메뉴 건너뛰기




Volumn 81, Issue 1, 2007, Pages 125-140

Impact of natural polymorphism within the gp41 cytoplasmic tail of human immunodeficiency virus type 1 on the intracellular distribution of envelope glycoproteins and viral assembly

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOHEXIMIDE; GLYCOPROTEIN GP 41; PLASMID DNA; VIRUS GLYCOPROTEIN;

EID: 33845752920     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.01659-06     Document Type: Article
Times cited : (28)

References (54)
  • 1
    • 0034000261 scopus 로고    scopus 로고
    • Cell-dependent requirement of human immunodeficiency virus type 1 gp41 cytoplasmic tail for Env incorporation into virions
    • Akari, H., T. Fukumori, and A. Adachi. 2000. Cell-dependent requirement of human immunodeficiency virus type 1 gp41 cytoplasmic tail for Env incorporation into virions. J. Virol. 74:4891-4893.
    • (2000) J. Virol. , vol.74 , pp. 4891-4893
    • Akari, H.1    Fukumori, T.2    Adachi, A.3
  • 2
    • 2442725956 scopus 로고    scopus 로고
    • Comparison of complete env gene sequences from individuals with symptomatic primary HIV type 1 infection
    • Ataman-Onal, Y., C. Coiffier, A. Giraud, A. Babic-Erceg, F. Biron, and B. Verrier. 1999. Comparison of complete env gene sequences from individuals with symptomatic primary HIV type 1 infection. AIDS Res. Hum. Retrovir. 15:1035-1039.
    • (1999) AIDS Res. Hum. Retrovir. , vol.15 , pp. 1035-1039
    • Ataman-Onal, Y.1    Coiffier, C.2    Giraud, A.3    Babic-Erceg, A.4    Biron, F.5    Verrier, B.6
  • 3
    • 0742290081 scopus 로고    scopus 로고
    • Interclade neutralization and enhancement of human immunodeficiency virus type 1 identified by an assay using HeLa cells expressing both CD4 receptor and CXCR4/CCR5 coreceptors
    • Barin, F., S. Brunet, D. Brand, C. Moog, R. Peyre, F. Damond, P. Chameau, and F. Barre-Sinoussi. 2004. Interclade neutralization and enhancement of human immunodeficiency virus type 1 identified by an assay using HeLa cells expressing both CD4 receptor and CXCR4/CCR5 coreceptors. J. Infect. Dis. 189:322-327.
    • (2004) J. Infect. Dis. , vol.189 , pp. 322-327
    • Barin, F.1    Brunet, S.2    Brand, D.3    Moog, C.4    Peyre, R.5    Damond, F.6    Chameau, P.7    Barre-Sinoussi, F.8
  • 4
    • 0032901996 scopus 로고    scopus 로고
    • Interactions of the cytoplasmic domains of human and simian retroviral transmembrane proteins with components of the clathrin adaptor complexes modulate intracellular and cell surface expression of envelope glycoproteins
    • Berlioz-Torrent, C., B. L. Schacklett, L. Erdtmann, L. Delamarre, I. Bouchaert, P. Sonigo, M. C. Dokhelar, and R. Benarous. 1999. Interactions of the cytoplasmic domains of human and simian retroviral transmembrane proteins with components of the clathrin adaptor complexes modulate intracellular and cell surface expression of envelope glycoproteins. J. Virol. 73:1350-1361.
    • (1999) J. Virol. , vol.73 , pp. 1350-1361
    • Berlioz-Torrent, C.1    Schacklett, B.L.2    Erdtmann, L.3    Delamarre, L.4    Bouchaert, I.5    Sonigo, P.6    Dokhelar, M.C.7    Benarous, R.8
  • 5
    • 0038618759 scopus 로고    scopus 로고
    • Targeting of the human immunodeficiency virus type 1 envelope to the trans-Golgi network through binding to TIP47 is required for Env incorporation into virions and infectivity
    • Blot, G., K. Janvier, S. Le Panse, R. Benarous, and C. Berlioz-Torrent. 2003. Targeting of the human immunodeficiency virus type 1 envelope to the trans-Golgi network through binding to TIP47 is required for Env incorporation into virions and infectivity. J. Virol. 77:6931-6945.
