메뉴 건너뛰기




Volumn 410, Issue 4, 2011, Pages 582-608

HIV-1 envelope glycoprotein biosynthesis, trafficking, and incorporation

Author keywords

Assembly; Envelope glycoprotein; HIV 1; Retrovirus; Trafficking

Indexed keywords

GAG PROTEIN; GLYCOPROTEIN GP 120; GLYCOPROTEIN GP 160; GLYCOPROTEIN GP 41; HUMAN IMMUNODEFICIENCY VIRUS PROTEINASE;

EID: 80051737642     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.04.042     Document Type: Review
Times cited : (342)

References (307)
  • 1
    • 0033012398 scopus 로고    scopus 로고
    • Chemokine receptors as HIV-1 coreceptors: Roles in viral entry, tropism, and disease
    • DOI 10.1146/annurev.immunol.17.1.657
    • Berger, E. A., Murphy, P. M. & Farber, J. M. (1999). Chemokine receptors as HIV-1 coreceptors: roles in viral entry, tropism, and disease. Annu. Rev. Immunol. 17, 657-700. (Pubitemid 29241137)
    • (1999) Annual Review of Immunology , vol.17 , pp. 657-700
    • Berger, E.A.1    Murphy, P.M.2    Farber, J.M.3
  • 2
    • 13744252968 scopus 로고    scopus 로고
    • Involvement of clathrin-mediated endocytosis in human immunodeficiency virus type 1 entry
    • DOI 10.1128/JVI.79.3.1581-1594.2005
    • Daecke, J., Fackler, O. T., Dittmar, M. T. & Kräusslich, H.-G. (2005). Involvement of clathrin-mediated en-docytosis in human immunodeficiency virus type 1 entry. J. Virol. 79, 1581-1594. (Pubitemid 40459105)
    • (2005) Journal of Virology , vol.79 , Issue.3 , pp. 1581-1594
    • Daecke, J.1    Fackler, O.T.2    Dittmar, M.T.3    Krausslich, H.-G.4
  • 3
    • 65249139458 scopus 로고    scopus 로고
    • HIV enters cells via endocy-tosis and dynamin-dependent fusion with endo-somes
    • Miyauchi, K., Kim, Y., Latinovic, O., Morozov, V. & Melikyan, G. B. (2009). HIV enters cells via endocy-tosis and dynamin-dependent fusion with endo-somes. Cell, 137, 433-444.
    • (2009) Cell , vol.137 , pp. 433-444
    • Miyauchi, K.1    Kim, Y.2    Latinovic, O.3    Morozov, V.4    Melikyan, G.B.5
  • 5
    • 79952699891 scopus 로고    scopus 로고
    • Coreceptors and HIV-1 pathogenesis
    • Gorry, P. R. & Ancuta, P. (2011). Coreceptors and HIV-1 pathogenesis. Curr. HIV/AIDS Rep. 8, 45-53.
    • (2011) Curr. HIV/AIDS Rep. , vol.8 , pp. 45-53
    • Gorry, P.R.1    Ancuta, P.2
  • 6
    • 0035524975 scopus 로고    scopus 로고
    • Intracellular trafficking of retroviral genomes during the early phase of infection: Viral exploitation of cellular pathways
    • DOI 10.1002/1521-2254(200111)3:6<517::AID-JGM234>3.0.CO;2-E
    • Goff, S. P. (2001). Intracellular trafficking of retroviral genomes during the early phase of infection: viral exploitation of cellular pathways. J. Gene Med. 3, 517-528. (Pubitemid 33685083)
    • (2001) Journal of Gene Medicine , vol.3 , Issue.6 , pp. 517-528
    • Goff, S.P.1
  • 7
    • 33847139800 scopus 로고    scopus 로고
    • The road to chromatin-nuclear entry of retroviruses
    • Suzuki, Y. & Craigie, R. (2007). The road to chromatin-nuclear entry of retroviruses. Nat. Rev., Microbiol. 5, 187-196.
    • (2007) Nat. Rev., Microbiol. , vol.5 , pp. 187-196
    • Suzuki, Y.1    Craigie, R.2
  • 8
    • 0035078745 scopus 로고    scopus 로고
    • Characterization of intracellular reverse transcription complexes of human immunodeficiency virus type 1
    • DOI 10.1128/JVI.75.8.3626-3635.2001
    • Fassati, A. & Goff, S. P. (2001). Characterization of intracellular reverse transcription complexes of human immunodeficiency virus type 1. J. Virol. 75, 3626-3635. (Pubitemid 32246372)
    • (2001) Journal of Virology , vol.75 , Issue.8 , pp. 3626-3635
    • Fassati, A.1    Goff, S.P.2
  • 11
    • 34250372513 scopus 로고    scopus 로고
    • HIVs and their replication
    • (Knipe, D. M., Howley, P. M., Griffin, D. E., Lamb, R. A., Martin, M. A., Roizman, B. & Straus, S. E., eds), 5th edit. Lippincott Williams & Wilkins, Philadelphia, PA
    • Freed, E. O. & Martin, M. A. (2006). HIVs and their replication. In Fields Virology (Knipe, D. M., Howley, P. M., Griffin, D. E., Lamb, R. A., Martin, M. A., Roizman, B. & Straus, S. E., eds), 5th edit. Lippincott Williams & Wilkins, Philadelphia, PA.
    • (2006) Fields Virology
    • Freed, E.O.1    Martin, M.A.2
  • 12
    • 80051737001 scopus 로고    scopus 로고
    • thesis, assembly, and processing of viral proteins (Coffin, J. M., Hughes, S. H. & Varmus, H. E., eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Swanstrom, R. & Wills, J. W. (1997). Synthesis, assembly, and processing of viral proteins. In Retro-viruses (Coffin, J. M., Hughes, S. H. & Varmus, H. E., eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1997) Syn Retro-viruses
    • Swanstrom, R.1    Wills, J.W.2
  • 13
    • 0032506207 scopus 로고    scopus 로고
    • HIV-1 Gag proteins: Diverse functions in the virus life cycle
    • DOI 10.1006/viro.1998.9398
    • Freed, E. O. (1998). HIV-1 gag proteins: diverse functions in the virus life cycle. Virology, 251, 1-15. (Pubitemid 28527713)
    • (1998) Virology , vol.251 , Issue.1 , pp. 1-15
    • Freed, E.O.1
  • 14
    • 34250347313 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 assembly, release, and maturation
    • Adamson, C. S. & Freed, E. O. (2007). Human immunodeficiency virus type 1 assembly, release, and maturation. Adv. Pharmacol. 55, 347-387.
    • (2007) Adv. Pharmacol. , vol.55 , pp. 347-387
    • Adamson, C.S.1    Freed, E.O.2
  • 15
    • 67649407509 scopus 로고    scopus 로고
    • The cell biology of HIV-1 virion genesis
    • Bieniasz, P. D. (2009). The cell biology of HIV-1 virion genesis. Cell Host Microbe, 5, 550-558.
