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Volumn 80, Issue 6, 2006, Pages 2924-2932

Recruitment of the adaptor protein 2 complex by the human immunodeficiency virus type 2 envelope protein is necessary for high levels of virus release

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; VIRUS ENVELOPE PROTEIN; VPU PROTEIN;

EID: 33644756661     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.80.6.2924-2932.2006     Document Type: Article
Times cited : (34)

References (54)
  • 1
    • 14744281049 scopus 로고    scopus 로고
    • Functional domains within the human immunodeficiency virus type 2 envelope protein required to enhance virus production
    • Abada, P., B. Noble, and P. M. Cannon. 2005. Functional domains within the human immunodeficiency virus type 2 envelope protein required to enhance virus production. J. Virol. 79:3627-3638.
    • (2005) J. Virol. , vol.79 , pp. 3627-3638
    • Abada, P.1    Noble, B.2    Cannon, P.M.3
  • 2
    • 0028297360 scopus 로고
    • Distinct effects in primary macrophages and lymphocytes of the human immunodeficiency virus type 1 accessory genes vpr, vpu, and nef: Mutational analysis of a primary HIV-1 isolate
    • Balliet, J. W., D. L. Kolson, G. Eiger, F. M. Kim, K. A. McGann, A. Srinivasan, and R. Collman. 1994. Distinct effects in primary macrophages and lymphocytes of the human immunodeficiency virus type 1 accessory genes vpr, vpu, and nef: mutational analysis of a primary HIV-1 isolate. Virology 200:623-631.
    • (1994) Virology , vol.200 , pp. 623-631
    • Balliet, J.W.1    Kolson, D.L.2    Eiger, G.3    Kim, F.M.4    McGann, K.A.5    Srinivasan, A.6    Collman, R.7
  • 3
    • 27644598271 scopus 로고    scopus 로고
    • Interaction of HIV-1 Gag with the clathrin-associated adaptor AP-2
    • Batonick, M., M. Favre, M. Boge, P. Spearman, S. Honing, and M. Thali. 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
  • 4
    • 0032546927 scopus 로고    scopus 로고
    • A membrane-proximal tyrosine-based signal mediates intcrnalization 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 intcrnalization 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
  • 5
    • 0038795645 scopus 로고    scopus 로고
    • Signals for sorting of transmembrane proteins to endosomes and lysosomes
    • Bonifacino, J. S., and L. M. Trauh. 2003. Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu. Rev. Biochem. 72:395-447.
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 395-447
    • Bonifacino, J.S.1    Trauh, L.M.2
  • 6
    • 0030052467 scopus 로고    scopus 로고
    • The envelope glycoprotein of human immunodeficiency virus type 2 enhances viral particle release: A Vpu-like factor?
    • Bour, S., U. Schubert, K. Peden, and K. Strebel. 1996. The envelope glycoprotein of human immunodeficiency virus type 2 enhances viral particle release: a Vpu-like factor? J. Virol. 70:820-829.
    • (1996) J. Virol. , vol.70 , pp. 820-829
    • Bour, S.1    Schubert, U.2    Peden, K.3    Strebel, K.4
  • 7
    • 0029956763 scopus 로고    scopus 로고
    • The human immunodeficiency virus (HIV) type 2 envelope protein is a functional complement to HIV type 1 Vpu that enhances particle release of heterologous retroviruses
    • Bour, S., and K. Strebel. 1996. The human immunodeficiency virus (HIV) type 2 envelope protein is a functional complement to HIV type 1 Vpu that enhances particle release of heterologous retroviruses. J. Virol. 70: 8285-8300.
    • (1996) J. Virol. , vol.70 , pp. 8285-8300
    • Bour, S.1    Strebel, K.2
  • 8
    • 0032889496 scopus 로고    scopus 로고
    • Lack of effect of cytoplasmic tail truncations on human immunodeficiency virus type 2 ROD Env particle release activity
    • Bour, S. P., C. Aberham, C. Perrin, and K. Strebel. 1999. Lack of effect of cytoplasmic tail truncations on human immunodeficiency virus type 2 ROD Env particle release activity. J. Virol. 73:778-782.
