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Volumn 52, Issue 5, 2008, Pages 287-295

Roles of the interactions between Env and Gag proteins in the HIV-1 replication cycle

Author keywords

Env glycoprotein; Env incorporation; Gag; Human immunodeficiency virus type 1; Membrane microdomains

Indexed keywords

GAG PROTEIN; GLYCOPROTEIN GP 120; GLYCOPROTEIN GP 160; GLYCOPROTEIN GP 41; VIRUS ENVELOPE PROTEIN;

EID: 72849117137     PISSN: 03855600     EISSN: 13480421     Source Type: Journal    
DOI: 10.1111/j.1348-0421.2008.00008.x     Document Type: Short Survey
Times cited : (22)

References (105)
  • 1
    • 75749100935 scopus 로고    scopus 로고
    • Freed E.O., Martin M.A. (2006) HIVs and their replication. In:Knipe D.M., Howley P.M., eds. Fields Virology, 5th edn. Philadelphia: Lippincott,Williams, andWilkins, pp. 2107-86.
    • Freed E.O., Martin M.A. (2006) HIVs and their replication. In:Knipe D.M., Howley P.M., eds. Fields Virology, 5th edn. Philadelphia: Lippincott,Williams, andWilkins, pp. 2107-86.
  • 2
    • 0029127787 scopus 로고
    • A single amino acid change in the cytoplasmic domain of the simian immunodeficiency virus transmembrane molecule increases envelope glycoprotein expression on infected cells
    • LaBranche C.C., Sauter M.M., Haggarty B.S., Vance P.J., Romano J., Hart T.K., Bugelski P. J., Marsh M., Hoxie J. A. (1995) A single amino acid change in the cytoplasmic domain of the simian immunodeficiency virus transmembrane molecule increases envelope glycoprotein expression on infected cells. J Virol 69: 5217-27.
    • (1995) J Virol , vol.69 , pp. 5217-5227
    • LaBranche, C.C.1    Sauter, M.M.2    Haggarty, B.S.3    Vance, P.J.4    Romano, J.5    Hart, T.K.6    Bugelski, P.J.7    Marsh, M.8    Hoxie, J.A.9
  • 3
    • 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., Stanhope P.E., Siliciano R.F. (1995) Endocytosis of endogenously synthesized HIV-1 envelope protein. Mechanism and role in processing for association with class II MHC. J Immunol 155: 473-88.
    • (1995) J Immunol , vol.155 , pp. 473-488
    • Rowell, J.F.1    Stanhope, P.E.2    Siliciano, R.F.3
  • 4
    • 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.,Wyss S., Bonifacino J.S., Thali M. (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: 15 773-8.
    • (1998) J Biol Chem , vol.273 , Issue.15 , pp. 773-778
    • Boge, M.1    Wyss, S.2    Bonifacino, J.S.3    Thali, M.4
  • 5
    • 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., Aguilar R.C., Fournier M.C., Hennecke S., Cosson P., Bonifacino J.S. (1997) Interaction of endocytic signals from the HIV-1 envelope glycoprotein complex with members of the adaptor medium chain family. Virology 238: 305-15.
    • (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
  • 6
    • 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., Shacklett B.L., Erdtmann L., Delamarre L., Bouchaert I., Sonigo P., Dokhelar M. C., Benarous R. (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: 1350-61.
    • (1999) J Virol , vol.73 , pp. 1350-1361
    • Berlioz-Torrent, C.1    Shacklett, B.L.2    Erdtmann, L.3    Delamarre, L.4    Bouchaert, I.5    Sonigo, P.6    Dokhelar, M.C.7    Benarous, R.8
  • 7
    • 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., Lalonde J.P., Lemay G., Cohen E.A. (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
  • 8
    • 33846821654 scopus 로고    scopus 로고
    • A conserved dileucine motif mediates clathrin and AP-2-dependent endocytosis of the HIV-1 envelope protein
    • Byland R., Vance P.J., Hoxie J.A., Marsh M. (2007) A conserved dileucine motif mediates clathrin and AP-2-dependent endocytosis of the HIV-1 envelope protein. Mol Biol Cell 18: 414-25.
    • (2007) Mol Biol Cell , vol.18 , pp. 414-425
    • Byland, R.1    Vance, P.J.2    Hoxie, J.A.3    Marsh, M.4
  • 9
    • 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., Berlioz-Torrent C., Boge M., Blot G., Honing S., Benarous R., Thali M. (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: 2982-92.
    • (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
  • 10
    • 0032076636 scopus 로고    scopus 로고
    • TIP47: A cargo selection device for mannose 6-phosphate receptor trafficking
    • Diaz E., Pfeffer S.R. (1998) TIP47: a cargo selection device for mannose 6-phosphate receptor trafficking. Cell 93: 433-43.
    • (1998) Cell , vol.93 , pp. 433-443
    • Diaz, E.1    Pfeffer, S.R.2
  • 11
    • 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., Janvier K., Le Panse S., Benarous R., Berlioz-Torrent C. (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: 6931-45.
    • (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
  • 12
    • 33749527044 scopus 로고    scopus 로고
    • Tail-interacting protein TIP47 is a connector between Gag and Env and is required for Env incorporation into HIV-1 virions
    • Lopez-Verges S., Camus G., Blot G., Beauvoir R., Benarous R., Berlioz-Torrent C. (2006) Tail-interacting protein TIP47 is a connector between Gag and Env and is required for Env incorporation into HIV-1 virions. Proc Natl Acad Sci USA 103: 14 947-52.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.14 , pp. 947-952
    • Lopez-Verges, S.1    Camus, G.2    Blot, G.3    Beauvoir, R.4    Benarous, R.5    Berlioz-Torrent, C.6
  • 13
    • 0037062441 scopus 로고    scopus 로고
    • Cell surface expression of the HIV-1 envelope glycoproteins is directed from intracellular CTLA-4-containing regulated secretory granules
    • Miranda L.R., Schaefer B.C., Kupfer A., Hu Z., Franzusoff A. (2002) Cell surface expression of the HIV-1 envelope glycoproteins is directed from intracellular CTLA-4-containing regulated secretory granules. Proc Natl Acad Sci USA 99: 8031-6.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 8031-8036
    • Miranda, L.R.1    Schaefer, B.C.2    Kupfer, A.3    Hu, Z.4    Franzusoff, A.5
  • 14
    • 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
  • 15
    • 0001118596 scopus 로고    scopus 로고
    • Synthesis, assembly, and processing of viral proteins
    • InCoffin J.M, Hughes S.H, Varmus H.E, eds, Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press, pp
    • Swanstrom R.,Wills J.W. (1997) Synthesis, assembly, and processing of viral proteins. InCoffin J.M., Hughes S.H., Varmus H.E., eds. Retroviruses, Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press, pp. 263-334.