    • (2009) Cell Host Microbe , vol.5 , pp. 550-558
    • Bieniasz, P.D.1
  • 16
    • 0028218274 scopus 로고
    • Identification of a membrane-binding domain within the amino-terminal region of human immunodeficiency virus type 1 Gag protein which interacts with acidic phospholipids
    • Zhou, W., Parent, L. J., Wills, J. W. & Resh, M. D. (1994). Identification of a membrane-binding domain within the amino-terminal region of human immunodeficiency virus type 1 Gag protein which interacts with acidic phospholipids. J. Virol. 68, 2556-2569.
    • (1994) J. Virol. , vol.68 , pp. 2556-2569
    • Zhou, W.1    Parent, L.J.2    Wills, J.W.3    Resh, M.D.4
  • 21
    • 9744221135 scopus 로고    scopus 로고
    • Retrovirus budding
    • DOI 10.1016/j.virusres.2004.08.007, PII S0168170204003181
    • Demirov, D. G. & Freed, E. O. (2004). Retrovirus budding. Virus Res. 106, 87-102. (Pubitemid 39582739)
    • (2004) Virus Research , vol.106 , Issue.4 SPEC.ISS. , pp. 87-102
    • Demirov, D.G.1    Freed, E.O.2
  • 23
    • 29144474443 scopus 로고    scopus 로고
    • Late budding domains and host proteins in enveloped virus release
    • DOI 10.1016/j.virol.2005.09.044, PII S0042682205005994
    • Bieniasz, P. D. (2006). Late budding domains and host proteins in enveloped virus release. Virology, 344, 55-63. (Pubitemid 41814450)
    • (2006) Virology , vol.344 , Issue.1 , pp. 55-63
    • Bieniasz, P.D.1
  • 24
    • 36248936657 scopus 로고    scopus 로고
    • Beyond Tsg101: The role of Alix in 'ESCRTing' HIV-1
    • DOI 10.1038/nrmicro1790, PII NRMICRO1790
    • Fujii, K., Hurley, J. H. & Freed, E. O. (2007). Beyond Tsg101: the role of Alix in ESCRTing' HIV-1. Nat. Rev., Microbiol. 5, 912-916. (Pubitemid 350131179)
    • (2007) Nature Reviews Microbiology , vol.5 , Issue.12 , pp. 912-916
    • Fujii, K.1    Hurley, J.H.2    Freed, E.O.3
  • 27
    • 80051615759 scopus 로고    scopus 로고
    • New insights into HIV assembly and trafficking
    • press
    • Balasubramaniam, M. & Freed, E. O. (2011). New insights into HIV assembly and trafficking. Physiology, in press.
    • (2011) Physiology
    • Balasubramaniam, M.1    Freed, E.O.2
  • 29
    • 34447285254 scopus 로고    scopus 로고
    • Productive human immunodeficiency virus type 1 assembly takes place at the plasma membrane
    • DOI 10.1128/JVI.00308-07
    • Finzi, A., Orthwein, A., Mercier, J. & Cohen, E. A. (2007). Productive human immunodeficiency virus type 1 assembly takes place at the plasma membrane. J. Virol. 81, 7476-7490. (Pubitemid 47047835)
    • (2007) Journal of Virology , vol.81 , Issue.14 , pp. 7476-7490
    • Finzi, A.1    Orthwein, A.2    Mercier, J.3    Cohen, E.A.4
  • 30
    • 66149085337 scopus 로고    scopus 로고
    • Evidence that productive human immunodeficiency virus type 1 assembly can occur in an intracellular compartment
    • Joshi, A., Ablan, S. D., Soheilian, F., Nagashima, K. & Freed, E. O. (2009). Evidence that productive human immunodeficiency virus type 1 assembly can occur in an intracellular compartment. J. Virol. 83, 5375-5387.
    • (2009) J. Virol. , vol.83 , pp. 5375-5387
    • Joshi, A.1    Ablan, S.D.2    Soheilian, F.3    Nagashima, K.4    Freed, E.O.5
  • 31
    • 34247529467 scopus 로고    scopus 로고
    • In macrophages, HIV-1 assembles into an intracellular plasma membrane domain containing the tetraspanins CD81, CD9, and CD53
    • DOI 10.1083/jcb.200609050
    • 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, 329-341. (Pubitemid 46658643)
    • (2007) Journal of Cell Biology , vol.177 , Issue.2 , pp. 329-341
    • Deneka, M.1    Pelchen-Matthews, A.2    Byland, R.3    Ruiz-Mateos, E.4    Marsh, M.5
  • 32
    • 70349686333 scopus 로고    scopus 로고
    • Ion-abrasion scanning electron microscopy reveals surface-connected tubular conduits in HIV-infected macro-phages
    • Bennett, A. E., Narayan, K., Shi, D., Hartnell, L. M., Gousset, K., He, H. et al. (2009). Ion-abrasion scanning electron microscopy reveals surface-connected tubular conduits in HIV-infected macro-phages. PLoS Pathog. 5, e1000591.
    • (2009) PLoS Pathog. , vol.5
    • Bennett, A.E.1    Narayan, K.2    Shi, D.3    Hartnell, L.M.4    Gousset, K.5    He, H.6
  • 34
    • 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, 311-358.
    • (2005) Adv. Virus Res. , vol.64 , pp. 311-358
    • Ono, A.1    Freed, E.O.2
  • 36
    • 0028788472 scopus 로고
    • The role of human immunodeficiency virus type 1 envelope glycoproteins in virus infection
    • Freed, E. O. & Martin, M. A. (1995). The role of human immunodeficiency virus type 1 envelope glycoproteins in virus infection. J. Biol. Chem. 270, 23883-23886.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23883-23886
    • Freed, E.O.1    Martin, M.A.2
  • 37
    • 0023732248 scopus 로고
    • Topogenic analysis of the human immunodeficiency virus type 1 envelope glycoprotein, gp160, in microsomal membranes
    • DOI 10.1083/jcb.107.5.1677
    • Haffar, O., Dowbenko, D. J. & Berman, P. W. (1988). Topogenic analysis of the human immunodeficiency virus type 1 envelope glycoprotein, gp160, in microsomal membranes. J. Cell Biol. 107, 1677-1687. (Pubitemid 18263541)
    • (1988) Journal of Cell Biology , vol.107 , Issue.5 , pp. 1677-1687
    • Haffar, O.K.1    Dowbenko, D.J.2    Berman, P.W.3
  • 38
    • 0023678874 scopus 로고
    • Expression of membrane-associated and secreted variants of gp160 of human immunodeficiency virus type 1 in vitro and in continuous cell lines
    • Berman, P. W., Nunes, W. M. & Haffar, O. (1988). Expression of membrane-associated and secreted variants of gp160 of human immunodeficiency virus type 1 in vitro and in continuous cell lines. J. Virol. 62, 3135-3142.