    • (1999) J. Virol. , vol.73 , pp. 778-782
    • Bour, S.P.1    Aberham, C.2    Perrin, C.3    Strebel, K.4
  • 9
    • 0033590168 scopus 로고    scopus 로고
    • Rapid and efficient cell-to-cell transmission of human immunodeficiency virus infection from monocyte-derived macrophages to peripheral blood lymphocytes
    • Carr, J. M., H. Hocking, P. Li, and C. J. Burrell. 1999. Rapid and efficient cell-to-cell transmission of human immunodeficiency virus infection from monocyte-derived macrophages to peripheral blood lymphocytes. Virology 265:319-329.
    • (1999) Virology , vol.265 , pp. 319-329
    • Carr, J.M.1    Hocking, H.2    Li, P.3    Burrell, C.J.4
  • 10
    • 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
  • 11
    • 0026085294 scopus 로고
    • Characterization of the antigenic domains of the major core protein (p26) of equine infectious anemia virus
    • Chong, Y. H., S. L. Payne, C. J. Issel, R. C. Montelaro, and K. E. Rushlow. 1991. Characterization of the antigenic domains of the major core protein (p26) of equine infectious anemia virus. J. Virol. 65:1007-1012.
    • (1991) J. Virol. , vol.65 , pp. 1007-1012
    • Chong, Y.H.1    Payne, S.L.2    Issel, C.J.3    Montelaro, R.C.4    Rushlow, K.E.5
  • 12
    • 9744221135 scopus 로고    scopus 로고
    • Retrovirus budding
    • Demirov, D. G., and E. O. Freed. 2004. Retrovirus budding. Virus Res. 106:87-102.
    • (2004) Virus Res. , vol.106 , pp. 87-102
    • Demirov, D.G.1    Freed, E.O.2
  • 13
    • 0036133283 scopus 로고    scopus 로고
    • The late domain of human immunodeficiency virus type 1 p6 promotes virus release in a cell type-dependent manner
    • Demirov, D. G., J. M. Orenstein, and E. O. Freed. 2002. The late domain of human immunodeficiency virus type 1 p6 promotes virus release in a cell type-dependent manner. J. Virol. 76:105-117.
    • (2002) J. Virol. , vol.76 , pp. 105-117
    • Demirov, D.G.1    Orenstein, J.M.2    Freed, E.O.3
  • 14
    • 0034991502 scopus 로고    scopus 로고
    • Viral protein U (Vpu)-mediated enhancement of human immunodeficiency virus type 1 particle release depends on the rate of cellular proliferation
    • Deora, A., and L. Ratner. 2001. Viral protein U (Vpu)-mediated enhancement of human immunodeficiency virus type 1 particle release depends on the rate of cellular proliferation. J. Virol. 75:6714-6718.
    • (2001) J. Virol. , vol.75 , pp. 6714-6718
    • Deora, A.1    Ratner, L.2
  • 15
    • 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
    • 0036520341 scopus 로고    scopus 로고
    • Amiloride derivatives block ion channel activity and enhancement of virus-like particle budding caused by HIV-1 protein Vpu
    • Ewart, G. D., K. Mills, G. B. Cox, and P. W. Gage. 2002. Amiloride derivatives block ion channel activity and enhancement of virus-like particle budding caused by HIV-1 protein Vpu. Eur. Biophys. J. 31:26-35.
    • (2002) Eur. Biophys. J. , vol.31 , pp. 26-35
    • Ewart, G.D.1    Mills, K.2    Cox, G.B.3    Gage, P.W.4
  • 18
    • 0028913261 scopus 로고
    • Unidirectional budding of HIV-1 at the site of cell-to-cell contact is associated with co-polarization of intercellular adhesion molecules and HIV-1 viral matrix protein
    • Fais, S., M. R. Capobianchi, I. Abbate, C. Castilletti, M. Gentile, P. Cordiali Fei, F. Ameglio, and F. Oianzani. 1995. Unidirectional budding of HIV-1 at the site of cell-to-cell contact is associated with co-polarization of intercellular adhesion molecules and HIV-1 viral matrix protein. AIDS 9:329-335.
    • (1995) AIDS , vol.9 , pp. 329-335
    • Fais, S.1    Capobianchi, M.R.2    Abbate, I.3    Castilletti, C.4    Gentile, M.5    Cordiali Fei, P.6    Ameglio, F.7    Oianzani, F.8
  • 20
    • 0024429254 scopus 로고
    • Assembly and release of HIV-1 precursor Pr55gag virus-like particles from recombinant baculovirus-infected insect cells
    • Gheysen, D., E. Jacobs, F. de Foresta, C. Thiriart, M. Francotte, D. Thines, and M. De Wilde. 1989. Assembly and release of HIV-1 precursor Pr55gag virus-like particles from recombinant baculovirus-infected insect cells. Cell 59:103-112.