    • (1997) Retroviruses , pp. 263-334
    • Swanstrom, R.1    Wills, J.W.2
  • 16
    • 9744221135 scopus 로고    scopus 로고
    • Retrovirus budding
    • Demirov D.G., Freed E.O. (2004) Retrovirus budding. Virus Res 106: 87-102.
    • (2004) Virus Res , vol.106 , pp. 87-102
    • Demirov, D.G.1    Freed, E.O.2
  • 17
    • 33646010475 scopus 로고    scopus 로고
    • The ESCRT complexes: Structure and mechanism of a membrane-trafficking network
    • Hurley J.H., Emr S.D. (2006) The ESCRT complexes: structure and mechanism of a membrane-trafficking network. Annu Rev Biophys Biomol Struct 35: 277-98.
    • (2006) Annu Rev Biophys Biomol Struct , vol.35 , pp. 277-298
    • Hurley, J.H.1    Emr, S.D.2
  • 18
    • 5044241819 scopus 로고    scopus 로고
    • Morita E., SundquistW.I. (2004) Retrovirus budding. Annu Rev Cell Dev Biol 20: 395-425.
    • Morita E., SundquistW.I. (2004) Retrovirus budding. Annu Rev Cell Dev Biol 20: 395-425.
  • 19
    • 33744938142 scopus 로고    scopus 로고
    • Assembly of infectious HIV-1 in human epithelial and T-lymphoblastic cell lines
    • Grigorov B., Arcanger F., Roingeard P., Darlix J.L., Muriaux D. (2006) Assembly of infectious HIV-1 in human epithelial and T-lymphoblastic cell lines. J Mol Biol 359: 848-62.
    • (2006) J Mol Biol , vol.359 , pp. 848-862
    • Grigorov, B.1    Arcanger, F.2    Roingeard, P.3    Darlix, J.L.4    Muriaux, D.5
  • 21
    • 0347634393 scopus 로고    scopus 로고
    • Cell-type-dependent targeting of human immunodeficiency virus type 1 assembly to the plasma membrane and the multivesicular body
    • Ono A., Freed E.O. (2004) Cell-type-dependent targeting of human immunodeficiency virus type 1 assembly to the plasma membrane and the multivesicular body. J Virol 78: 1552-63.
    • (2004) J Virol , vol.78 , pp. 1552-1563
    • Ono, A.1    Freed, E.O.2
  • 22
    • 33646410462 scopus 로고    scopus 로고
    • Identification of an intracellular trafficking and assembly pathway for HIV-1 gag
    • Perlman M., Resh M.D. (2006) Identification of an intracellular trafficking and assembly pathway for HIV-1 gag. Traffic 7: 731-45.
    • (2006) Traffic , vol.7 , pp. 731-745
    • Perlman, M.1    Resh, M.D.2
  • 24
    • 23144434990 scopus 로고    scopus 로고
    • Intracellular trafficking of HIV-1 Gag: How Gag interacts with cell membranes and makes viral particles
    • Resh M.D. (2005) Intracellular trafficking of HIV-1 Gag: how Gag interacts with cell membranes and makes viral particles. AIDS Rev 7: 84-91.
    • (2005) AIDS Rev , vol.7 , pp. 84-91
    • Resh, M.D.1
  • 25
    • 0038009933 scopus 로고    scopus 로고
    • Basyuk E., Galli T.,Mougel M., Blanchard J.M., SitbonM., Bertrand E. (2003) Retroviral genomic RNAs are transported to the plasma membrane by endosomal vesicles. Dev Cell 5: 161-74.
    • Basyuk E., Galli T.,Mougel M., Blanchard J.M., SitbonM., Bertrand E. (2003) Retroviral genomic RNAs are transported to the plasma membrane by endosomal vesicles. Dev Cell 5: 161-74.
  • 26
    • 3042694692 scopus 로고    scopus 로고
    • Nedd4.1-mediated ubiquitination and subsequent recruitment of Tsg101 ensure HTLV-1 Gag trafficking towards the multivesicular body pathway prior to virus budding
    • Blot V., Perugi F., Gay B., Prevost M.C., Briant L., Tangy F., Abriel H., Staub O., Dokhelar M. C., Pique C. (2004) Nedd4.1-mediated ubiquitination and subsequent recruitment of Tsg101 ensure HTLV-1 Gag trafficking towards the multivesicular body pathway prior to virus budding. J Cell Sci 117: 2357-67.
    • (2004) J Cell Sci , vol.117 , pp. 2357-2367
    • Blot, V.1    Perugi, F.2    Gay, B.3    Prevost, M.C.4    Briant, L.5    Tangy, F.6    Abriel, H.7    Staub, O.8    Dokhelar, M.C.9    Pique, C.10
  • 27
    • 0141605864 scopus 로고    scopus 로고
    • M-PMV capsid transport is mediated by Env/Gag interactions at the pericentriolar recycling endosome
    • Sfakianos J.N., Hunter E. (2003) M-PMV capsid transport is mediated by Env/Gag interactions at the pericentriolar recycling endosome. Traffic 4: 671-80.