    • (1988) J. Virol. , vol.62 , pp. 3135-3142
    • Berman, P.W.1    Nunes, W.M.2    Haffar, O.3
  • 39
    • 0021997051 scopus 로고
    • Major glycoprotein antigens that induce antibodies in AIDS patients are encoded by HTLV-III
    • Allan, J. S., Coligan, J. E., Barin, F., McLane, M. F., Sodroski, J. G., Rosen, C. A. et al. (1985). Major glycoprotein antigens that induce antibodies in AIDS patients are encoded by HTLV-III. Science, 228, 1091-1094. (Pubitemid 15227368)
    • (1985) Science , vol.228 , Issue.4703 , pp. 1091-1094
    • Allan, J.S.1    Coligan, J.E.2    Barin, F.3
  • 40
    • 0025292252 scopus 로고
    • Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells
    • Leonard, C. K., Spellman, M. W., Riddle, L., Harris, R. J., Thomas, J. N. & Gregory, T. J. (1990). Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells. J. Biol. Chem. 265, 10373-10382.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10373-10382
    • Leonard, C.K.1    Spellman, M.W.2    Riddle, L.3    Harris, R.J.4    Thomas, J.N.5    Gregory, T.J.6
  • 41
    • 0027957921 scopus 로고
    • Human immunodeficiency virus type 1 envelope glycoprotein is modified by O-linked oligosaccharides
    • Bernstein, H. B., Tucker, S. P., Hunter, E., Schutzbach, J. S. & Compans, R. W. (1994). Human immunodeficiency virus type 1 envelope glycoprotein is modified by O-linked oligosaccharides. J. Virol. 68, 463-468.
    • (1994) J. Virol. , vol.68 , pp. 463-468
    • Bernstein, H.B.1    Tucker, S.P.2    Hunter, E.3    Schutzbach, J.S.4    Compans, R.W.5
  • 42
  • 43
    • 0024433219 scopus 로고
    • Studies with crosslinking reagents on the oligomeric structure of the env glycoprotein of HIV
    • DOI 10.1016/0042-6822(89)90142-6
    • Schawaller, M., Smith, G. E., Skehel, J. J. & Wiley, D. C. (1989). Studies with crosslinking reagents on the oligomeric structure of the env glycoprotein of HIV. Virology, 172, 367-369. (Pubitemid 19221465)
    • (1989) Virology , vol.172 , Issue.1 , pp. 367-369
    • Schawaller, M.1    Smith, G.E.2    Skehel, J.J.3    Wiley, D.C.4
  • 44
    • 0025095635 scopus 로고
    • Oligomeric structure of the human immunodeficiency virus type 1 envelope glycoprotein
    • Earl, P. L., Doms, R. W. & Moss, B. (1990). Oligomeric structure of the human immunodeficiency virus type 1 envelope glycoprotein. Proc. Natl Acad. Sci. USA, 87, 648-652.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 648-652
    • Earl, P.L.1    Doms, R.W.2    Moss, B.3
  • 45
    • 0026068529 scopus 로고
    • Biological and immunological properties of human immunodeficiency virus type 1 envelope glycoprotein: Analysis of proteins with truncations and deletions expressed by recombinant vaccinia viruses
    • Earl, P. L., Koenig, S. & Moss, B. (1991). Biological and immunological properties of human immunodeficiency virus type 1 envelope glycoprotein: analysis of proteins with truncations and deletions expressed by recombinant vaccinia viruses. J. Virol. 65, 31-41.
    • (1991) J. Virol. , vol.65 , pp. 31-41
    • Earl, P.L.1    Koenig, S.2    Moss, B.3
  • 46
    • 0031057925 scopus 로고    scopus 로고
    • Rapid degradation of CD4 in cells expressing human immunodeficiency virus type 1 Env and Vpu is blocked by proteasome inhibitors
    • Fujita, K., Omura, S. & Silver, J. (1997). Rapid degradation of CD4 in cells expressing human immunodeficiency virus type 1 Env and Vpu is blocked by proteasome inhibitors. J. Gen. Virol. 78, 619-625. (Pubitemid 27116783)
    • (1997) Journal of General Virology , vol.78 , Issue.3 , pp. 619-625
    • Fujita, K.1    Omura, S.2    Silver, J.3
  • 47
    • 0031935031 scopus 로고    scopus 로고
    • CD4 glycoprotein degradation induced by human immunodeficiency virus type 1 Vpu protein requires the function of proteasomes and the ubiquitin- conjugating pathway
    • Schubert, U., Antón, L. C., Bacík, I., Cox, J. H., Bour, S., Bennink, J. R. et al. (1998). CD4 glycoprotein degradation induced by human immunodeficiency virus type 1 Vpu protein requires the function of proteasomes and the ubiquitin-conjugating pathway. J. Virol. 72, 2280-2288. (Pubitemid 28100787)
    • (1998) Journal of Virology , vol.72 , Issue.3 , pp. 2280-2288
    • Schubert, U.1    Anton, L.C.2    Bacik, I.3    Cox, J.H.4    Bour, S.5    Bennink, J.R.6    Orlowski, M.7    Strebel, K.8    Yewdell, J.W.9
  • 48
    • 0032012456 scopus 로고    scopus 로고
    • A novel human WD protein, h-βTrCP, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif
    • Margottin, F., Bour, S. P., Durand, H., Selig, L., Benichou, S., Richard, V. et al. (1998). A novel human WD protein, h-beta TrCp, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif. Mol. Cell, 1, 565-574. (Pubitemid 128374692)
    • (1998) Molecular Cell , vol.1 , Issue.4 , pp. 565-574
    • Margottin, F.1    Bour, S.P.2    Durand, H.3    Selig, L.4    Benichou, S.5    Richard, V.6    Thomas, D.7    Strebel, K.8    Benarous, R.9
  • 49
    • 0026716831 scopus 로고
    • Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gp160
    • DOI 10.1038/360358a0
    • Hallenberger, S., Bosch, V., Angliker, H., Shaw, E., Klenk, H. D. & Garten, W. (1992). Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gp160. Nature, 360, 358-361. (Pubitemid 23000676)
    • (1992) Nature , vol.360 , Issue.6402 , pp. 358-361
    • Hallenberger, S.1    Bosch, V.2    Angliker, H.3    Shaw, E.4    Klenk, H.-D.5    Garten, W.6
  • 50
    • 0023921610 scopus 로고
    • Endoproteolytic cleavage of gp160 is required for the activation of human immunodeficiency virus
    • McCune,J.M., Rabin,L.B., Feinberg,M.B., Lieberman, M., Kosek, J. C., Reyes, G. R. & Weissman, I. L. (1988). Endoproteolytic cleavage of gp160 is required for the activation of human immunodeficiency virus. Cell, 53, 55-67.