    • (1989) Cell , vol.59 , pp. 103-112
    • Gheysen, D.1    Jacobs, E.2    De Foresta, F.3    Thiriart, C.4    Francotte, M.5    Thines, D.6    De Wilde, M.7
  • 21
    • 0027306176 scopus 로고
    • Vpu protein of human immunodeficiency virus type 1 enhances the release of capsids produced by gag gene constructs of widely divergent retroviruses
    • Gottlinger, H. G., T. Dorfman, E. A. Cohen, and W. A. Haseltine. 1993. Vpu protein of human immunodeficiency virus type 1 enhances the release of capsids produced by gag gene constructs of widely divergent retroviruses. Proc. Natl. Acad. Sci. USA 90:7381-7385.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7381-7385
    • Gottlinger, H.G.1    Dorfman, T.2    Cohen, E.A.3    Haseltine, W.A.4
  • 22
    • 3042839154 scopus 로고    scopus 로고
    • Vpu: A multifunctional protein that enhances the pathogenesis of human immunodeficiency virus type 1
    • Hout, D. R., E. R. Mulcahy, E. Pacyniak, L. M. Gomez, M. L. Gomez, and E. B. Stephens. 2004. Vpu: a multifunctional protein that enhances the pathogenesis of human immunodeficiency virus type 1. Curr. HIV Res. 2:255-270.
    • (2004) Curr. HIV Res. , vol.2 , pp. 255-270
    • Hout, D.R.1    Mulcahy, E.R.2    Pacyniak, E.3    Gomez, L.M.4    Gomez, M.L.5    Stephens, E.B.6
  • 23
    • 0033049762 scopus 로고    scopus 로고
    • Compatibility of Vpu-like activity in the four groups of primate immunodeficiency viruses
    • Iida, S., T. Fukumori, Y. Oshima, H. Akari, A. H. Koyama, and A. Adachi. 1999. Compatibility of Vpu-like activity in the four groups of primate immunodeficiency viruses. Virus Gene 18:183-187.
    • (1999) Virus Gene , vol.18 , pp. 183-187
    • Iida, S.1    Fukumori, T.2    Oshima, Y.3    Akari, H.4    Koyama, A.H.5    Adachi, A.6
  • 24
    • 1642540589 scopus 로고    scopus 로고
    • HIV-1 cell to cell transfer across an Env-induced, actin-dependent synapse
    • Jolly, C., K. Kashefi, M. Hollinshead, and Q. J. Sattentau. 2004. HIV-1 cell to cell transfer across an Env-induced, actin-dependent synapse. J. Exp. Med. 199:283-293.
    • (2004) J. Exp. Med. , vol.199 , pp. 283-293
    • Jolly, C.1    Kashefi, K.2    Hollinshead, M.3    Sattentau, Q.J.4
  • 25
    • 0036148338 scopus 로고    scopus 로고
    • Functional replacement and positional dependence of homologous and heterologous L domains in equine infectious anemia virus replication
    • Li, F., C. Chen, B. A. Puffer, and R. C. Montelaro. 2002. Functional replacement and positional dependence of homologous and heterologous L domains in equine infectious anemia virus replication. J. Virol. 76:1569-1577.
    • (2002) J. Virol. , vol.76 , pp. 1569-1577
    • Li, F.1    Chen, C.2    Puffer, B.A.3    Montelaro, R.C.4
  • 26
    • 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. Coben, 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    Coben, E.A.4    Lemay, G.5
  • 27
    • 0031039756 scopus 로고    scopus 로고
    • The membrane-proximal intracytoplasmic tyrosine residue of HIV-1 envelope glyeoprotein 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 glyeoprotein 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
  • 28
    • 0142123069 scopus 로고    scopus 로고
    • Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins
    • Martin-Serrano, J., A. Yarovoy, D. Perez-Caballero, and P. D. Bieniasz. 2003. Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins. Proc. Natl. Acad. Sci. USA 100:12414-12419.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12414-12419
    • Martin-Serrano, J.1    Yarovoy, A.2    Perez-Caballero, D.3    Bieniasz, P.D.4
  • 30
  • 31
    • 0347993084 scopus 로고    scopus 로고
    • Evidence that HIV budding in primary macrophages occurs through the exosome release pathway
    • Nguyen, D. G., A. Booth, S. J. Gould, and J. E. Hildreth. 2003. Evidence that HIV budding in primary macrophages occurs through the exosome release pathway. J. Biol. Chem. 278:52347-52354.
