopus 로고
    • A trimeric structural domain of the HIV-1 transmembrane glycoprotein
    • Lu M, Blacklow SC, and Kim PS: A trimeric structural domain of the HIV-1 transmembrane glycoprotein. Nature Struct Biol 1995;2:1075-1082.
    • (1995) Nature Struct Biol , vol.2 , pp. 1075-1082
    • Lu, M.1    Blacklow, S.C.2    Kim, P.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.