    • (1988) Cell , vol.53 , pp. 55-67
    • McCune, J.M.1    Rabin, L.B.2    Feinberg, M.B.3    Lieberman, M.4    Kosek, J.C.5    Reyes, G.R.6    Weissman, I.L.7
  • 51
    • 0024435050 scopus 로고
    • Mutational analysis of the cleavage sequence of the human immunodeficiency virus type 1 envelope glycoprotein precursor gp160
    • Freed, E. O., Myers, D. J. & Risser, R. (1989). Mutational analysis of the cleavage sequence of the human immunodeficiency virus type 1 envelope glycoprotein precursor gp160. J. Virol. 63, 4670-4675. (Pubitemid 19257842)
    • (1989) Journal of Virology , vol.63 , Issue.11 , pp. 4670-4675
    • Freed, E.O.1    Myers, D.J.2    Risser, R.3
  • 52
    • 0029151298 scopus 로고
    • Lysosome-associated membrane protein-1-mediated targeting of the HIV-1 envelope protein to an endosomal/lysosomal compartment enhances its presentation to MHC class II-restricted T cells
    • Rowell, J. F., Ruff, A. L., Guarnieri, F. G., Staveley-O'Carroll, K., Lin, X., Tang, J. et al. (1995). Lysosome-associated membrane protein-1-mediated targeting of the HIV-1 envelope protein to an endosomal/lysosomal compartment enhances its presentation to MHC class II-restricted T cells. J. Immunol. 155, 1818-1828.
    • (1995) J. Immunol. , vol.155 , pp. 1818-1828
    • Rowell, J.F.1    Ruff, A.L.2    Guarnieri, F.G.3    Staveley-O'Carroll, K.4    Lin, X.5    Tang, J.6
  • 53
    • 0029794677 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 envelope protein endocytosis mediated by a highly conserved intrinsic internalization signal in the cytoplasmic domain of gp41 is suppressed in the presence of the Pr55(gag) precursor protein
    • Egan, M. A., Carruth, L. M., Rowell, J. F., Yu, X. & Siliciano, R. F. (1996). Human immunodeficiency virus type 1 envelope protein endocytosis mediated by a highly conserved intrinsic internalization signal in the cytoplasmic domain of gp41 is suppressed in the presence of the Pr55gag precursor protein. J. Virol. 70, 6547-6556. (Pubitemid 26307359)
    • (1996) Journal of Virology , vol.70 , Issue.10 , pp. 6547-6556
    • Egan, M.A.1    Carruth, L.M.2    Rowell, J.F.3    Yu, X.4    Siliciano, R.F.5
  • 55
    • 4444231440 scopus 로고    scopus 로고
    • Retroviral spread by induction of virological synapses
    • DOI 10.1111/j.1600-0854.2004.00209.x
    • Jolly, C. & Sattentau, Q. J. (2004). Retroviral spread by induction of virological synapses. Traffic, 5, 643-650. (Pubitemid 39199128)
    • (2004) Traffic , vol.5 , Issue.9 , pp. 643-650
    • Jolly, C.1    Sattentau, Q.J.2
  • 56
    • 0038025223 scopus 로고    scopus 로고
    • Recruitment of HIV and its receptors to dendritic cell-T cell junctions
    • DOI 10.1126/science.1084238
    • McDonald, D., Wu, L., Bohks, S. M., KewalRamani, V. N., Unutmaz, D. & Hope, T. J. (2003). Recruitment of HIV and its receptors to dendritic cell-T cell junctions. Science, 300, 1295-1297. (Pubitemid 36618241)
    • (2003) Science , vol.300 , Issue.5623 , pp. 1295-1297
    • McDonald, D.1    Wu, L.2    Bohks, S.M.3    KewalRamani, V.N.4    Unutmaz, D.5    Hope, T.J.6
  • 57
    • 79952073945 scopus 로고    scopus 로고
    • Cell-to-cell spread of retrovi-ruses
    • Sattentau, Q. J. (2010). Cell-to-cell spread of retrovi-ruses. Viruses, 2, 1306-1321.
    • (2010) Viruses , vol.2 , pp. 1306-1321
    • Sattentau, Q.J.1
  • 58
    • 79952067916 scopus 로고    scopus 로고
    • T cell polarization at the virological synapse
    • Jolly, C. (2010). T cell polarization at the virological synapse. Viruses, 2, 1261-1278.
    • (2010) Viruses , vol.2 , pp. 1261-1278
    • Jolly, C.1
  • 59
    • 77956643036 scopus 로고    scopus 로고
    • Virus cell-to-cell transmission
    • Mothes, W., Sherer, N. M., Jin, J. & Zhong, P. (2010). Virus cell-to-cell transmission. J. Virol. 84, 8360-8368.
    • (2010) J. Virol. , vol.84 , pp. 8360-8368
    • Mothes, W.1    Sherer, N.M.2    Jin, J.3    Zhong, P.4
  • 61
    • 1642540589 scopus 로고    scopus 로고
    • HIV-1 Cell to Cell Transfer across an Env-induced, Actin-dependent Synapse
    • DOI 10.1084/jem.20030648
    • Jolly, C., Kashefi, K., Hollinshead, M. & Sattentau, Q. J. (2004). HIV-1 cell to cell transfer across an Env-induced, actin-dependent synapse. J. Exp. Med. 199, 283-293. (Pubitemid 38129707)
    • (2004) Journal of Experimental Medicine , vol.199 , Issue.2 , pp. 283-293
    • Jolly, C.1    Kashefi, K.2    Hollinshead, M.3    Sattentau, Q.J.4
  • 62
    • 37049018852 scopus 로고    scopus 로고
    • Adhesion molecule interactions facilitate human immunodeficiency virus type 1-induced virological synapse formation between T cells
    • DOI 10.1128/JVI.01585-07
    • Jolly, C., Mitar, I. & Sattentau, Q. J. (2007). Adhesion molecule interactions facilitate human immunodeficiency virus type 1-induced virological synapse formation between T cells. J. Virol. 81, 13916-13921. (Pubitemid 350247884)
    • (2007) Journal of Virology , vol.81 , Issue.24 , pp. 13916-13921
    • Jolly, C.1    Mitar, I.2    Sattentau, Q.J.3
  • 63
    • 34249823098 scopus 로고    scopus 로고
    • Requirement for an intact T-cell actin and tubulin cytoskeleton for efficient assembly and spread of human immunodeficiency virus type 1
    • DOI 10.1128/JVI.01469-06
    • Jolly, C., Mitar, I. & Sattentau, Q. J. (2007). Requirement for an intact T-cell actin and tubulin cytoskeleton for efficient assembly and spread of human immunodeficiency virus type 1. J. Virol. 81, 5547-5560. (Pubitemid 46846995)
    • (2007) Journal of Virology , vol.81 , Issue.11 , pp. 5547-5560
    • Jolly, C.1    Mitar, I.2    Sattentau, Q.J.3
  • 64
    • 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
    • DOI 10.1128/JVI.01845-06
    • 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, 7873-7884. (Pubitemid 47101473)
    • (2007) Journal of Virology , vol.81 , Issue.15 , pp. 7873-7884
    • Jolly, C.1    Sattentau, Q.J.2
  • 65
    • 33847366661 scopus 로고    scopus 로고
    • Retroviruses can establish filopodial bridges for efficient cell-to-cell transmission
    • DOI 10.1038/ncb1544, PII NCB1544
    • Sherer, N. M., Lehmann, M. J., Jimenez-Soto, L. F., Horensavitz, C., Pypaert, M. & Mothes, W. (2007). Retroviruses can establish filopodial bridges for efficient cell-to-cell transmission. Nat. Cell Biol. 9, 310-315. (Pubitemid 46344610)
    • (2007) Nature Cell Biology , vol.9 , Issue.3 , pp. 310-315
    • Sherer, N.M.1    Lehmann, M.J.2    Jimenez-Soto, L.F.3    Horensavitz, C.4    Pypaert, M.5    Mothes, W.6
  • 66
    • 77949406401 scopus 로고    scopus 로고
    • Directional spread of surface-associated retroviruses regulated by differential virus-cell interactions
    • Sherer, N. M., Jin, J. & Mothes, W. (2010). Directional spread of surface-associated retroviruses regulated by differential virus-cell interactions. J. Virol. 84, 3248-3258.