    • (2003) J. Biol. Chem. , vol.278 , pp. 52347-52354
    • Nguyen, D.G.1    Booth, A.2    Gould, S.J.3    Hildreth, J.E.4
  • 32
    • 33644770609 scopus 로고    scopus 로고
    • Unpublished observations
    • Noble, B., and P. M. Cannon. Unpublished observations.
    • Noble, B.1    Cannon, P.M.2
  • 33
  • 35
    • 0347634393 scopus 로고    scopus 로고
    • Cell-type-dependent targeting of human immunodeficiency virus type I assembly to the plasma membrane and the multivesicular body
    • Ono, A., and E. O. Freed. 2004. Cell-type-dependent targeting of human immunodeficiency virus type I assembly to the plasma membrane and the multivesicular body. J. Virol. 78:1552-1563.
    • (2004) J. Virol. , vol.78 , pp. 1552-1563
    • Ono, A.1    Freed, E.O.2
  • 37
    • 0025822399 scopus 로고
    • Human immunodeficiency virus envelope protein determines the site of virus release in polarized epithelial cells
    • Owens, R. J., J. W. Dubay, E. Hunter, and R. W. Compans. 1991. Human immunodeficiency virus envelope protein determines the site of virus release in polarized epithelial cells. Proc. Natl. Acad. Sci. USA 88:3987-3991.
    • (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
  • 38
    • 0036184661 scopus 로고    scopus 로고
    • Budding of equine infectious anemia virus is insensitive to proteasome inhibitors
    • Patnaik, A., V. Chau, F. Li, R. C. Montelaro, and J. W. Wills. 2002. Budding of equine infectious anemia virus is insensitive to proteasome inhibitors. J. Virol. 76:2641-2647.
    • (2002) J. Virol. , vol.76 , pp. 2641-2647
    • Patnaik, A.1    Chau, V.2    Li, F.3    Montelaro, R.C.4    Wills, J.W.5
  • 39
    • 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
  • 40
    • 0028233744 scopus 로고
    • The role of cell-to-cell transmission in HIV infection
    • Phillips, D. M. 1994. The role of cell-to-cell transmission in HIV infection. AIDS 8:719-731.
    • (1994) AIDS , vol.8 , pp. 719-731
    • Phillips, D.M.1
  • 41
    • 0031797730 scopus 로고    scopus 로고
    • Equine infectious anemia virus Gag polyprotein late domain specifically recruits cellular AP-2 adapter protein complexes during virion assembly
    • Puffer, B. A., S. C. Watkins, and R. C. Montelaro. 1998. Equine infectious anemia virus Gag polyprotein late domain specifically recruits cellular AP-2 adapter protein complexes during virion assembly. J. Virol. 72:10218-10221.
    • (1998) J. Virol. , vol.72 , pp. 10218-10221
    • Puffer, B.A.1    Watkins, S.C.2    Montelaro, R.C.3
  • 42
    • 0028271720 scopus 로고
    • pH-independent murine leukemia virus ecotropic envelope-mediated cell fusion: Implications for the role of the R peptide and p12E TM in viral entry
    • Ragheb, J. A., and W. F. Anderson. 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. 68:3220-3231.
    • (1994) J. Virol. , vol.68 , pp. 3220-3231
    • Ragheb, J.A.1    Anderson, W.F.2
  • 43
    • 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., J. Mirro, J. G. Haynes, S. M. Ernst, and K. Nagashima. 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. 68:1773-1781.
    • (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
  • 44
    • 0029918147 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 2 glycoprotein enhancement of particle budding: Role of the cytoplasmic domain
    • Ritter, G. D., Jr., G. Yamshchikov, S. J. Cohen, and M. J. Mulligan. 1996. Human immunodeficiency virus type 2 glycoprotein enhancement of particle budding: role of the cytoplasmic domain. J. Virol. 70:2669-2673.