    • (2003) Traffic , vol.4 , pp. 671-680
    • Sfakianos, J.N.1    Hunter, E.2
  • 28
    • 0141717669 scopus 로고    scopus 로고
    • The M-PMV cytoplasmic targeting-retention signal directs nascent Gag polypeptides to a pericentriolar region of the cell
    • Sfakianos J.N., LaCasse R.A., Hunter E. (2003) The M-PMV cytoplasmic targeting-retention signal directs nascent Gag polypeptides to a pericentriolar region of the cell. Traffic 4: 660-70.
    • (2003) Traffic , vol.4 , pp. 660-670
    • Sfakianos, J.N.1    LaCasse, R.A.2    Hunter, E.3
  • 29
    • 6944255361 scopus 로고    scopus 로고
    • Phosphatidylinositol (4,5) bisphosphate regulates HIV-1 Gag targeting to the plasma membrane
    • Ono A., Ablan S.D., Lockett S.J., Nagashima K., Freed E.O. (2004) Phosphatidylinositol (4,5) bisphosphate regulates HIV-1 Gag targeting to the plasma membrane. Proc Natl Acad Sci USA 101: 14 889-94.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.14 , pp. 889-894
    • Ono, A.1    Ablan, S.D.2    Lockett, S.J.3    Nagashima, K.4    Freed, E.O.5
  • 30
    • 33746625935 scopus 로고    scopus 로고
    • Structural basis for targeting HIV-1 Gag proteins to the plasma membrane for virus assembly
    • Saad J.S., Miller J., Tai J., Kim A., Ghanam R.H., Summers M.F. (2006) Structural basis for targeting HIV-1 Gag proteins to the plasma membrane for virus assembly. Proc Natl Acad Sci USA 103: 11 364-9.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.11 , pp. 364-369
    • Saad, J.S.1    Miller, J.2    Tai, J.3    Kim, A.4    Ghanam, R.H.5    Summers, M.F.6
  • 31
    • 15344350796 scopus 로고    scopus 로고
    • Dynamic fluorescent imaging of human immunodeficiency virus type 1 gag in live cells by biarsenical labeling
    • Rudner L., Nydegger S., Coren L.V., Nagashima K., Thali M., Ott D.E. (2005) Dynamic fluorescent imaging of human immunodeficiency virus type 1 gag in live cells by biarsenical labeling. J Virol 79: 4055-65.
    • (2005) J Virol , vol.79 , pp. 4055-4065
    • Rudner, L.1    Nydegger, S.2    Coren, L.V.3    Nagashima, K.4    Thali, M.5    Ott, D.E.6
  • 34
    • 34247529467 scopus 로고    scopus 로고
    • In macrophages, HIV-1 assembles into an intracellular plasma membrane domain containing the tetraspanins CD81, CD9, and CD53
    • Deneka M., Pelchen-Matthews A., Byland R., Ruiz-Mateos E., Marsh M. (2007) In macrophages, HIV-1 assembles into an intracellular plasma membrane domain containing the tetraspanins CD81, CD9, and CD53. J Cell Biol 177: 329-41.
    • (2007) J Cell Biol , vol.177 , pp. 329-341
    • Deneka, M.1    Pelchen-Matthews, A.2    Byland, R.3    Ruiz-Mateos, E.4    Marsh, M.5
  • 36
    • 27644598271 scopus 로고    scopus 로고
    • Interaction of HIV-1 Gag with the clathrin-associated adaptor AP-2
    • Batonick M., Favre M., Boge M., Spearman P., Honing S., Thali M. (2005) Interaction of HIV-1 Gag with the clathrin-associated adaptor AP-2. Virology 342: 190-200.
    • (2005) Virology , vol.342 , pp. 190-200
    • Batonick, M.1    Favre, M.2    Boge, M.3    Spearman, P.4    Honing, S.5    Thali, M.6
  • 38
    • 1342289622 scopus 로고    scopus 로고
    • Adaptor protein complexes as the key regulators of protein sorting in the post-Golgi network
    • Nakatsu F., Ohno H. (2003) Adaptor protein complexes as the key regulators of protein sorting in the post-Golgi network. Cell Struct Funct 28: 419-29.
    • (2003) Cell Struct Funct , vol.28 , pp. 419-429
    • Nakatsu, F.1    Ohno, H.2
  • 39
    • 33750365613 scopus 로고    scopus 로고
    • Clathrin-associated adaptor protein complexes
    • Ohno H. (2006) Clathrin-associated adaptor protein complexes. J Cell Sci 119: 3719-21.
    • (2006) J Cell Sci , vol.119 , pp. 3719-3721
    • Ohno, H.1
  • 41
    • 13444294247 scopus 로고    scopus 로고
    • Alroy I., Tuvia S., Greener T., Gordon D., Barr H.M., Taglicht D., Mandil-Levin R., Ben-Avraham D., Konforty D., Nir A., Levius O., Bicoviski V.,DoriM., Cohen S., Yaar L., Erez O., Propheta-Meiran O., Koskas M., Caspi-Bachar E., Alchanati I., Sela-Brown A., Moskowitz H., Tessmer U., Schubert U., Reiss Y. (2005) The trans-Golgi network-associated human ubiquitin-protein ligase POSH is essential for HIV type 1 production. Proc Natl Acad Sci USA 102: 1478-83.
    • Alroy I., Tuvia S., Greener T., Gordon D., Barr H.M., Taglicht D., Mandil-Levin R., Ben-Avraham D., Konforty D., Nir A., Levius O., Bicoviski V.,DoriM., Cohen S., Yaar L., Erez O., Propheta-Meiran O., Koskas M., Caspi-Bachar E., Alchanati I., Sela-Brown A., Moskowitz H., Tessmer U., Schubert U., Reiss Y. (2005) The trans-Golgi network-associated human ubiquitin-protein ligase POSH is essential for HIV type 1 production. Proc Natl Acad Sci USA 102: 1478-83.
  • 43
    • 34247516888 scopus 로고    scopus 로고
    • Host ABCE1 is at plasma membrane HIV assembly sites and its dissociation from Gag is linked to subsequent events of virus production
    • Dooher J.E., Schneider B.L., Reed J.C., Lingappa J.R. (2007) Host ABCE1 is at plasma membrane HIV assembly sites and its dissociation from Gag is linked to subsequent events of virus production. Traffic 8: 195-211.