    • (2010) J. Virol. , vol.84 , pp. 3248-3258
    • Sherer, N.M.1    Jin, J.2    Mothes, W.3
  • 67
    • 68049136145 scopus 로고    scopus 로고
    • Assembly of the murine leukemia virus is directed towards sites of cell-cell contact
    • Jin, J., Sherer, N. M., Heidecker, G., Derse, D. & Mothes, W. (2009). Assembly of the murine leukemia virus is directed towards sites of cell-cell contact. PLoS Biol. 7, e1000163.
    • (2009) PLoS Biol. , vol.7
    • Jin, J.1    Sherer, N.M.2    Heidecker, G.3    Derse, D.4    Mothes, W.5
  • 68
    • 79952072460 scopus 로고    scopus 로고
    • Macrophages and cell-cell spread of HIV-1
    • Waki, K. & Freed, E. O. (2010). Macrophages and cell-cell spread of HIV-1. Viruses, 2, 1603-1620.
    • (2010) Viruses , vol.2 , pp. 1603-1620
    • Waki, K.1    Freed, E.O.2
  • 69
    • 0022459886 scopus 로고
    • Identification and characterization of conserved and variable regions in the envelope gene of HTLV-III/LAV, the retrovirus of AIDS
    • Starcich, B. R., Hahn, B. H., Shaw, G. M., McNeely, P. D., Modrow, S., Wolf, H. et al. (1986). Identification and characterization of conserved and variable regions in the envelope gene of HTLV-III/LAV, the retrovirus of AIDS. Cell, 45, 637-648. (Pubitemid 16063128)
    • (1986) Cell , vol.45 , Issue.5 , pp. 637-648
    • Starcich, B.R.1    Hahn, B.H.2    Shaw, G.M.3
  • 70
    • 0022524810 scopus 로고
    • Identification of conserved and divergent domains within the envelope gene of the acquired immunodeficiency syndrome retrovirus
    • Willey, R. L., Rutledge, R. A., Dias, S., Folks, T., Theodore, T., Buckler, C. E. & Martin, M. A. (1986). Identification of conserved and divergent domains within the envelope gene of the acquired immunodeficiency syndrome retrovirus. Proc. Natl Acad. Sci. USA, 83, 5038-5042. (Pubitemid 16051313)
    • (1986) Proceedings of the National Academy of Sciences of the United States of America , vol.83 , Issue.14 , pp. 5038-5042
    • Willey, R.L.1    Rutledge, R.A.2    Dias, S.3
  • 72
    • 33846220009 scopus 로고    scopus 로고
    • High incidence of unusual cysteine variants in gp120 envelope proteins from early HIV type 1 infections from a phase 3 vaccine efficacy trial
    • DOI 10.1089/aid.2006.22.1014
    • Jobes, D. V., Daoust, M., Nguyen, V., Padua, A., Michele, S., Lock, M. D. et al. (2006). High incidence of unusual cysteine variants in gp120 envelope proteins from early HIV type 1 infections from a Phase 3 vaccine efficacy trial. AIDS Res. Hum. Retroviruses, 22, 1014-1021. (Pubitemid 46100687)
    • (2006) AIDS Research and Human Retroviruses , vol.22 , Issue.10 , pp. 1014-1021
    • Jobes, D.V.1    Daoust, M.2    Nguyen, V.3    Padua, A.4    Michele, S.5    Lock, M.D.6    Chen, A.7    Sinangil, F.8    Berman, P.W.9
  • 74
    • 44849108137 scopus 로고    scopus 로고
    • Identification of an N-linked glycosylation in the C4 region of HIV-1 envelope gp120 that is critical for recognition of neighboring CD4 T cell epitopes
    • Li, H., Chien, P. C., Tuen, M., Visciano, M. L., Cohen, S., Blais, S. et al. (2008). Identification of an N-linked glycosylation in the C4 region of HIV-1 envelope gp120 that is critical for recognition of neighboring CD4 T cell epitopes. J. Immunol. 180, 4011-4021.
    • (2008) J. Immunol. , vol.180 , pp. 4011-4021
    • Li, H.1    Chien, P.C.2    Tuen, M.3    Visciano, M.L.4    Cohen, S.5    Blais, S.6
  • 75
    • 77953028154 scopus 로고    scopus 로고
    • Involvement of envelope-glycoprotein glycans in HIV-1 biology and infection
    • Raska, M. & Novak, J. (2010). Involvement of envelope-glycoprotein glycans in HIV-1 biology and infection. Arch. Immunol. Ther. Exp. (Warsz), 58, 191-208.
