메뉴 건너뛰기




Volumn 85, Issue 22, 2011, Pages 11945-11954

Sequences in gibbon ape leukemia virus envelope that confer sensitivity to HIV-1 accessory protein Vpu

Author keywords

[No Author keywords available]

Indexed keywords

CELL SURFACE PROTEIN; PROTEIN CD4; UNCLASSIFIED DRUG; VPU PROTEIN;

EID: 80655125487     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.05171-11     Document Type: Article
Times cited : (10)

References (51)
  • 1
    • 37749032764 scopus 로고    scopus 로고
    • Requirements for the selective degradation of CD4 receptor molecules by the human immunodeficiency virus type 1 Vpu protein in the endoplasmic reticulum
    • Binette, J., et al. 2007. Requirements for the selective degradation of CD4 receptor molecules by the human immunodeficiency virus type 1 Vpu protein in the endoplasmic reticulum. Retrovirology 4:75.
    • (2007) Retrovirology , vol.4 , pp. 75
    • Binette, J.1
  • 2
    • 34250798068 scopus 로고    scopus 로고
    • An acidic cluster of the cytoplasmic tail of the RD114 virus glycoprotein controls assembly of retroviral envelopes
    • Bouard, D., et al. 2007. An acidic cluster of the cytoplasmic tail of the RD114 virus glycoprotein controls assembly of retroviral envelopes. Traffic 8:835-847.
    • (2007) Traffic , vol.8 , pp. 835-847
    • Bouard, D.1
  • 3
    • 0029160083 scopus 로고
    • A versatile vector for gene and oligonucleotide transfer into cells in culture and in vivo: polyethylenimine
    • Boussif, O., et al. 1995. A versatile vector for gene and oligonucleotide transfer into cells in culture and in vivo: polyethylenimine. Proc. Natl. Acad. Sci. U. S. A. 92:7297-7301.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 7297-7301
    • Boussif, O.1
  • 4
    • 23144444979 scopus 로고    scopus 로고
    • Protein structure prediction servers at University College London
    • Bryson, K., et al. 2005. Protein structure prediction servers at University College London. Nucleic Acids Res. 33:W36-W38.
    • (2005) Nucleic Acids Res , vol.33
    • Bryson, K.1
  • 5
    • 0026672676 scopus 로고
    • Macrophagetropic human immunodeficiency virus isolates from different patients exhibit unusual V3 envelope sequence homogeneity in comparison with T-celltropic isolates: definition of critical amino acids involved in cell tropism
    • Chesebro, B., K. Wehrly, J. Nishio, and S. Perryman. 1992. Macrophagetropic human immunodeficiency virus isolates from different patients exhibit unusual V3 envelope sequence homogeneity in comparison with T-celltropic isolates: definition of critical amino acids involved in cell tropism. J. Virol. 66:6547-6554.
    • (1992) J. Virol. , vol.66 , pp. 6547-6554
    • Chesebro, B.1    Wehrly, K.2    Nishio, J.3    Perryman, S.4
  • 6
    • 0035047142 scopus 로고    scopus 로고
    • Sequences in the cytoplasmic tail of the gibbon ape leukemia virus envelope protein that prevent its incorporation into lentiviral vectors
    • Christodoulopoulos, I., and P. M. Cannon. 2001. Sequences in the cytoplasmic tail of the gibbon ape leukemia virus envelope protein that prevent its incorporation into lentiviral vectors. J. Virol. 75:4129-4138.
    • (2001) J. Virol. , vol.75 , pp. 4129-4138
    • Christodoulopoulos, I.1    Cannon, P.M.2
  • 8
    • 67749095196 scopus 로고    scopus 로고
    • Vpu directs the degradation of the human immunodeficiency virus restriction factor BST-2/tetherin via a βTrCP-dependent mechanism
    • Douglas, J. L., K. Viswanathan, M. N. McCarroll, J. K. Gustin, K. Fruh, and A. V. Moses. 2009. Vpu directs the degradation of the human immunodeficiency virus restriction factor BST-2/tetherin via a βTrCP-dependent mechanism. J. Virol. 83:7931-7947.