    • (2007) Traffic , vol.8 , pp. 195-211
    • Dooher, J.E.1    Schneider, B.L.2    Reed, J.C.3    Lingappa, J.R.4
  • 44
    • 12144291130 scopus 로고    scopus 로고
    • Identification of Staufen in the human immunodeficiency virus type 1 Gag ribonucleoprotein complex and a role in generating infectious viral particles
    • Chatel-Chaix L., Clement J.F., Martel C., Beriault V., Gatignol A., DesGroseillers L., Mouland A. J. (2004) Identification of Staufen in the human immunodeficiency virus type 1 Gag ribonucleoprotein complex and a role in generating infectious viral particles. Mol Cell Biol 24: 2637-48.
    • (2004) Mol Cell Biol , vol.24 , pp. 2637-2648
    • Chatel-Chaix, L.1    Clement, J.F.2    Martel, C.3    Beriault, V.4    Gatignol, A.5    DesGroseillers, L.6    Mouland, A.J.7
  • 46
    • 0027979135 scopus 로고    scopus 로고
    • Dorfman T., Mammano F., HaseltineW.A., Gottlinger H.G. (1994) Role of the matrix protein in the virion association of the human immunodeficiency virus type 1 envelope glycoprotein. J Virol 68: 1689-96.
    • Dorfman T., Mammano F., HaseltineW.A., Gottlinger H.G. (1994) Role of the matrix protein in the virion association of the human immunodeficiency virus type 1 envelope glycoprotein. J Virol 68: 1689-96.
  • 47
    • 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., Martin M.A. (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: 1984-9.
    • (1995) J Virol , vol.69 , pp. 1984-1989
    • Freed, E.O.1    Martin, M.A.2
  • 48
    • 0026715925 scopus 로고
    • The matrix protein of human immunodeficiency virus type 1 is required for incorporation of viral envelope protein into mature virions
    • Yu X., Yuan X., Matsuda Z., Lee T.H., Essex M. (1992) The matrix protein of human immunodeficiency virus type 1 is required for incorporation of viral envelope protein into mature virions. J Virol 66: 4966-71.
    • (1992) J Virol , vol.66 , pp. 4966-4971
    • Yu, X.1    Yuan, X.2    Matsuda, Z.3    Lee, T.H.4    Essex, M.5
  • 49
    • 0029655514 scopus 로고    scopus 로고
    • Domains of the human immunodeficiency virus type 1 matrix and gp41 cytoplasmic tail required for envelope incorporation into virions
    • Freed E.O., Martin M.A. (1996) Domains of the human immunodeficiency virus type 1 matrix and gp41 cytoplasmic tail required for envelope incorporation into virions. J Virol 70: 341-51.
    • (1996) J Virol , vol.70 , pp. 341-351
    • Freed, E.O.1    Martin, M.A.2
  • 50
    • 0029037089 scopus 로고
    • Rescue of human immunodeficiency virus type 1 matrix protein mutants by envelope glycoproteins with short cytoplasmic domains
    • Mammano F., Kondo E., Sodroski J., Bukovsky A., Gottlinger H.G. (1995) Rescue of human immunodeficiency virus type 1 matrix protein mutants by envelope glycoproteins with short cytoplasmic domains. J Virol 69: 3824-30.
    • (1995) J Virol , vol.69 , pp. 3824-3830
    • Mammano, F.1    Kondo, E.2    Sodroski, J.3    Bukovsky, A.4    Gottlinger, H.G.5
  • 51
    • 0034026083 scopus 로고    scopus 로고
    • Genetic evidence for an interaction between human immunodeficiency virus type 1 matrix and a-helix 2 of the gp41 cytoplasmic tail
    • Murakami T., Freed E.O. (2000) Genetic evidence for an interaction between human immunodeficiency virus type 1 matrix and a-helix 2 of the gp41 cytoplasmic tail. J Virol 74: 3548-54.
    • (2000) J Virol , vol.74 , pp. 3548-3554
    • Murakami, T.1    Freed, E.O.2
  • 52
    • 0028229632 scopus 로고
    • The intracytoplasmic domain of gp41 mediates polarized budding of human immunodeficiency virus type 1 in MDCK cells
    • Lodge R., Gottlinger H., Gabuzda D., Cohen E.A., Lemay G. (1994) The intracytoplasmic domain of gp41 mediates polarized budding of human immunodeficiency virus type 1 in MDCK cells. J Virol 68: 4857-61.
    • (1994) J Virol , vol.68 , pp. 4857-4861
    • Lodge, R.1    Gottlinger, H.2    Gabuzda, D.3    Cohen, E.A.4    Lemay, G.5
  • 53
    • 0025822399 scopus 로고
    • Human immunodeficiency virus envelope protein determines the site of virus release in polarized epithelial cells
    • Owens R.J., Dubay J.W., Hunter E., Compans R.W. (1991) Human immunodeficiency virus envelope protein determines the site of virus release in polarized epithelial cells. Proc Natl Acad Sci USA 88: 3987-91.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 3987-3991
    • Owens, R.J.1    Dubay, J.W.2    Hunter, E.3    Compans, R.W.4
  • 54
    • 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., Lalonde J.P., Cervantes-Acosta G., Lodge R., Cohen E.A., Lemay G. (1999) Polarized human immunodeficiency virus budding in lymphocytes involves a tyrosine-based signal and favors cell-to-cell viral transmission. J Virol 73: 5010-7.
    • (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
  • 55
    • 0034000261 scopus 로고    scopus 로고
    • Cell-dependent requirement of human immunodeficiency virus type 1 gp41 cytoplasmic tail for Env incorporation into virions
    • Akari H., Fukumori T., Adachi A. (2000) Cell-dependent requirement of human immunodeficiency virus type 1 gp41 cytoplasmic tail for Env incorporation into virions. J Virol 74: 4891-3.