    • (2010) Arch. Immunol. Ther. Exp. (Warsz) , vol.58 , pp. 191-208
    • Raska, M.1    Novak, J.2
  • 76
    • 0029929738 scopus 로고    scopus 로고
    • Functional characterization of the V1V2 region of human immunodeficiency virus type I
    • DOI 10.1006/viro.1996.0331
    • Palmer, C., Balfe, P., Fox, D., May, J. C., Frederiksson, R., Fenyö, E. M. & McKeating, J. A. (1996). Functional characterization of the V1V2 region of human immunodeficiency virus type 1. Virology, 220, 436-449. (Pubitemid 26201698)
    • (1996) Virology , vol.220 , Issue.2 , pp. 436-449
    • Palmer, C.1    Balfe, P.2    Fox, D.3    May, J.C.4    Frederiksson, R.5    Fenyo, E.-M.6    McKeating, J.A.7
  • 77
    • 0037183931 scopus 로고    scopus 로고
    • Temporal relationship between V1V2 variation, macrophage replication, and coreceptor adaptation during HIV-1 disease progression
    • Masciotra, S., Owen, S. M., Rudolph, D., Yang, C., Wang, B., Saksena, N. et al. (2002). Temporal relationship between V1V2 variation, macrophage replication, and coreceptor adaptation during HIV-1 disease progression. AIDS, 16, 1887-1898.
    • (2002) AIDS , vol.16 , pp. 1887-1898
    • Masciotra, S.1    Owen, S.M.2    Rudolph, D.3    Yang, C.4    Wang, B.5    Saksena, N.6
  • 79
    • 18144397438 scopus 로고    scopus 로고
    • Selection for human immunodeficiency virus type 1 envelope glycosylation variants with shorter V1-V2 loop sequences occurs during transmission of certain genetic subtypes and may impact viral RNA levels
    • DOI 10.1128/JVI.79.10.6528-6531.2005
    • Chohan, B., Lang, D., Sagar, M., Korber, B., Lavreys, L., Richardson, B. & Overbaugh, J. (2005). Selection for human immunodeficiency virus type 1 envelope glycosylation variants with shorter V1-V2 loop sequences occurs during transmission of certain genetic subtypes and may impact viral RNA levels. J. Virol. 79, 6528-6531. (Pubitemid 40617257)
    • (2005) Journal of Virology , vol.79 , Issue.10 , pp. 6528-6531
    • Chohan, B.1    Lang, D.2    Sagar, M.3    Korber, B.4    Lavreys, L.5    Richardson, B.6    Overbaugh, J.7
  • 80
    • 33748925430 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 V1-V2 envelope loop sequences expand and add glycosylation sites over the course of infection, and these modifications affect antibody neutralization sensitivity
    • DOI 10.1128/JVI.00141-06
    • Sagar, M., Wu, X., Lee, S. & Overbaugh, J. (2006). Human immunodeficiency virus type 1 V1-V2 envelope loop sequences expand and add glycosyl-ation sites over the course of infection, and these modifications affect antibody neutralization sensitivity. J. Virol. 80, 9586-9598. (Pubitemid 44435633)
    • (2006) Journal of Virology , vol.80 , Issue.19 , pp. 9586-9598
    • Sagar, M.1    Wu, X.2    Lee, S.3    Overbaugh, J.4
  • 81
    • 0037942744 scopus 로고    scopus 로고
    • Turnover of env variable region 1 and 2 genotypes in subjects with late-stage human immunodeficiency virus type 1 infection
    • DOI 10.1128/JVI.77.12.6811-6822.2003
    • Kitrinos, K. M., Hoffman, N. G., Nelson, J. A. E. & Swanstrom, R. (2003). Turnover of env variable region 1 and 2 genotypes in subjects with late-stage human immunodeficiency virus type 1 infection. J. Virol. 77, 6811-6822. (Pubitemid 36666875)
    • (2003) Journal of Virology , vol.77 , Issue.12 , pp. 6811-6822
    • Kitrinos, K.M.1    Hoffman, N.G.2    Nelson, J.A.E.3    Swanstrom, R.4
  • 83
    • 0023651341 scopus 로고
    • Delineation of a region of the human immunodeficiency virus type 1 gp120 glycoprotein critical for interaction with the CD4 receptor
    • Lasky, L. A., Nakamura, G., Smith, D. H., Fennie, C., Shimasaki, C., Patzer, E. et al. (1987). Delineation of a region of the human immunodeficiency virus type 1 gp120 glycoprotein critical for interaction with the CD4 receptor. Cell, 50, 975-985.
    • (1987) Cell , vol.50 , pp. 975-985
    • Lasky, L.A.1    Nakamura, G.2    Smith, D.H.3    Fennie, C.4    Shimasaki, C.5    Patzer, E.6
  • 84
    • 0023217711 scopus 로고
    • Functional regions of the envelope glycoprotein of human immunodeficiency virus type 1
    • Kowalski, M., Potz, J., Basiripour, L., Dorfman, T., Goh, W. C., Terwilliger, E. et al. (1987). Functional regions of the envelope glycoprotein of human immunodeficiency virus type 1. Science, 237, 1351-1355. (Pubitemid 17134619)
    • (1987) Science , vol.237 , Issue.4820 , pp. 1351-1355
    • Kowalski, M.1    Potz, J.2    Basiripour, L.3
  • 85
    • 0025253819 scopus 로고
    • Identification of individual human immunodeficiency virus type 1 gp120 amino acids important for CD4 receptor binding
    • Olshevsky, U., Helseth, E., Furman, C., Li, J., Haseltine, W. & Sodroski, J. (1990). Identification of individual human immunodeficiency virus type 1 gp120 amino acids important for CD4 receptor binding. J. Virol. 64, 5701-5707.
    • (1990) J. Virol. , vol.64 , pp. 5701-5707
    • Olshevsky, U.1    Helseth, E.2    Furman, C.3    Li, J.4    Haseltine, W.5    Sodroski, J.6
  • 86
    • 0026567492 scopus 로고
    • Truncated variants of gp120 bind CD4 with high affinity and suggest a minimum CD4 binding region
    • Pollard, S. R., Rosa, M. D., Rosa, J. J. & Wiley, D. C. (1992). Truncated variants of gp120 bind CD4 with high affinity and suggest a minimum CD4 binding region. EMBO J. 11, 585-591.
    • (1992) EMBO J. , vol.11 , pp. 585-591
    • Pollard, S.R.1    Rosa, M.D.2    Rosa, J.J.3    Wiley, D.C.4
  • 87
    • 0027194743 scopus 로고
    • Functional and immunologic characterization of human immunodeficiency virus type 1 envelope glycoproteins containing deletions of the major variable regions
    • Wyatt, R., Sullivan, N., Thali, M., Repke, H., Ho, D., Robinson, J. et al. (1993). Functional and immuno-logic characterization of human immunodeficiency virus type 1 envelope glycoproteins containing deletions of the major variable regions. J. Virol. 67, 4557-4565. (Pubitemid 23215934)
    • (1993) Journal of Virology , vol.67 , Issue.8 , pp. 4557-4565
    • Wyatt, R.1    Sullivan, N.2    Thali, M.3    Repke, H.4    Ho, D.5    Robinson, J.6    Posner, M.7    Sodroski, J.8
  • 88
    • 0025961011 scopus 로고
    • Identification of the principal neutralizing determinant of human immunodeficiency virus type 1 as a fusion domain
    • Freed, E. O., Myers, D. J. & Risser, R. (1991). Identification of the principal neutralizing determinant of human immunodeficiency virus type 1 as a fusion domain. J. Virol. 65, 190-194.