    • (2009) J. Virol. , vol.83 , pp. 7931-7947
    • Douglas, J.L.1    Viswanathan, K.2    McCarroll, M.N.3    Gustin, J.K.4    Fruh, K.5    Moses, A.V.6
  • 9
    • 77954055324 scopus 로고    scopus 로고
    • Antagonism of tetherin restriction of HIV-1 release by Vpu involves binding and sequestration of the restriction factor in a perinuclear compartment
    • Dubé, M., et al. 2010. Antagonism of tetherin restriction of HIV-1 release by Vpu involves binding and sequestration of the restriction factor in a perinuclear compartment. PLoS Pathog. 6:e1000856.
    • (2010) PLoS Pathog , vol.6
    • Dubé, M.1
  • 10
    • 77950424913 scopus 로고    scopus 로고
    • Direct restriction of virus release and incorporation of the interferon-induced protein BST-2 into HIV-1 particles
    • Fitzpatrick, K., et al. 2010. Direct restriction of virus release and incorporation of the interferon-induced protein BST-2 into HIV-1 particles. PLoS Pathog. 6:e1000701.
    • (2010) PLoS Pathog , vol.6
    • Fitzpatrick, K.1
  • 11
    • 1942502838 scopus 로고    scopus 로고
    • Mutual functional destruction of HIV-1 Vpu and host TASK-1 channel
    • Hsu, K., J. Seharaseyon, P. Dong, S. Bour, and E. Marbán. 2004. Mutual functional destruction of HIV-1 Vpu and host TASK-1 channel. Mol. Cell 14:259-267.
    • (2004) Mol. Cell , vol.14 , pp. 259-267
    • Hsu, K.1    Seharaseyon, J.2    Dong, P.3    Bour, S.4    Marbán, E.5
  • 12
    • 37849053288 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vpu protein interacts with CD74 and modulates major histocompatibility complex class II presentation
    • Hussain, A., C. Wesley, M. Khalid, A. Chaudhry, and S. Jameel. 2008. Human immunodeficiency virus type 1 Vpu protein interacts with CD74 and modulates major histocompatibility complex class II presentation. J. Virol. 82:893-902.
    • (2008) J. Virol. , vol.82 , pp. 893-902
    • Hussain, A.1    Wesley, C.2    Khalid, M.3    Chaudhry, A.4    Jameel, S.5
  • 13
    • 0030952367 scopus 로고    scopus 로고
    • Functional analysis of the cytoplasmic tail of Moloney murine leukemia virus envelope protein
    • Januszeski, M. M., P. M. Cannon, D. Chen, Y. Rozenberg, and W. F. Anderson. 1997. Functional analysis of the cytoplasmic tail of Moloney murine leukemia virus envelope protein. J. Virol. 71:3613-3619.
    • (1997) J. Virol. , vol.71 , pp. 3613-3619
    • Januszeski, M.M.1    Cannon, P.M.2    Chen, D.3    Rozenberg, Y.4    Anderson, W.F.5
  • 14
    • 79952579918 scopus 로고    scopus 로고
    • Mechanisms for Env glycoprotein acquisition by retroviruses
    • Johnson, M. C. 2011. Mechanisms for Env glycoprotein acquisition by retroviruses. AIDS Res. Hum. Retroviruses 27:239-247.
    • (2011) AIDS Res. Hum. Retroviruses , vol.27 , pp. 239-247
    • Johnson, M.C.1
  • 15
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on positionspecific scoring matrices
    • Jones, D. T. 1999. Protein secondary structure prediction based on positionspecific scoring matrices. J. Mol. Biol. 292:195-202.
    • (1999) J. Mol. Biol. , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 16
    • 0030940154 scopus 로고    scopus 로고
    • The human immunodeficiency virus type 1 (HIV-1) Vpu protein interferes with an early step in the biosynthesis of major histocompatibility complex (MHC) class I molecules
    • Kerkau, T., et al. 1997. The human immunodeficiency virus type 1 (HIV-1) Vpu protein interferes with an early step in the biosynthesis of major histocompatibility complex (MHC) class I molecules. J. Exp. Med. 185:1295-1305.
    • (1997) J. Exp. Med. , vol.185 , pp. 1295-1305
    • Kerkau, T.1
  • 17
    • 0035105820 scopus 로고    scopus 로고
    • Filoviruspseudotyped lentiviral vector can efficiently and stably transduce airway epithelia in vivo
    • Kobinger, G. P., D. J. Weiner, Q.-C. Yu, and J. M. Wilson. 2001. Filoviruspseudotyped lentiviral vector can efficiently and stably transduce airway epithelia in vivo. Nat. Biotechnol. 19:225-230.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 225-230
    • Kobinger, G.P.1    Weiner, D.J.2    Yu, Q.-C.3    Wilson, J.M.4
  • 18
    • 0027517186 scopus 로고
    • Vpu-induced degradation of CD4: requirement for specific amino acid residues in the cytoplasmic domain of CD4
    • Lenburg, M. E., and N. R. Landau. 1993. Vpu-induced degradation of CD4: requirement for specific amino acid residues in the cytoplasmic domain of CD4. J. Virol. 67:7238-7245.