    • (2000) J Virol , vol.74 , pp. 4891-4893
    • Akari, H.1    Fukumori, T.2    Adachi, A.3
  • 56
    • 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., Freed E.O. (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: 343-8.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 343-348
    • Murakami, T.1    Freed, E.O.2
  • 58
    • 33646722688 scopus 로고    scopus 로고
    • Gag regulates association of human immunodeficiency virus type 1 envelope with detergent-resistant membranes
    • Bhattacharya J., Repik A., Clapham P.R. (2006) Gag regulates association of human immunodeficiency virus type 1 envelope with detergent-resistant membranes. J Virol 80: 5292-300.
    • (2006) J Virol , vol.80 , pp. 5292-5300
    • Bhattacharya, J.1    Repik, A.2    Clapham, P.R.3
  • 59
    • 0029857253 scopus 로고    scopus 로고
    • Direct interaction between the envelope and matrix proteins of HIV-1
    • Cosson P. (1996) Direct interaction between the envelope and matrix proteins of HIV-1. EMBO J 15: 5783-8.
    • (1996) EMBO J , vol.15 , pp. 5783-5788
    • Cosson, P.1
  • 60
    • 0031901456 scopus 로고    scopus 로고
    • Specific interactions between retrovirus Env and Gag proteins in rat neurons
    • Weclewicz K., Ekstrom M., Kristensson K., Garoff H. (1998) Specific interactions between retrovirus Env and Gag proteins in rat neurons. J Virol 72: 2832-45.
    • (1998) J Virol , vol.72 , pp. 2832-2845
    • Weclewicz, K.1    Ekstrom, M.2    Kristensson, K.3    Garoff, H.4
  • 61
    • 0026052031 scopus 로고
    • Brefeldin A inhibits the processing and secretion of envelope glycoproteins of human immunodeficiency virus type 1
    • Pal R., Mumbauer S., Hoke G.M., Takatsuki A., Sarngadharan M.G. (1991) Brefeldin A inhibits the processing and secretion of envelope glycoproteins of human immunodeficiency virus type 1. AIDS Res Hum Retroviruses 7: 707-12.
    • (1991) AIDS Res Hum Retroviruses , vol.7 , pp. 707-712
    • Pal, R.1    Mumbauer, S.2    Hoke, G.M.3    Takatsuki, A.4    Sarngadharan, M.G.5
  • 62
    • 0030747371 scopus 로고    scopus 로고
    • Transfer of endoplasmic reticulum and Golgi retention signals to human immunodeficiency virus type 1 gp160 inhibits intracellular transport and proteolytic processing of viral glycoprotein but does not influence the cellular site of virus particle budding
    • Pfeiffer T., Zentgraf H., Freyaldenhoven B., Bosch V. (1997) Transfer of endoplasmic reticulum and Golgi retention signals to human immunodeficiency virus type 1 gp160 inhibits intracellular transport and proteolytic processing of viral glycoprotein but does not influence the cellular site of virus particle budding. J Gen Virol 78(Pt 7): 1745-53.
    • (1997) J Gen Virol , vol.78 , Issue.PART 7 , pp. 1745-1753
    • Pfeiffer, T.1    Zentgraf, H.2    Freyaldenhoven, B.3    Bosch, V.4
  • 63
    • 0031846868 scopus 로고    scopus 로고
    • Retention of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum does not redirect virus assembly from the plasma membrane
    • Salzwedel K.,West J.T., Jr., Mulligan M.J., Hunter E. (1998) Retention of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum does not redirect virus assembly from the plasma membrane. J Virol 72: 7523-31.
    • (1998) J Virol , vol.72 , pp. 7523-7531
    • Salzwedel, K.1    West Jr., J.T.2    Mulligan, M.J.3    Hunter, E.4
  • 64
    • 0032826395 scopus 로고    scopus 로고
    • Intracellular interaction of simian immunodeficiency virus Gag and Env proteins
    • Vincent M.J., Melsen L.R., Martin A.S., Compans R.W. (1999) Intracellular interaction of simian immunodeficiency virus Gag and Env proteins. J Virol 73: 8138-44.
    • (1999) J Virol , vol.73 , pp. 8138-8144
    • Vincent, M.J.1    Melsen, L.R.2    Martin, A.S.3    Compans, R.W.4
  • 65
    • 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., Resh M.D. (2000) Localization of human immunodeficiency virus type 1 Gag and Env at the plasma membrane by confocal imaging. J Virol 74: 8670-9.
    • (2000) J Virol , vol.74 , pp. 8670-8679
    • Hermida-Matsumoto, L.1    Resh, M.D.2
  • 66
    • 0034625373 scopus 로고    scopus 로고
    • Structure and function of sphingolipid- and cholesterol-rich membrane rafts
    • Brown D.A., London E. (2000) Structure and function of sphingolipid- and cholesterol-rich membrane rafts. J Biol Chem 275: 17 221-4.
    • (2000) J Biol Chem , vol.275 , Issue.17 , pp. 221-224
    • Brown, D.A.1    London, E.2
  • 67
    • 1842588906 scopus 로고    scopus 로고
    • Lipids as targeting signals: Lipid rafts and intracellular trafficking
    • Helms J.B., Zurzolo C. (2004) Lipids as targeting signals: lipid rafts and intracellular trafficking. Traffic 5: 247-54.
    • (2004) Traffic , vol.5 , pp. 247-254
    • Helms, J.B.1    Zurzolo, C.2
  • 68
    • 0034304851 scopus 로고    scopus 로고
    • Lipid rafts and signal transduction
    • Simons K., Toomre D. (2000) Lipid rafts and signal transduction. Nat RevMol Cell Biol 1: 31-9.
    • (2000) Nat RevMol Cell Biol , vol.1 , pp. 31-39
    • Simons, K.1    Toomre, D.2
  • 69
    • 26944452885 scopus 로고    scopus 로고
    • Role of lipid rafts in virus replication
    • Ono A., Freed E.O. (2005) Role of lipid rafts in virus replication. Adv Virus Res 64: 311-58.