    • (1996) J. Virol. , vol.70 , pp. 2669-2673
    • Ritter Jr., G.D.1    Yamshchikov, G.2    Cohen, S.J.3    Mulligan, M.J.4
  • 45
    • 0028863722 scopus 로고
    • Function of human immunodeficiency virus type 1 Vpu protein in various cell types
    • Sakai, H., K. Tokunaga, M. Kawamura, and A. Adachi. 1995. Function of human immunodeficiency virus type 1 Vpu protein in various cell types. J. Gen. Virol. 76:2717-2722.
    • (1995) J. Gen. Virol. , vol.76 , pp. 2717-2722
    • Sakai, H.1    Tokunaga, K.2    Kawamura, M.3    Adachi, A.4
  • 46
    • 0028857927 scopus 로고
    • Augmentation of virus secretion by the human immunodeficiency virus type 1 Vpu protein is cell type independent and occurs in cultured human primary macrophages and lymphocytes
    • Schubert, U., K. A. Clouse, and K. Strebel. 1995. Augmentation of virus secretion by the human immunodeficiency virus type 1 Vpu protein is cell type independent and occurs in cultured human primary macrophages and lymphocytes. J. Virol. 69:7699-7711.
    • (1995) J. Virol. , vol.69 , pp. 7699-7711
    • Schubert, U.1    Clouse, K.A.2    Strebel, K.3
  • 47
    • 0030273297 scopus 로고    scopus 로고
    • HIV-1 particle release mediated by Vpu is distinct from that mediated by p6
    • Schwartz, M. D., R. J. Geraghty, and A. T. Panganiban. 1996. HIV-1 particle release mediated by Vpu is distinct from that mediated by p6. Virology 224:302-309.
    • (1996) Virology , vol.224 , pp. 302-309
    • Schwartz, M.D.1    Geraghty, R.J.2    Panganiban, A.T.3
  • 50
    • 0036059017 scopus 로고    scopus 로고
    • Deletion of the vpu sequences prior to the env in a simian-human immunodeficiency virus results in enhanced Env precursor synthesis but is less pathogenic for pig-tailed macaques
    • Stephens, E. B., C. McCormick, E. Pacyniak, D. Griffin, D. M. Pinson, F. Sun, W. Nothnick, S. W. Wong, R. Gunderson, N. E. Berman, and D. K. Singh. 2002. Deletion of the vpu sequences prior to the env in a simian-human immunodeficiency virus results in enhanced Env precursor synthesis but is less pathogenic for pig-tailed macaques. Virology 293:252-261.
    • (2002) Virology , vol.293 , pp. 252-261
    • Stephens, E.B.1    McCormick, C.2    Pacyniak, E.3    Griffin, D.4    Pinson, D.M.5    Sun, F.6    Nothnick, W.7    Wong, S.W.8    Gunderson, R.9    Berman, N.E.10    Singh, D.K.11
  • 51
    • 0141844660 scopus 로고    scopus 로고
    • AIPI/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding
    • Strack, B., A. Calistri, S. Craig, W. Popova, and H. G. Gottlinger. 2003. AIPI/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding. Cell 114:689-699.
    • (2003) Cell , vol.114 , pp. 689-699
    • Strack, B.1    Calistri, A.2    Craig, S.3    Popova, W.4    Gottlinger, H.G.5
  • 52
    • 0024381228 scopus 로고
    • Molecular and biochemical analyses of human immunodeficiency virus type 1 vpu protein
    • Strebel, K., T. Klimkait, F. Maldarelli, and M. A. Martin. 1989. Molecular and biochemical analyses of human immunodeficiency virus type 1 vpu protein. J. Virol. 63:3784-3791.
    • (1989) J. Virol. , vol.63 , pp. 3784-3791
    • Strebel, K.1    Klimkait, T.2    Maldarelli, F.3    Martin, M.A.4
  • 54
    • 0344303622 scopus 로고    scopus 로고
    • Viral protein U counteracts a human host cell restriction that inhibits HIV-1 particle production
    • Varthakavi, V., R. M. Smith, S. P. Bour, K. Strebel, and P. Spearman. 2003. Viral protein U counteracts a human host cell restriction that inhibits HIV-1 particle production. Proc. Natl. Acad. Sci. USA 100:15154-15159.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 15154-15159
    • Varthakavi, V.1    Smith, R.M.2    Bour, S.P.3    Strebel, K.4    Spearman, P.5


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