    • (2003) J. Virol. , vol.77 , pp. 6931-6945
    • Blot, G.1    Janvier, K.2    Le Panse, S.3    Benarous, R.4    Berlioz-Torrent, C.5
  • 6
    • 0032546927 scopus 로고    scopus 로고
    • A membrane-proximal tyrosine-based signal mediates internalization of the HIV-1 envelope glycoprotein via interaction with the AP-2 clathrin adaptor
    • Boge, M., S. Wyss, J. S. Bonifacino, and M. Thali. 1998. A membrane-proximal tyrosine-based signal mediates internalization of the HIV-1 envelope glycoprotein via interaction with the AP-2 clathrin adaptor. J. Biol. Chem. 273:15773-15778.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15773-15778
    • Boge, M.1    Wyss, S.2    Bonifacino, J.S.3    Thali, M.4
  • 8
    • 0343462450 scopus 로고    scopus 로고
    • Identification of two sequences in the cytoplasmic tail of the human immunodeficiency virus type 1 envelope glycoprotein that inhibit surface expression
    • Bultmann, A., W. Muranyi, B. Seed, and J. Haas. 2001. Identification of two sequences in the cytoplasmic tail of the human immunodeficiency virus type 1 envelope glycoprotein that inhibit surface expression. J. Virol. 75:5263-5276.
    • (2001) J. Virol. , vol.75 , pp. 5263-5276
    • Bultmann, A.1    Muranyi, W.2    Seed, B.3    Haas, J.4
  • 9
    • 0035728592 scopus 로고    scopus 로고
    • Influence of human immunodeficiency virus type 1 envelope glycoprotein YXXL endocytosis/polarization signal on viral accessory protein functions
    • Cervantes-Acosta, G., R. Lodge, G. Lemay, and E. A. Cohen. 2001. Influence of human immunodeficiency virus type 1 envelope glycoprotein YXXL endocytosis/polarization signal on viral accessory protein functions. J. Hum. Virol. 4:249-259.
    • (2001) J. Hum. Virol. , vol.4 , pp. 249-259
    • Cervantes-Acosta, G.1    Lodge, R.2    Lemay, G.3    Cohen, E.A.4
  • 10
    • 0034812854 scopus 로고    scopus 로고
    • Cellular membrane-binding ability of the C-terminal cytoplasmic domain of human immunodeficiency virus type 1 envelope transmembrane protein gp41
    • Chen, S. S., S. F. Lee, and C. T. Wang. 2001. Cellular membrane-binding ability of the C-terminal cytoplasmic domain of human immunodeficiency virus type 1 envelope transmembrane protein gp41. J. Virol. 75:9925-9938.
    • (2001) J. Virol. , vol.75 , pp. 9925-9938
    • Chen, S.S.1    Lee, S.F.2    Wang, C.T.3
  • 12
    • 0029857253 scopus 로고    scopus 로고
    • Direct interaction between the envelope and matrix proteins in HIV-1
    • Cosson, P. 1996. Direct interaction between the envelope and matrix proteins in HIV-1. EMBO J. 15:5783-5788.
    • (1996) EMBO J. , vol.15 , pp. 5783-5788
    • Cosson, P.1
  • 13
    • 7644239787 scopus 로고    scopus 로고
    • Evolutionary dynamics of the glycan shield of human immunodeficiency virus envelope during natural infection and implications for exposure of the 2G12 epitope
    • Dacheux, L., A. Moreau, Y. Ataman-Onal, F. Bion, B. Verrier, and F. Barin. 2004. Evolutionary dynamics of the glycan shield of human immunodeficiency virus envelope during natural infection and implications for exposure of the 2G12 epitope. J. Virol. 78:12625-12637.
    • (2004) J. Virol. , vol.78 , pp. 12625-12637
    • Dacheux, L.1    Moreau, A.2    Ataman-Onal, Y.3    Bion, F.4    Verrier, B.5    Barin, F.6
  • 14
    • 0346373731 scopus 로고    scopus 로고
    • The membrane-proximal tyrosine-based sorting signal of human immunodeficiency virus type 1 gp41 is required for optimal viral infectivity
    • Day, J. R., C. Münk, and J. C. Guatelli. 2004. The membrane-proximal tyrosine-based sorting signal of human immunodeficiency virus type 1 gp41 is required for optimal viral infectivity. J. Virol. 78:1069-1079.