    • (2005) Adv Virus Res , vol.64 , pp. 311-358
    • Ono, A.1    Freed, E.O.2
  • 70
    • 0027325411 scopus 로고
    • Lipid composition and fluidity of the human immunodeficiency virus envelope and host cell plasma membranes
    • Aloia R.C., Tian H., Jensen F.C. (1993) Lipid composition and fluidity of the human immunodeficiency virus envelope and host cell plasma membranes. Proc Natl Acad Sci USA 90: 5181-5.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 5181-5185
    • Aloia, R.C.1    Tian, H.2    Jensen, F.C.3
  • 72
    • 0034015604 scopus 로고    scopus 로고
    • Evidence for budding of human immunodeficiency virus type 1 selectively from glycolipid-enriched membrane lipid rafts
    • Nguyen D.H., Hildreth J.E. (2000) Evidence for budding of human immunodeficiency virus type 1 selectively from glycolipid-enriched membrane lipid rafts. J Virol 74: 3264-72.
    • (2000) J Virol , vol.74 , pp. 3264-3272
    • Nguyen, D.H.1    Hildreth, J.E.2
  • 73
    • 0034951851 scopus 로고    scopus 로고
    • PicklW.F., Pimentel-Muinos F.X., Seed B. (2001) Lipid rafts and pseudotyping. J Virol 75: 7175-83.
    • PicklW.F., Pimentel-Muinos F.X., Seed B. (2001) Lipid rafts and pseudotyping. J Virol 75: 7175-83.
  • 74
    • 0034610368 scopus 로고    scopus 로고
    • Palmitoylation of the HIV-1 envelope glycoprotein is critical for viral infectivity
    • Rousso I., Mixon M.B., Chen B.K., Kim P.S. (2000) Palmitoylation of the HIV-1 envelope glycoprotein is critical for viral infectivity. Proc Natl Acad Sci USA 97: 13 523-5.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.13 , pp. 523-525
    • Rousso, I.1    Mixon, M.B.2    Chen, B.K.3    Kim, P.S.4
  • 75
    • 2342539802 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 envelope glycoproteins that lack cytoplasmic domain cysteines: Impact on association with membrane lipid rafts and incorporation onto budding virus particles
    • Bhattacharya J., Peters P.J., Clapham P.R. (2004) Human immunodeficiency virus type 1 envelope glycoproteins that lack cytoplasmic domain cysteines: impact on association with membrane lipid rafts and incorporation onto budding virus particles. J Virol 78: 5500-6.
    • (2004) J Virol , vol.78 , pp. 5500-5506
    • Bhattacharya, J.1    Peters, P.J.2    Clapham, P.R.3
  • 76
    • 20744433027 scopus 로고    scopus 로고
    • ChanW.E., Lin H.H., Chen S.S. (2005)Wild-type-like viral replication potential of human immunodeficiency virus type 1 envelope mutants lacking palmitoylation signals. J Virol 79: 8374-87.
    • ChanW.E., Lin H.H., Chen S.S. (2005)Wild-type-like viral replication potential of human immunodeficiency virus type 1 envelope mutants lacking palmitoylation signals. J Virol 79: 8374-87.
  • 77
    • 0037379284 scopus 로고    scopus 로고
    • Rapid localization of Gag/GagPol complexes to detergent-resistant membrane during the assembly of human immunodeficiency virus type 1
    • Halwani R., Khorchid A., Cen S., Kleiman L. (2003) Rapid localization of Gag/GagPol complexes to detergent-resistant membrane during the assembly of human immunodeficiency virus type 1. J Virol 77: 3973-84.
    • (2003) J Virol , vol.77 , pp. 3973-3984
    • Halwani, R.1    Khorchid, A.2    Cen, S.3    Kleiman, L.4
  • 78
    • 0037384986 scopus 로고    scopus 로고
    • gag associates with membrane domains that are largely resistant to Brij98 but sensitive to Triton X-100
    • gag associates with membrane domains that are largely resistant to Brij98 but sensitive to Triton X-100. J Virol 77: 4805-17.
    • (2003) J Virol , vol.77 , pp. 4805-4817
    • Holm, K.1    Weclewicz, K.2    Hewson, R.3    Suomalainen, M.4
  • 79
    • 0034864631 scopus 로고    scopus 로고
    • Multimerization of human immunodeficiency virus type 1 Gag promotes its localization to barges, raft-like membrane microdomains
    • Lindwasser O.W., Resh M.D. (2001) Multimerization of human immunodeficiency virus type 1 Gag promotes its localization to barges, raft-like membrane microdomains. J Virol 75: 7913-24.
    • (2001) J Virol , vol.75 , pp. 7913-7924
    • Lindwasser, O.W.1    Resh, M.D.2
  • 80
    • 0035923525 scopus 로고    scopus 로고
    • Plasma membrane rafts play a critical role in HIV-1 assembly and release
    • Ono A., Freed E.O. (2001) Plasma membrane rafts play a critical role in HIV-1 assembly and release. Proc Natl Acad Sci USA 98: 13 925-30.
    • (2001) Proc Natl Acad Sci USA , vol.98 , Issue.13 , pp. 925-930
    • Ono, A.1    Freed, E.O.2
  • 81
    • 0036789937 scopus 로고    scopus 로고
    • Myristoylation as a target for inhibiting HIV assembly: Unsaturated fatty acids block viral budding
    • Lindwasser O.W., Resh M.D. (2002) Myristoylation as a target for inhibiting HIV assembly: unsaturated fatty acids block viral budding. Proc Natl Acad Sci USA 99: 13 037-42.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.13 , pp. 037-042
    • Lindwasser, O.W.1    Resh, M.D.2
  • 82
    • 33847254050 scopus 로고    scopus 로고
    • Depletion of cellular cholesterol inhibits membrane binding and higher-order multimerization of human immunodeficiency virus type 1 Gag
    • Ono A.,Waheed A.A., Freed E.O. (2007) Depletion of cellular cholesterol inhibits membrane binding and higher-order multimerization of human immunodeficiency virus type 1 Gag. Virology 360: 27-35.
    • (2007) Virology , vol.360 , pp. 27-35
    • Ono, A.1    Waheed, A.A.2    Freed, E.O.3
  • 83
    • 28444441957 scopus 로고    scopus 로고
    • Tetraspanin functions and associated microdomains
    • Hemler M.E. (2005) Tetraspanin functions and associated microdomains.Nat RevMol Cell Biol 6: 801-11.