    • (1991) J. Virol. , vol.65 , pp. 190-194
    • Freed, E.O.1    Myers, D.J.2    Risser, R.3
  • 89
    • 0025065099 scopus 로고
    • HIV-1 tropism for mononuclear phagocytes can be determined by regions of gp120 outside the CD4-binding domain
    • O'Brien, W. A., Koyanagi, Y., Namazie, A., Zhao, J. Q., Diagne, A., Idler, K. et al. (1990). HIV-1 tropism for mononuclear phagocytes can be determined by regions of gp120 outside the CD4-binding domain. Nature, 348, 69-73.
    • (1990) Nature , vol.348 , pp. 69-73
    • O'Brien, W.A.1    Koyanagi, Y.2    Namazie, A.3    Zhao, J.Q.4    Diagne, A.5    Idler, K.6
  • 90
    • 0025783669 scopus 로고
    • Identification of the envelope V3 loop as the primary determinant of cell tropism in HIV-1
    • Hwang, S. S., Boyle, T. J., Lyerly, H. K. & Cullen, B. R. (1991). Identification of the envelope V3 loop as the primary determinant of cell tropism in HIV-1. Science, 253, 71-74. (Pubitemid 21917121)
    • (1991) Science , vol.253 , Issue.5015 , pp. 71-74
    • Hwang, S.S.1    Boyle, T.J.2    Lyerly, H.K.3    Cullen, B.R.4
  • 91
    • 0026089184 scopus 로고
    • Macrophage and T cell-line tropisms of HIV-1 are determined by specific regions of the envelope gp120 gene
    • Shioda, T., Levy, J. A. & Cheng-Mayer, C. (1991). Macrophage and T cell-line tropisms of HIV-1 are determined by specific regions of the envelope gp120 gene. Nature, 349, 167-169. (Pubitemid 21912038)
    • (1991) Nature , vol.349 , Issue.6305 , pp. 167-169
    • Shioda, T.1    Levy, J.A.2    Cheng-Mayer, C.3
  • 92
    • 0025930562 scopus 로고
    • Identification of human immunodeficiency virus envelope gene sequences influencing viral entry into CD4-positive HeLa cells, T-leukemia cells, and macrophages
    • Chesebro, B., Nishio, J., Perryman, S., Cann, A., O'Brien, W., Chen, I. S. & Wehrly, K. (1991). Identification of human immunodeficiency virus envelope gene sequences influencing viral entry into CD4-positive HeLa cells, T-leukemia cells, and macrophages. J. Virol. 65, 5782-5789.
    • (1991) J. Virol. , vol.65 , pp. 5782-5789
    • Chesebro, B.1    Nishio, J.2    Perryman, S.3    Cann, A.4    O'Brien, W.5    Chen, I.S.6    Wehrly, K.7
  • 93
    • 0026597418 scopus 로고
    • The region of the envelope gene of human immunodeficiency virus type 1 responsible for determination of cell tropism
    • Cann, A. J., Churcher, M. J., Boyd, M., O'Brien, W., Zhao, J. Q., Zack, J. & Chen, I. S. (1992). The region of the envelope gene of human immunodeficiency virus type 1 responsible for determination of cell tropism. J. Virol. 66, 305-309.
    • (1992) J. Virol. , vol.66 , pp. 305-309
    • Cann, A.J.1    Churcher, M.J.2    Boyd, M.3    O'Brien, W.4    Zhao, J.Q.5    Zack, J.6    Chen, I.S.7
  • 94
    • 0041914944 scopus 로고
    • Antibodies that inhibit fusion of human immunodeficiency virus-infected cells bind a 24-amino acid sequence of the viral envelope gp120
    • Rusche, J. R., Javaherian, K., McDanal, C., Petro, J., Lynn, D. L., Grimaila, R. et al. (1988). Antibodies that inhibit fusion of human immunodeficiency virus-infected cells bind a 24-amino acid sequence of the viral envelope, gp120. Proc. Natl Acad. Sci. USA, 85, 3198-3202.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 3198-3202
    • Rusche, J.R.1    Javaherian, K.2    McDanal, C.3    Petro, J.4    Lynn, D.L.5    Grimaila, R.6
  • 96
    • 0043080631 scopus 로고
    • Human immunodeficiency virus type 1 neutralization epi-tope with conserved architecture elicits early type-specific antibodies in experimentally infected chimpanzees
    • Goudsmit, J., Debouck, C., Meloen, R. H., Smit, L., Bakker, M., Asher, D. M. et al. (1988). Human immunodeficiency virus type 1 neutralization epi-tope with conserved architecture elicits early type-specific antibodies in experimentally infected chimpanzees. Proc. Natl Acad. Sci. USA, 85, 4478-4482.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 4478-4482
    • Goudsmit, J.1    Debouck, C.2    Meloen, R.H.3    Smit, L.4    Bakker, M.5    Asher, D.M.6
  • 97
    • 0023940408 scopus 로고
    • Characterization of a human immunodeficiency virus neutralizing monoclonal antibody and mapping of the neutralizing epitope
    • Matsushita, S., Robert-Guroff, M., Rusche, J., Koito, A., Hattori, T., Hoshino, H. et al. (1988). Characterization of a human immunodeficiency virus neutralizing monoclonal antibody and mapping of the neutralizing epitope. J. Virol. 62, 2107-2114.
    • (1988) J. Virol. , vol.62 , pp. 2107-2114
    • Matsushita, S.1    Robert-Guroff, M.2    Rusche, J.3    Koito, A.4    Hattori, T.5    Hoshino, H.6
  • 98
    • 0028148476 scopus 로고
    • A naturally occurring single basic amino acid substitution in the V3 region of the human immunodeficiency virus type 1 env protein alters the cellular host range and antigenic structure of the virus
    • Shioda, T., Oka, S., Ida, S., Nokihara, K., Toriyoshi, H., Mori, S. et al. (1994). A naturally occurring single basic amino acid substitution in the V3 region of the human immunodeficiency virus type 1 env protein alters the cellular host range and antigenic structure of the virus. J. Virol. 68, 7689-7696. (Pubitemid 24362654)
    • (1994) Journal of Virology , vol.68 , Issue.12 , pp. 7689-7696
    • Shioda, T.1    Oka, S.2    Ida, S.3    Nokihara, K.4    Toriyoshi, H.5    Mori, S.6    Takebe, Y.7    Kimura, S.8    Shimada, K.9    Nagai, Y.10
  • 99
    • 0026606727 scopus 로고
    • Phenotype-associated sequence variation in the third variable domain of the human immunodeficiency virus type 1 gp120 molecule
    • Fouchier, R. A., Groenink, M., Kootstra, N. A., Tersmette, M., Huisman, H. G., Miedema, F. & Schuitemaker, H. (1992). Phenotype-associated sequence variation in the third variable domain of the human immunodeficiency virus type 1 gp120 molecule. J. Virol. 66, 3183-3187.