    • (2004) J. Virol. , vol.78 , pp. 1069-1079
    • Day, J.R.1    Münk, C.2    Guatelli, J.C.3
  • 16
    • 0032994155 scopus 로고    scopus 로고
    • Polarized human immunodeficiency virus budding in lymphocytes involves a tyrosine-based signal and favors cell-to-cell viral transmission
    • Deschambeault, J., J. P. Lalonde, G. Cervantes-Acosta, R. Lodge, E. A. Cohen, and G. Lemay. 1999. Polarized human immunodeficiency virus budding in lymphocytes involves a tyrosine-based signal and favors cell-to-cell viral transmission. J. Virol. 73:5010-5017.
    • (1999) J. Virol. , vol.73 , pp. 5010-5017
    • Deschambeault, J.1    Lalonde, J.P.2    Cervantes-Acosta, G.3    Lodge, R.4    Cohen, E.A.5    Lemay, G.6
  • 17
    • 0027979135 scopus 로고
    • Role of the matrix protein in the virion association of the human immunodeficiency virus type 1 envelope glycoprotein
    • Dorfman, T., F. Mammano, W. A. Haseltine, and H. G. Gottlinger. 1994. Role of the matrix protein in the virion association of the human immunodeficiency virus type 1 envelope glycoprotein. J. Virol. 68:1689-1696.
    • (1994) J. Virol. , vol.68 , pp. 1689-1696
    • Dorfman, T.1    Mammano, F.2    Haseltine, W.A.3    Gottlinger, H.G.4
  • 18
    • 0026713860 scopus 로고
    • Truncation of the human immunodeficiency virus type 1 transmembrane glycoprotein cytoplasmic domain blocks virus infectivity
    • Dubay, J. W., S. J. Roberts, B. H. Hahn, and E. Hunter. 1992. Truncation of the human immunodeficiency virus type 1 transmembrane glycoprotein cytoplasmic domain blocks virus infectivity. J. Virol. 66:6616-6625.
    • (1992) J. Virol. , vol.66 , pp. 6616-6625
    • Dubay, J.W.1    Roberts, S.J.2    Hahn, B.H.3    Hunter, E.4
  • 19
    • 0025055304 scopus 로고
    • The most highly amphiphilic alpha-helices include two amino acid segments in human immunodeficiency virus glycoprotein 41
    • Eisenberg, D., and M. Wesson. 1990. The most highly amphiphilic alpha-helices include two amino acid segments in human immunodeficiency virus glycoprotein 41. Biopolymers 29:171-177.
    • (1990) Biopolymers , vol.29 , pp. 171-177
    • Eisenberg, D.1    Wesson, M.2
  • 20
    • 0030002637 scopus 로고    scopus 로고
    • HIV-1 entry co-factor: Functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor
    • Feng, Y., C. C. Broder, P. E. Kennedy, and E. A. Berger. 1996. HIV-1 entry co-factor: 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
  • 21
    • 0029062117 scopus 로고
    • Role of the basic domain of human immunodeficiency virus type 1 matrix in macrophage infection
    • Freed, E. O., G. Englund, and M. A. Martin. 1995. Role of the basic domain of human immunodeficiency virus type 1 matrix in macrophage infection. J. Virol. 69:3949-3954.
    • (1995) J. Virol. , vol.69 , pp. 3949-3954
    • Freed, E.O.1    Englund, G.2    Martin, M.A.3
  • 22
    • 0028819071 scopus 로고
    • Virion incorporation of envelope glycoproteins with long but not short cytoplasmic tails is blocked by specific, single amino acid substitutions in the human immunodeficiency virus type 1 matrix
    • Freed, E. O., and M. A. Martin. 1995. Virion incorporation of envelope glycoproteins with long but not short cytoplasmic tails is blocked by specific, single amino acid substitutions in the human immunodeficiency virus type 1 matrix. J. Virol. 69:1984-1989.
    • (1995) J. Virol. , vol.69 , pp. 1984-1989
    • Freed, E.O.1    Martin, M.A.2
  • 23
    • 0032506207 scopus 로고    scopus 로고
    • HIV-1 Gag proteins: Diverse functions in the virus life cycle
    • Freed, E. O. 1998. HIV-1 Gag proteins: diverse functions in the virus life cycle. Virology 251:1-15.