    • (2005) Nat RevMol Cell Biol , vol.6 , pp. 801-811
    • Hemler, M.E.1
  • 85
    • 34547105037 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 assembly, budding, and cell-cell spread in T cells take place in tetraspanin-enriched plasma membrane domains
    • Jolly C., Sattentau Q.J. (2007) Human immunodeficiency virus type 1 assembly, budding, and cell-cell spread in T cells take place in tetraspanin-enriched plasma membrane domains. J Virol 81: 7873-84.
    • (2007) J Virol , vol.81 , pp. 7873-7884
    • Jolly, C.1    Sattentau, Q.J.2
  • 86
    • 33747394451 scopus 로고    scopus 로고
    • Mapping of tetraspanin-enriched microdomains that can function as gateways for HIV-1
    • Nydegger S., Khurana S., Krementsov D.N., Foti M., Thali M. (2006) Mapping of tetraspanin-enriched microdomains that can function as gateways for HIV-1. J Cell Biol 173: 795-807.
    • (2006) J Cell Biol , vol.173 , pp. 795-807
    • Nydegger, S.1    Khurana, S.2    Krementsov, D.N.3    Foti, M.4    Thali, M.5
  • 87
    • 0342394457 scopus 로고    scopus 로고
    • Gottlinger H.G., Sodroski J.G., HaseltineW.A. (1989) Role of capsid precursor processing and myristoylation in morphogenesis and infectivity of human immunodeficiency virus type 1. Proc Natl Acad Sci USA 86: 5781-5.
    • Gottlinger H.G., Sodroski J.G., HaseltineW.A. (1989) Role of capsid precursor processing and myristoylation in morphogenesis and infectivity of human immunodeficiency virus type 1. Proc Natl Acad Sci USA 86: 5781-5.
  • 88
    • 0005241362 scopus 로고    scopus 로고
    • Kohl N.E., Emini E.A., SchleifW.A., Davis L.J., Heimbach J.C., Dixon R.A., Scolnick E. M., Sigal I. S. (1988) Active human immunodeficiency virus protease is required for viral infectivity. Proc Natl Acad Sci USA 85: 4686-90.
    • Kohl N.E., Emini E.A., SchleifW.A., Davis L.J., Heimbach J.C., Dixon R.A., Scolnick E. M., Sigal I. S. (1988) Active human immunodeficiency virus protease is required for viral infectivity. Proc Natl Acad Sci USA 85: 4686-90.
  • 89
    • 0024334170 scopus 로고
    • Role of human immunodeficiency virus type 1-specific protease in core protein maturation and viral infectivity
    • Peng C., Ho B.K., Chang T.W., Chang N.T. (1989) Role of human immunodeficiency virus type 1-specific protease in core protein maturation and viral infectivity. J Virol 63: 2550-6.
    • (1989) J Virol , vol.63 , pp. 2550-2556
    • Peng, C.1    Ho, B.K.2    Chang, T.W.3    Chang, N.T.4
  • 90
    • 0031925586 scopus 로고    scopus 로고
    • Sequential steps in human immunodeficiency virus particle maturation revealed by alterations of individual Gag polyprotein cleavage sites
    • Wiegers K., Rutter G., Kottler H., Tessmer U., Hohenberg H., Krausslich H.G. (1998) Sequential steps in human immunodeficiency virus particle maturation revealed by alterations of individual Gag polyprotein cleavage sites. J Virol 72: 2846-54.
    • (1998) J Virol , vol.72 , pp. 2846-2854
    • Wiegers, K.1    Rutter, G.2    Kottler, H.3    Tessmer, U.4    Hohenberg, H.5    Krausslich, H.G.6
  • 91
    • 0033809342 scopus 로고    scopus 로고
    • Evidence for a stable interaction of gp41 with Pr55(Gag) in immature human immunodeficiency virus type 1 particles
    • Wyma D.J., Kotov A., Aiken C. (2000) Evidence for a stable interaction of gp41 with Pr55(Gag) in immature human immunodeficiency virus type 1 particles. J Virol 74: 9381-7.
    • (2000) J Virol , vol.74 , pp. 9381-9387
    • Wyma, D.J.1    Kotov, A.2    Aiken, C.3
  • 92
    • 0028241598 scopus 로고
    • Postassembly cleavage of a retroviral glycoprotein cytoplasmic domain removes a necessary incorporation signal and activates fusion activity
    • Brody B.A., Rhee S.S., Hunter E. (1994) Postassembly cleavage of a retroviral glycoprotein cytoplasmic domain removes a necessary incorporation signal and activates fusion activity. J Virol 68: 4620-7.
    • (1994) J Virol , vol.68 , pp. 4620-4627
    • Brody, B.A.1    Rhee, S.S.2    Hunter, E.3
  • 93
    • 0028271720 scopus 로고    scopus 로고
    • Ragheb J.A., AndersonW.F. (1994) pH-independent murine leukemia virus ecotropic envelope-mediated cell fusion: implications for the role of the R peptide and p12E TM in viral entry. J Virol 68: 3220-31.
    • Ragheb J.A., AndersonW.F. (1994) pH-independent murine leukemia virus ecotropic envelope-mediated cell fusion: implications for the role of the R peptide and p12E TM in viral entry. J Virol 68: 3220-31.
  • 94
    • 0028047579 scopus 로고
    • Function of the cytoplasmic domain of a retroviral transmembrane protein: P15E-p2E cleavage activates the membrane fusion capability of the murine leukemia virus Env protein
    • Rein A., Mirro J., Haynes J.G., Ernst S.M., Nagashima K. (1994) Function of the cytoplasmic domain of a retroviral transmembrane protein: p15E-p2E cleavage activates the membrane fusion capability of the murine leukemia virus Env protein. J Virol 68: 1773-81.