    • (1993) J. Virol. , vol.67 , pp. 7238-7245
    • Lenburg, M.E.1    Landau, N.R.2
  • 19
    • 0042346262 scopus 로고    scopus 로고
    • Vpu exerts a positive effect on HIV-1 infectivity by down-modulating CD4 receptor molecules at the surface of HIV-1 producing cells
    • Levesque, K., Y.-S. Zhao, and E. A. Cohen. 2003. Vpu exerts a positive effect on HIV-1 infectivity by down-modulating CD4 receptor molecules at the surface of HIV-1 producing cells. J. Biol. Chem. 278:28346-28353.
    • (2003) J. Biol. Chem. , vol.278 , pp. 28346-28353
    • Levesque, K.1    Zhao, Y.-S.2    Cohen, E.A.3
  • 20
    • 0034855638 scopus 로고    scopus 로고
    • Development of an avian leukosis-sarcoma virus subgroup A pseudotyped lentiviral vector
    • Lewis, B. C., N. Chinnasamy, R. A. Morgan, and H. E. Varmus. 2001. Development of an avian leukosis-sarcoma virus subgroup A pseudotyped lentiviral vector. J. Virol. 75:9339-9344.
    • (2001) J. Virol. , vol.75 , pp. 9339-9344
    • Lewis, B.C.1    Chinnasamy, N.2    Morgan, R.A.3    Varmus, H.E.4
  • 21
    • 77649091147 scopus 로고    scopus 로고
    • Pseudotyping incompatibility between HIV-1 and gibbon ape leukemia virus Env is modulated by Vpu
    • Lucas, T. M., T. D. Lyddon, P. M. Cannon, and M. C. Johnson. 2010. Pseudotyping incompatibility between HIV-1 and gibbon ape leukemia virus Env is modulated by Vpu. J. Virol. 84:2666-2674.
    • (2010) J. Virol. , vol.84 , pp. 2666-2674
    • Lucas, T.M.1    Lyddon, T.D.2    Cannon, P.M.3    Johnson, M.C.4
  • 22
    • 77954047969 scopus 로고    scopus 로고
    • Multilayered mechanism of CD4 downregulation by HIV-1 Vpu involving distinct ER retention and ERAD targeting steps
    • Magadán, J. G., et al. 2010. Multilayered mechanism of CD4 downregulation by HIV-1 Vpu involving distinct ER retention and ERAD targeting steps. PLoS Pathog. 6:e1000869.
    • (2010) PLoS Pathog , vol.6
    • Magadán, J.G.1
  • 23
    • 0032012456 scopus 로고    scopus 로고
    • A novel human WD protein, h-beta TrCp, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif
    • Margottin, F., et al. 1998. A novel human WD protein, h-beta TrCp, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif. Mol. Cell 1:565-574.
    • (1998) Mol. Cell , vol.1 , pp. 565-574
    • Margottin, F.1
  • 24
    • 11144229400 scopus 로고    scopus 로고
    • Directed evolution of retrovirus envelope protein cytoplasmic tails guided by functional incorporation into lentivirus particles
    • Merten, C. A., et al. 2005. Directed evolution of retrovirus envelope protein cytoplasmic tails guided by functional incorporation into lentivirus particles. J. Virol. 79:834-840.
    • (2005) J. Virol. , vol.79 , pp. 834-840
    • Merten, C.A.1
  • 25
    • 67249157032 scopus 로고    scopus 로고
    • Vpu antagonizes BST-2-mediated restriction of HIV-1 release via beta-TrCP and endo-lysosomal trafficking
    • Mitchell, R. S., et al. 2009. Vpu antagonizes BST-2-mediated restriction of HIV-1 release via beta-TrCP and endo-lysosomal trafficking. PLoS Pathog. 5:e1000450.