    • (1998) Virology , vol.251 , pp. 1-15
    • Freed, E.O.1
  • 24
    • 0026755725 scopus 로고
    • Effects of deletions in the cytoplasmic domain on biological fuctions of human immunodeficiency virus type 1 envelope glycoproteins
    • Gabuzda, D. H., A. Lever, E. Terwilliger, and J. Sodroski. 1992. Effects of deletions in the cytoplasmic domain on biological fuctions of human immunodeficiency virus type 1 envelope glycoproteins. J. Virol. 66:3306-3315.
    • (1992) J. Virol. , vol.66 , pp. 3306-3315
    • Gabuzda, D.H.1    Lever, A.2    Terwilliger, E.3    Sodroski, J.4
  • 25
    • 0033856584 scopus 로고    scopus 로고
    • Localization of human immunodeficiency virus type 1 Gag and Env at the plasma membrane by confocal imaging
    • Hermida-Matsumoto, L., and M. D. Resh. 2000. Localization of human immunodeficiency virus type 1 Gag and Env at the plasma membrane by confocal imaging. J. Virol. 74:8670-8679.
    • (2000) J. Virol. , vol.74 , pp. 8670-8679
    • Hermida-Matsumoto, L.1    Resh, M.D.2
  • 28
    • 0031962175 scopus 로고    scopus 로고
    • Conformational changes in cell surface HIV-1 envelope glycoproteins are triggered by cooperation between cell surface CD4 and co-receptor
    • Jones, P. L., T. Korte, and R. Blumenthal. 1998. Conformational changes in cell surface HIV-1 envelope glycoproteins are triggered by cooperation between cell surface CD4 and co-receptor. J. Biol. Chem. 273:403-409.
    • (1998) J. Biol. Chem. , vol.273 , pp. 403-409
    • Jones, P.L.1    Korte, T.2    Blumenthal, R.3
  • 29
    • 0037334568 scopus 로고    scopus 로고
    • Rational site-directed mutations of the LLP-1 and LLP-2 lentivirus lytic peptide domains in the intracytoplasmic tail of human immunodeficiency virus type 1 gp41 indicate common functions in cell-cell fusion but distinct roles in virion envelope incorporation
    • Kalia, V., S. Sarkar, P. Gupta, and R. C. Montelaro. 2003. Rational site-directed mutations of the LLP-1 and LLP-2 lentivirus lytic peptide domains in the intracytoplasmic tail of human immunodeficiency virus type 1 gp41 indicate common functions in cell-cell fusion but distinct roles in virion envelope incorporation. J. Virol. 77:3634-3646.
    • (2003) J. Virol. , vol.77 , pp. 3634-3646
    • Kalia, V.1    Sarkar, S.2    Gupta, P.3    Montelaro, R.C.4
  • 30
    • 0030969495 scopus 로고    scopus 로고
    • A leucine zipper-like sequence from the cytoplasmic tail of the HIV-1 envelope glycoprotein binds and perturbs lipid bilayers
    • Kliger, Y., and Y. Shai. 1997. A leucine zipper-like sequence from the cytoplasmic tail of the HIV-1 envelope glycoprotein binds and perturbs lipid bilayers. Biochemistry 36:5157-5169.
    • (1997) Biochemistry , vol.36 , pp. 5157-5169
    • Kliger, Y.1    Shai, Y.2
  • 32
    • 0028229632 scopus 로고
    • The intracytoplasmic domain of gp41 mediates polarized budding of human immunodeficiency virus type 1 in MDCK cells
    • Lodge, R., H. Gottlinger, D. Gabuzda, E. A. Cohen, and G. Lemay. 1994. The intracytoplasmic domain of gp41 mediates polarized budding of human immunodeficiency virus type 1 in MDCK cells. J. Virol. 68:4857-4861.
    • (1994) J. Virol. , vol.68 , pp. 4857-4861
    • Lodge, R.1    Gottlinger, H.2    Gabuzda, D.3    Cohen, E.A.4    Lemay, G.5
  • 33
    • 0031039756 scopus 로고    scopus 로고
    • The membrane-proximal intracytoplasmic tyrosine residue of HIV-1 envelope glycoprotein is critical for basolateral targeting of viral budding in MDCK cells
    • Lodge, R., J. P. Lalonde, G. Lemay, and E. A. Cohen. 1997. The membrane-proximal intracytoplasmic tyrosine residue of HIV-1 envelope glycoprotein is critical for basolateral targeting of viral budding in MDCK cells. EMBO J. 16:695-705.