    • (1994) J Virol , vol.68 , pp. 1773-1781
    • Rein, A.1    Mirro, J.2    Haynes, J.G.3    Ernst, S.M.4    Nagashima, K.5
  • 95
    • 0037225838 scopus 로고    scopus 로고
    • Human T-cell leukemia virus type 1 envelope-mediated syncytium formation can be activated in resistant Mammalian cell lines by a carboxy-terminal truncation of the envelope cytoplasmic domain
    • Kim F.J., Manel N., Boublik Y., Battini J.L., Sitbon M. (2003) Human T-cell leukemia virus type 1 envelope-mediated syncytium formation can be activated in resistant Mammalian cell lines by a carboxy-terminal truncation of the envelope cytoplasmic domain. J Virol 77: 963-9.
    • (2003) J Virol , vol.77 , pp. 963-969
    • Kim, F.J.1    Manel, N.2    Boublik, Y.3    Battini, J.L.4    Sitbon, M.5
  • 96
    • 0027428352 scopus 로고
    • Cell fusion activity of the simian immunodeficiency virus envelope protein is modulated by the intracytoplasmic domain
    • Ritter G.D., Jr., Mulligan M.J., Lydy S.L., Compans R.W. (1993) Cell fusion activity of the simian immunodeficiency virus envelope protein is modulated by the intracytoplasmic domain. Virology 197: 255-64.
    • (1993) Virology , vol.197 , pp. 255-264
    • Ritter Jr., G.D.1    Mulligan, M.J.2    Lydy, S.L.3    Compans, R.W.4
  • 97
    • 0028112013 scopus 로고
    • Effects of cytoplasmic domain length on cell surface expression and syncytium-forming capacity of the simian immunodeficiency virus envelope glycoprotein
    • Spies C.P., Compans R.W. (1994) Effects of cytoplasmic domain length on cell surface expression and syncytium-forming capacity of the simian immunodeficiency virus envelope glycoprotein. Virology 203: 8-19.
    • (1994) Virology , vol.203 , pp. 8-19
    • Spies, C.P.1    Compans, R.W.2
  • 98
    • 0026713860 scopus 로고
    • Truncation of the human immunodeficiency virus type 1 transmembrane glycoprotein cytoplasmic domain blocks virus infectivity
    • Dubay J.W., Roberts S.J., Hahn B.H., Hunter E. (1992) Truncation of the human immunodeficiency virus type 1 transmembrane glycoprotein cytoplasmic domain blocks virus infectivity. J Virol 66: 6616-25.
    • (1992) J Virol , vol.66 , pp. 6616-6625
    • Dubay, J.W.1    Roberts, S.J.2    Hahn, B.H.3    Hunter, E.4
  • 99
    • 0026741425 scopus 로고
    • Retained in vitro infectivity and cytopathogenicity of HIV-1 despite truncation of the C-terminal tail of the env gene product
    • Wilk T., Pfeiffer T., Bosch V. (1992) Retained in vitro infectivity and cytopathogenicity of HIV-1 despite truncation of the C-terminal tail of the env gene product. Virology 189: 167-77.
    • (1992) Virology , vol.189 , pp. 167-177
    • Wilk, T.1    Pfeiffer, T.2    Bosch, V.3
  • 100
    • 34347233854 scopus 로고    scopus 로고
    • HIV-1 escape from the entry-inhibiting effects of a cholesterol-binding compound via cleavage of gp41 by the viral protease
    • Waheed A.A., Ablan S.D., Roser J.D., Sowder R.C., Schaffner C.P., Chertova E., Freed E. O. (2007) HIV-1 escape from the entry-inhibiting effects of a cholesterol-binding compound via cleavage of gp41 by the viral protease. Proc Natl Acad Sci USA 104: 8467-71.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 8467-8471
    • Waheed, A.A.1    Ablan, S.D.2    Roser, J.D.3    Sowder, R.C.4    Schaffner, C.P.5    Chertova, E.6    Freed, E.O.7
  • 101
    • 33644830997 scopus 로고    scopus 로고
    • Maturation of the viral core enhances the fusion of HIV-1 particles with primary human T cells and monocyte-derived macrophages
    • Jiang J., Aiken C. (2006) Maturation of the viral core enhances the fusion of HIV-1 particles with primary human T cells and monocyte-derived macrophages. Virology 346: 460-8.
    • (2006) Virology , vol.346 , pp. 460-468
    • Jiang, J.1    Aiken, C.2
  • 102
    • 0347319099 scopus 로고    scopus 로고
    • Regulation of human immunodeficiency virus type 1 Env-mediated membrane fusion by viral protease activity
    • Murakami T., Ablan S., Freed E.O., Tanaka Y. (2004) Regulation of human immunodeficiency virus type 1 Env-mediated membrane fusion by viral protease activity. J Virol 78: 1026-31.
    • (2004) J Virol , vol.78 , pp. 1026-1031
    • Murakami, T.1    Ablan, S.2    Freed, E.O.3    Tanaka, Y.4
  • 103
    • 1842457792 scopus 로고    scopus 로고
    • Coupling of human immunodeficiency virus type 1 fusion to virion maturation: A novel role of the gp41 cytoplasmic tail
    • Wyma D.J., Jiang J., Shi J., Zhou J., Lineberger J.E., Miller M.D., Aiken C. (2004) Coupling of human immunodeficiency virus type 1 fusion to virion maturation: a novel role of the gp41 cytoplasmic tail. J Virol 78: 3429-35.
    • (2004) J Virol , vol.78 , pp. 3429-3435
    • Wyma, D.J.1    Jiang, J.2    Shi, J.3    Zhou, J.4    Lineberger, J.E.5    Miller, M.D.6    Aiken, C.7
  • 104
    • 35348908350 scopus 로고    scopus 로고
    • Maturation-dependent human immunodeficiency virus type 1 particle fusion requires a carboxyl-terminal region of the gp41 cytoplasmic tail
    • Jiang J., Aiken C. (2007) Maturation-dependent human immunodeficiency virus type 1 particle fusion requires a carboxyl-terminal region of the gp41 cytoplasmic tail. J Virol 81: 9999-10008.
    • (2007) J Virol , vol.81 , pp. 9999-10008
    • Jiang, J.1    Aiken, C.2


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