    • (2009) PLoS Pathog , vol.5
    • Mitchell, R.S.1
  • 26
    • 77956939580 scopus 로고    scopus 로고
    • Inhibition of lipid antigen presentation in dendritic cells by HIV-1 Vpu interference with CD1d recycling from endosomal compartments
    • Moll, M., S. K. Andersson, A. Smed-Sörensen, and J. K. Sandberg. 2010. Inhibition of lipid antigen presentation in dendritic cells by HIV-1 Vpu interference with CD1d recycling from endosomal compartments. Blood 116:1876-1884.
    • (2010) Blood , vol.116 , pp. 1876-1884
    • Moll, M.1    Andersson, S.K.2    Smed-Sörensen, A.3    Sandberg, J.K.4
  • 27
    • 38549095979 scopus 로고    scopus 로고
    • Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu
    • Neil, S. J. D., T. Zang, and P. D. Beiniasz. 2008. Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu. Nature 451:425-430.
    • (2008) Nature , vol.451 , pp. 425-430
    • Neil, S.J.D.1    Zang, T.2    Beiniasz, P.D.3
  • 28
    • 0031808074 scopus 로고    scopus 로고
    • A helix propensity scale based on experimental studies of peptides and proteins
    • Pace, C. N., and J. M. Scholtz. 1998. A helix propensity scale based on experimental studies of peptides and proteins. Biophys. J. 75:422-427.
    • (1998) Biophys. J. , vol.75 , pp. 422-427
    • Pace, C.N.1    Scholtz, J.M.2
  • 30
    • 0031908685 scopus 로고    scopus 로고
    • Mutational analysis of the human immunodeficiency virus type 1 Vpu transmembrane domain that promotes the enhanced release of virus-like particles from the plasma membrane of mammalian cells
    • Paul, M., S. Mazumder, N. Raja, and M. A. Jabbar. 1998. Mutational analysis of the human immunodeficiency virus type 1 Vpu transmembrane domain that promotes the enhanced release of virus-like particles from the plasma membrane of mammalian cells. J. Virol. 72:1270-1279.
    • (1998) J. Virol. , vol.72 , pp. 1270-1279
    • Paul, M.1    Mazumder, S.2    Raja, N.3    Jabbar, M.A.4
  • 31
    • 70350348675 scopus 로고    scopus 로고
    • Tetherin inhibits HIV-1 release by directly tethering virions to cells
    • Perez-Caballero, D., et al. 2009. Tetherin inhibits HIV-1 release by directly tethering virions to cells. Cell 139:499-511.
    • (2009) Cell , vol.139 , pp. 499-511
    • Perez-Caballero, D.1
  • 32
    • 0020623678 scopus 로고
    • Topography of murine leukemia virus envelope proteins: characterization of transmembrane components
    • Pinter, A., and W. J. Honnen. 1983. Topography of murine leukemia virus envelope proteins: characterization of transmembrane components. J. Virol. 46:1056-1060.
    • (1983) J. Virol. , vol.46 , pp. 1056-1060
    • Pinter, A.1    Honnen, W.J.2
  • 33
    • 0021234845 scopus 로고
    • Antibodies reactive with human T-lymphotropic retroviruses (HTLVIII) in the serum of patients with AIDS
    • Sarngadharan, M. G., M. Popovic, L. Bruch, J. Schüpbach, and R. C. Gallo. 1984. Antibodies reactive with human T-lymphotropic retroviruses (HTLVIII) in the serum of patients with AIDS. Science 224:506-508.
    • (1984) Science , vol.224 , pp. 506-508
    • Sarngadharan, M.G.1    Popovic, M.2    Bruch, L.3    Schüpbach, J.4    Gallo, R.C.5
  • 34
    • 0031935031 scopus 로고    scopus 로고
    • CD4 glycoprotein degradation induced by human immunodeficiency virus type 1 Vpu protein requires the function of proteasomes and the ubiquitin-conjugating pathway
    • Schubert, U., et al. 1998. CD4 glycoprotein degradation induced by human immunodeficiency virus type 1 Vpu protein requires the function of proteasomes and the ubiquitin-conjugating pathway. J. Virol. 72:2280-2288.
    • (1998) J. Virol. , vol.72 , pp. 2280-2288
    • Schubert, U.1
  • 35
    • 0030069139 scopus 로고    scopus 로고
    • The two biological activities of human immunodeficiency virus type 1 Vpu protein involve two separable structural domains
    • Schubert, U., et al. 1996. The two biological activities of human immunodeficiency virus type 1 Vpu protein involve two separable structural domains. J. Virol. 70:809-819.