    • (1997) EMBO J. , vol.16 , pp. 695-705
    • Lodge, R.1    Lalonde, J.P.2    Lemay, G.3    Cohen, E.A.4
  • 34
    • 0028917784 scopus 로고
    • Primary isolates of human immunodeficiency virus type 1 are relatively resistant to neutralization by monoclonal antibodies to gp120, and their neutralization is not predicted by studies with monomeric gp120
    • Moore, J. P., Y. Cao, L. Qing, Q. J. Sattentau, J. Pyati, R. Koduri, J. Robinson, C. F. Barbas III, D. R. Burton, and D. D. Ho. 1995. Primary isolates of human immunodeficiency virus type 1 are relatively resistant to neutralization by monoclonal antibodies to gp120, and their neutralization is not predicted by studies with monomeric gp120. J. Virol. 69:101-109.
    • (1995) J. Virol. , vol.69 , pp. 101-109
    • Moore, J.P.1    Cao, Y.2    Qing, L.3    Sattentau, Q.J.4    Pyati, J.5    Koduri, R.6    Robinson, J.7    Barbas III, C.F.8    Burton, D.R.9    Ho, D.D.10
  • 35
    • 0034602736 scopus 로고    scopus 로고
    • The long cytoplasmic tail of gp41 is required in a cell type-dependent manner for HIV-1 envelope glycoprotein incorporation into virions
    • Murakami, T., and E. O. Freed. 2000. The long cytoplasmic tail of gp41 is required in a cell type-dependent manner for HIV-1 envelope glycoprotein incorporation into virions. Proc. Natl. Acad. Sci. USA 97:343-348.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 343-348
    • Murakami, T.1    Freed, E.O.2
  • 36
    • 0034026083 scopus 로고    scopus 로고
    • Genetic evidence for an interaction between human immunodeficiency virus type 1 matrix and α-helix 2 of the gp41 cytoplasmic tail
    • Murakami, T., and E. O. Freed. 2000. Genetic evidence for an interaction between human immunodeficiency virus type 1 matrix and α-helix 2 of the gp41 cytoplasmic tail. J. Virol. 74:3548-3554.
    • (2000) J. Virol. , vol.74 , pp. 3548-3554
    • Murakami, T.1    Freed, E.O.2
  • 37
    • 0031585539 scopus 로고    scopus 로고
    • Interaction of endocytic signals from the HIV-1 envelope glycoprotein complex with members of the adaptor medium chain family
    • Ohno, H., R. C. Aguilar, M. C. Fournier, S. Hennecke, P. Cosson, and J. S. Bonifacino. 1997. Interaction of endocytic signals from the HIV-1 envelope glycoprotein complex with members of the adaptor medium chain family. Virology 238:305-315.
    • (1997) Virology , vol.238 , pp. 305-315
    • Ohno, H.1    Aguilar, R.C.2    Fournier, M.C.3    Hennecke, S.4    Cosson, P.5    Bonifacino, J.S.6
  • 38
    • 0033999270 scopus 로고    scopus 로고
    • Role of the Gag matrix domain in targeting human immunodeficiency virus type 1 assembly
    • Ono, A., J. M. Orenstein, and E. O. Freed. 2000. Role of the Gag matrix domain in targeting human immunodeficiency virus type 1 assembly. J. Virol. 74:2855-2866.
    • (2000) J. Virol. , vol.74 , pp. 2855-2866
    • Ono, A.1    Orenstein, J.M.2    Freed, E.O.3
  • 39
    • 0347634393 scopus 로고    scopus 로고
    • Cell-type-dependent targeting of human immunodeficiency virus type 1 assembly to the plasma membrane and multivesicular body
    • Ono, A., and E. O. Freed. 2004. Cell-type-dependent targeting of human immunodeficiency virus type 1 assembly to the plasma membrane and multivesicular body. J. Virol. 78:1552-1563.
    • (2004) J. Virol. , vol.78 , pp. 1552-1563
    • Ono, A.1    Freed, E.O.2
  • 40
    • 0041488655 scopus 로고    scopus 로고
    • Infectious HIV-1 assembles in late endosomes in primary macrophages
    • Pelchen-Matthews, A., B. Kramer, and M. Marsh. 2003. Infectious HIV-1 assembles in late endosomes in primary macrophages. J. Cell Biol. 162:443-455.
    • (2003) J. Cell Biol. , vol.162 , pp. 443-455
    • Pelchen-Matthews, A.1    Kramer, B.2    Marsh, M.3
  • 41
    • 0037374764 scopus 로고    scopus 로고
    • Fcgamma receptor-mediated suppression of human immunodeficiency virus type 1 replication in primary human macrophages
    • Perez-Bercoff, D., A. David, H. Sudry, F. Barre-Sinoussi, and G. Pancino. 2003. Fcgamma receptor-mediated suppression of human immunodeficiency virus type 1 replication in primary human macrophages. J. Virol. 77:4081-4094.
    • (2003) J. Virol. , vol.77 , pp. 4081-4094
    • Perez-Bercoff, D.1    David, A.2    Sudry, H.3    Barre-Sinoussi, F.4    Pancino, G.5
  • 42
    • 0034467955 scopus 로고    scopus 로고
    • Mutational analysis of conserved domains within the cytoplasmic tail of gp41 from human immunodeficiency virus type 1: Effects on glycoprotein incorporation and infectivity
    • Piller, S. C., J. W. Dubay, C. A. Derdeyn, and E. Hunter. 2000. Mutational analysis of conserved domains within the cytoplasmic tail of gp41 from human immunodeficiency virus type 1: effects on glycoprotein incorporation and infectivity. J. Virol. 74:11717-11723.
    • (2000) J. Virol. , vol.74 , pp. 11717-11723
    • Piller, S.C.1    Dubay, J.W.2    Derdeyn, C.A.3    Hunter, E.4
  • 44
    • 0029044133 scopus 로고
    • Endocytosis of endogenously synthesized HIV-1 envelope protein. Mechanism and role in processing for association with class II MHC
    • Rowell, J. F., P. E. Stanhope, and R. F. Siciliano. 1995. Endocytosis of endogenously synthesized HIV-1 envelope protein. Mechanism and role in processing for association with class II MHC. J. Immunol. 155:473-488.
    • (1995) J. Immunol. , vol.155 , pp. 473-488
    • Rowell, J.F.1    Stanhope, P.E.2    Siciliano, R.F.3
  • 45
    • 0023580063 scopus 로고
    • Blocking of HIV infectivity by a soluble, secreted form of the CD4 antigen
    • Smith, D. H., R. A. Byrn, S. A. Marsters, T. Gregory, J. E. Groopman, and D. J. Capon. 1987. Blocking of HIV infectivity by a soluble, secreted form of the CD4 antigen. Science 238:1704-1707.
    • (1987) Science , vol.238 , pp. 1704-1707
    • Smith, D.H.1    Byrn, R.A.2    Marsters, S.A.3    Gregory, T.4    Groopman, J.E.5    Capon, D.J.6
  • 46
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 47
    • 0034749279 scopus 로고    scopus 로고
    • Determination of coreceptor usage of human immunodeficiency virus type 1 from patient plasma samples by using a recombinant phenotypic assay
    • Trouplin, V., F. Salvatori, F. Cappello, V. Obry, A. Brelot, N. Heveker, M. Alizon, G. Scarlatti, F. Clavel, and F. Mammano. 2001. Determination of coreceptor usage of human immunodeficiency virus type 1 from patient plasma samples by using a recombinant phenotypic assay. J. Virol. 75:251-259.
    • (2001) J. Virol. , vol.75 , pp. 251-259
    • Trouplin, V.1    Salvatori, F.2    Cappello, F.3    Obry, V.4    Brelot, A.5    Heveker, N.6    Alizon, M.7    Scarlatti, G.8    Clavel, F.9    Mammano, F.10
  • 48
    • 3843073102 scopus 로고    scopus 로고
    • Retrospective study to time the introduction of HIV-I type 1 non-B subtypes in Lyon, France, using env genes obtained from primary infection samples
    • Vachot, L., Y. Ataman-Önal, C. Terrat, P.-Y. Durand, B. Ponceau, F. Biron, and B. Verrier. 2004. Retrospective study to time the introduction of HIV-I type 1 non-B subtypes in Lyon, France, using env genes obtained from primary infection samples. AIDS Res. Hum. Retrovir. 20:687-691.