    • (1996) J. Virol. , vol.70 , pp. 809-819
    • Schubert, U.1
  • 36
    • 0028349047 scopus 로고
    • Differential activities of the human immunodeficiency virus type 1-encoded Vpu protein are regulated by phosphorylation and occur in different cellular compartments
    • Schubert, U., and K. Strebel. 1994. Differential activities of the human immunodeficiency virus type 1-encoded Vpu protein are regulated by phosphorylation and occur in different cellular compartments. J. Virol. 68:2260-2271.
    • (1994) J. Virol. , vol.68 , pp. 2260-2271
    • Schubert, U.1    Strebel, K.2
  • 37
    • 78349264184 scopus 로고    scopus 로고
    • Degranulation of natural killer cells following interaction with HIV-1-infected cells is hindered by downmodulation of NTB-A by Vpu
    • Shah, A. H., et al. 2010. Degranulation of natural killer cells following interaction with HIV-1-infected cells is hindered by downmodulation of NTB-A by Vpu. Cell Host Microbe 8:397-409.
    • (2010) Cell Host Microbe , vol.8 , pp. 397-409
    • Shah, A.H.1
  • 38
    • 33744814048 scopus 로고    scopus 로고
    • Envelope proteins of spleen necrosis virus form infectious human immunodeficiency virus type 1 pseudotype vector particles, but fail to incorporate upon substitution of the cytoplasmic domain with that of gibbon ape leukemia virus
    • Stitz, J., N. Wolfrum, C. J. Buchholz, and K. Cichutek. 2006. Envelope proteins of spleen necrosis virus form infectious human immunodeficiency virus type 1 pseudotype vector particles, but fail to incorporate upon substitution of the cytoplasmic domain with that of gibbon ape leukemia virus. J. Gen. Virol. 87:1577-1581.
    • (2006) J. Gen. Virol. , vol.87 , pp. 1577-1581
    • Stitz, J.1    Wolfrum, N.2    Buchholz, C.J.3    Cichutek, K.4
  • 39
    • 0034691558 scopus 로고    scopus 로고
    • Lentiviral vectors pseudotyped with envelope glycoproteins derived from gibbon ape leukemia virus and murine leukemia virus 10A1
    • Stitz, J., et al. 2000. Lentiviral vectors pseudotyped with envelope glycoproteins derived from gibbon ape leukemia virus and murine leukemia virus 10A1. Virology 273:16-20.
    • (2000) Virology , vol.273 , pp. 16-20
    • Stitz, J.1
  • 40
    • 0023677668 scopus 로고
    • A novel gene of HIV-1, vpu, and its 16-kilodalton product
    • Strebel, K., T. Klimkait, and M. A. Martin. 1988. A novel gene of HIV-1, vpu, and its 16-kilodalton product. Science 241:1221-1223.
    • (1988) Science , vol.241 , pp. 1221-1223
    • Strebel, K.1    Klimkait, T.2    Martin, M.A.3
  • 41
    • 0038309969 scopus 로고    scopus 로고
    • Downregulation of CD4 is required for maintenance of viral infectivity of HIV-1
    • Tanaka, M., et al. 2003. Downregulation of CD4 is required for maintenance of viral infectivity of HIV-1. Virology 311:316-325.
    • (2003) Virology , vol.311 , pp. 316-325
    • Tanaka, M.1
  • 42
    • 55549093726 scopus 로고    scopus 로고
    • Biology and evolution of the endogenous koala retrovirus
    • Tarlinton, R., J. Meers, and P. Young. 2008. Biology and evolution of the endogenous koala retrovirus. Cell. Mol. Life Sci. 65:3413-3421.
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 3413-3421
    • Tarlinton, R.1    Meers, J.2    Young, P.3
  • 43
    • 0043064053 scopus 로고    scopus 로고
    • Structural criteria for regulation of membrane fusion and virion incorporation by the murine leukemia virus TM cytoplasmic domain
    • Taylor, G. M., and D. A. Sanders. 2003. Structural criteria for regulation of membrane fusion and virion incorporation by the murine leukemia virus TM cytoplasmic domain. Virology 312:295-305.
    • (2003) Virology , vol.312 , pp. 295-305
    • Taylor, G.M.1    Sanders, D.A.2
  • 44
    • 0032506276 scopus 로고    scopus 로고
    • Structural and functional analysis of the membranespanning domain of the human immunodeficiency virus type 1 Vpu protein
    • Tiganos, E., et al. 1998. Structural and functional analysis of the membranespanning domain of the human immunodeficiency virus type 1 Vpu protein. Virology 251:96-107.