    • (2004) AIDS Res. Hum. Retrovir. , vol.20 , pp. 687-691
    • Vachot, L.1    Ataman-Önal, Y.2    Terrat, C.3    Durand, P.-Y.4    Ponceau, B.5    Biron, F.6    Verrier, B.7
  • 49
    • 0036122454 scopus 로고    scopus 로고
    • Mutation of the dominant endocytosis motif in human immunodeficiency virus type 1 gp41 can complement matrix mutations without increasing Env incorporation
    • West, J. T., S. K. Weldon, S. Wyss, X. Lin, Q. Yu, M. Thali, and E. Hunter. 2002. Mutation of the dominant endocytosis motif in human immunodeficiency virus type 1 gp41 can complement matrix mutations without increasing Env incorporation. J. Virol. 76:3338-3349.
    • (2002) J. Virol. , vol.76 , pp. 3338-3349
    • West, J.T.1    Weldon, S.K.2    Wyss, S.3    Lin, X.4    Yu, Q.5    Thali, M.6    Hunter, E.7
  • 50
    • 0028966078 scopus 로고
    • Adaptation to persistent growth in the H9 cell line renders a primary isolate of human immunodeficiency virus type 1 sensitive to neutralization by vaccine sera
    • Wrin, T., T. P. Loh, J. C. Vennari, H., Schuitemaker, and J. H. Nunberg. 1995. Adaptation to persistent growth in the H9 cell line renders a primary isolate of human immunodeficiency virus type 1 sensitive to neutralization by vaccine sera. J. Virol. 69:39-48.
    • (1995) J. Virol. , vol.69 , pp. 39-48
    • Wrin, T.1    Loh, T.P.2    Vennari, J.C.3    Schuitemaker, H.4    Nunberg, J.H.5
  • 51
    • 0032546844 scopus 로고    scopus 로고
    • The HIV-1 envelope glycoproteins: Fuso gens, antigens, and immunogens
    • Wyatt, R., and J. Sodroski. 1998. The HIV-1 envelope glycoproteins: fuso gens, antigens, and immunogens. Science 280:1884-1888.
    • (1998) Science , vol.280 , pp. 1884-1888
    • Wyatt, R.1    Sodroski, J.2
  • 52
    • 0035123458 scopus 로고    scopus 로고
    • The highly conserved C-terminal dileucine motif in the cytosolic domain of the human immunodeficiency virus type 1 envelope glycoprotein is critical for its association with the AP-1 clathrin adaptor
    • Wyss, S., C. Berlioz-Torrent, M. Boge, G. Blot, S. Honing, R. Benarous, and M. Thali. 2001. The highly conserved C-terminal dileucine motif in the cytosolic domain of the human immunodeficiency virus type 1 envelope glycoprotein is critical for its association with the AP-1 clathrin adaptor. J. Virol. 75:2982-2992.
    • (2001) J. Virol. , vol.75 , pp. 2982-2992
    • Wyss, S.1    Berlioz-Torrent, C.2    Boge, M.3    Blot, G.4    Honing, S.5    Benarous, R.6    Thali, M.7
  • 53
    • 25144500649 scopus 로고    scopus 로고
    • Stoichiometry of envelope glycoprotein trimers in the entry of human immunodeficiency virus type 1
    • Yang, X., S. Kurteva, X. Ren, S. Lee, and J. Sodroski. 2005. Stoichiometry of envelope glycoprotein trimers in the entry of human immunodeficiency virus type 1. J. Virol. 79:12132-12147.
    • (2005) J. Virol. , vol.79 , pp. 12132-12147
    • Yang, X.1    Kurteva, S.2    Ren, X.3    Lee, S.4    Sodroski, J.5
  • 54
    • 0027473610 scopus 로고
    • Mutations in the cytoplasmic domain of human immunodeficiency type 1 transmembrane protein impair the incorporation of Env proteins into mature virions
    • Yu, X., X. Yuan, M. F. McLane, T. H. Lee, and M. Essex. 1993. Mutations in the cytoplasmic domain of human immunodeficiency type 1 transmembrane protein impair the incorporation of Env proteins into mature virions. J. Virol. 67:213-221.
    • (1993) J. Virol. , vol.67 , pp. 213-221
    • Yu, X.1    Yuan, X.2    McLane, M.F.3    Lee, T.H.4    Essex, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.