    • (1998) Virology , vol.251 , pp. 96-107
    • Tiganos, E.1
  • 45
    • 41849116366 scopus 로고    scopus 로고
    • The interferon-induced protein BST-2 restricts HIV-1 release and is downregulated from the cell surface by the viral Vpu protein
    • Van Damme, N., et al. 2008. The interferon-induced protein BST-2 restricts HIV-1 release and is downregulated from the cell surface by the viral Vpu protein. Cell Host Microbe 3:245-252.
    • (2008) Cell Host Microbe , vol.3 , pp. 245-252
    • Van Damme, N.1
  • 46
    • 0027261551 scopus 로고
    • Human immunodeficiency virus type 1 Vpu protein induces degradation of chimeric envelope glycoproteins bearing the cytoplasmic and anchor domains of CD4: role of the cytoplasmic domain in Vpu-induced degradation in the endoplasmic reticulum
    • Vincent, M. J., N. U. Raja, and M. A. Jabbar. 1993. Human immunodeficiency virus type 1 Vpu protein induces degradation of chimeric envelope glycoproteins bearing the cytoplasmic and anchor domains of CD4: role of the cytoplasmic domain in Vpu-induced degradation in the endoplasmic reticulum. J. Virol. 67:5538-5549.
    • (1993) J. Virol. , vol.67 , pp. 5538-5549
    • Vincent, M.J.1    Raja, N.U.2    Jabbar, M.A.3
  • 47
    • 0026452726 scopus 로고
    • Human immunodeficiency virus type 1 Vpu protein induces rapid degradation of CD4
    • Willey, R., F. Maldarelli, M. Martin, and K. Strebel. 1992. Human immunodeficiency virus type 1 Vpu protein induces rapid degradation of CD4. J. Virol. 66:7193-7200.
    • (1992) J. Virol. , vol.66 , pp. 7193-7200
    • Willey, R.1    Maldarelli, F.2    Martin, M.3    Strebel, K.4
  • 48
    • 0026567269 scopus 로고
    • Human immunodeficiency virus type 1 Vpu protein regulates the formation of intracellular gpl60-CD4 complexes
    • Willey, R., F. Maldarelli, M. Martin, and K. Strebel. 1992. Human immunodeficiency virus type 1 Vpu protein regulates the formation of intracellular gpl60-CD4 complexes. J. Virol. 66:226-234.
    • (1992) J. Virol. , vol.66 , pp. 226-234
    • Willey, R.1    Maldarelli, F.2    Martin, M.3    Strebel, K.4
  • 49
    • 0028047321 scopus 로고
    • Sequences present in cytoplasmic domain of CD4 are necessary and sufficient to confer sensitivity to the human immunodeficiency virus type 1 Vpu protein
    • Willey, R. L., A. Buckler-White, and K. Strebel. 1994. Sequences present in cytoplasmic domain of CD4 are necessary and sufficient to confer sensitivity to the human immunodeficiency virus type 1 Vpu protein. J. Virol. 68:1207-1212.
    • (1994) J. Virol. , vol.68 , pp. 1207-1212
    • Willey, R.L.1    Buckler-White, A.2    Strebel, K.3
  • 50
    • 0029044110 scopus 로고
    • Degradation of CD4 induced by human immunodeficiency virus type 1 Vpu protein: a predicted alpha helix structure in the proximal cytoplasmic region of CD4 contributes to Vpu sensitivity
    • Yao, X. J., et al. 1995. Degradation of CD4 induced by human immunodeficiency virus type 1 Vpu protein: a predicted alpha helix structure in the proximal cytoplasmic region of CD4 contributes to Vpu sensitivity. Virology 209:615-623.
    • (1995) Virology , vol.209 , pp. 615-623
    • Yao, X.J.1
  • 51
    • 0030819379 scopus 로고    scopus 로고
    • Multiply attenuated lentiviral vector achieves efficient gene delivery in vivo
    • Zufferey, R., D. Nagy, R. J. Mandel, L. Naldini, and D. Trono. 1997. Multiply attenuated lentiviral vector achieves efficient gene delivery in vivo. Nat. Biotechnol. 15:871-875.
    • (1997) Nat. Biotechnol. , vol.15 , pp. 871-875
    • Zufferey, R.1    Nagy, D.2    Mandel, R.J.3    Naldini, L.4    Trono, D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.