    • (1992) J. Virol. , vol.66 , pp. 3183-3187
    • Fouchier, R.A.1    Groenink, M.2    Kootstra, N.A.3    Tersmette, M.4    Huisman, H.G.5    Miedema, F.6    Schuitemaker, H.7
  • 100
    • 12144287132 scopus 로고    scopus 로고
    • Phenotypic and genotypic comparisons of CCR5-and CXCR4-tropic human immunodeficiency virus type 1 biological clones isolated from subtype C-infected individuals
    • DOI 10.1128/JVI.78.6.2841-2852.2004
    • Pollakis, G., Abebe, A., Kliphuis, A., Chalaby, M. I.M., Bakker, M., Mengistu, Y. et al. (2004). Phenotypic and genotypic comparisons of CCR5-and CXCR4-tropic human immunodeficiency virus type 1 biological clones isolated from subtype C-infected individuals. J. Virol. 78, 2841-2852. (Pubitemid 38314342)
    • (2004) Journal of Virology , vol.78 , Issue.6 , pp. 2841-2852
    • Pollakis, G.1    Abebe, A.2    Kliphuis, A.3    Chalaby, M.I.M.4    Bakker, M.5    Mengistu, Y.6    Brouwer, M.7    Goudsmit, J.8    Schuitemaker, H.9    Paxton, W.A.10
  • 101
    • 0032546952 scopus 로고    scopus 로고
    • A conserved HIV gp120 glycoprotein structure involved in chemokine receptor binding
    • DOI 10.1126/science.280.5371.1949
    • Rizzuto, C. D., Wyatt, R., Hernández-Ramos, N., Sun, Y., Kwong, P. D., Hendrickson, W. A. & Sodroski, J. (1998). A conserved HIV gp120 glyco-protein structure involved in chemokine receptor binding. Science, 280, 1949-1953. (Pubitemid 28299405)
    • (1998) Science , vol.280 , Issue.5371 , pp. 1949-1953
    • Rizzuto, C.D.1    Wyatt, R.2    Hernandez-Ramos, N.3    Sun, Y.4    Kwong, P.D.5    Hendrickson, W.A.6    Sodroski, J.7
  • 102
    • 0034690683 scopus 로고    scopus 로고
    • Fine definition of a conserved CCR5-binding region on the human immunodeficiency virus type 1 glycoprotein 120
    • DOI 10.1089/088922200308747
    • Rizzuto, C. & Sodroski, J. (2000). Fine definition of a conserved CCR5-binding region on the human immunodeficiency virus type 1 glycoprotein 120. AIDS Res. Hum. Retroviruses, 16, 741-749. (Pubitemid 30327291)
    • (2000) AIDS Research and Human Retroviruses , vol.16 , Issue.8 , pp. 741-749
    • Rizzuto, C.1    Sodroski, J.2
  • 103
    • 0035000023 scopus 로고    scopus 로고
    • Mapping the determinants of the CCR5 amino-terminal sulfopeptide interaction with soluble human immunodeficiency virus type 1 gp120-CD4 complexes
    • DOI 10.1128/JVI.75.12.5541-5549.2001
    • Cormier, E. G., Tran, D. N., Yukhayeva, L., Olson, W. C. & Dragic, T. (2001). Mapping the determinants of the CCR5 amino-terminal sulfopeptide interaction with soluble human immunodeficiency virus type 1 gp120-CD4 complexes. J. Virol. 75, 5541-5549. (Pubitemid 32488147)
    • (2001) Journal of Virology , vol.75 , Issue.12 , pp. 5541-5549
    • Cormier, E.G.1    Tran, D.N.H.2    Yukhayeva, L.3    Olson, W.C.4    Dragic, T.5
  • 104
    • 0036333648 scopus 로고    scopus 로고
    • The crown and stem of the V3 loop play distinct roles in human immunodeficiency virus type 1 envelope glycoprotein interactions with the CCR5 coreceptor
    • DOI 10.1128/JVI.76.17.8953-8957.2002
    • Cormier, E. G. & Dragic, T. (2002). The crown and stem of the V3 loop play distinct roles in human immunodeficiency virus type 1 envelope glycopro-tein interactions with the CCR5 coreceptor. J. Virol. 76, 8953-8957. (Pubitemid 34864089)
    • (2002) Journal of Virology , vol.76 , Issue.17 , pp. 8953-8957
    • Cormier, E.G.1    Dragic, T.2
  • 106
    • 33847237614 scopus 로고    scopus 로고
    • Reduced maximal inhibition in phenotypic susceptibility assays indicates that viral strains resistant to the CCR5 antagonist maraviroc utilize inhibitor-bound receptor for entry
    • Westby, M., Smith-Burchnell, C., Mori, J., Lewis, M., Mosley, M., Stockdale, M. et al. (2007). Reduced maximal inhibition in phenotypic susceptibility assays indicates that viral strains resistant to the CCR5 antagonist maraviroc utilize inhibitor-bound receptor for entry. J. Virol. 81, 2359-2371.
    • (2007) J. Virol. , vol.81 , pp. 2359-2371
    • Westby, M.1    Smith-Burchnell, C.2    Mori, J.3    Lewis, M.4    Mosley, M.5    Stockdale, M.6
  • 107
    • 34047271098 scopus 로고    scopus 로고
    • HIV-1 clones resistant to a small molecule CCR5 inhibitor use the inhibitor-bound form of CCR5 for entry
    • DOI 10.1016/j.virol.2006.11.004, PII S0042682206008245
    • Pugach, P., Marozsan, A. J., Ketas, T. J., Landes, E. L., Moore, J. P. & Kuhmann, S. E. (2007). HIV-1 clones resistant to a small molecule CCR5 inhibitor use the inhibitor-bound form of CCR5 for entry. Virology, 361, 212-228. (Pubitemid 46551222)
    • (2007) Virology , vol.361 , Issue.1 , pp. 212-228
    • Pugach, P.1    Marozsan, A.J.2    Ketas, T.J.3    Landes, E.L.4    Moore, J.P.5    Kuhmann, S.E.6
  • 108
    • 0032543307 scopus 로고    scopus 로고
    • Structure of an HIV gp 120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
    • DOI 10.1038/31405
    • Kwong, P. D., Wyatt, R., Robinson, J., Sweet, R. W., Sodroski, J. & Hendrickson, W. A. (1998). Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature, 393, 648-659. (Pubitemid 28289647)
    • (1998) Nature , vol.393 , Issue.6686 , pp. 648-659
    • Kwong, P.D.1    Wyatt, R.2    Robinson, J.3    Sweet, R.W.4    Sodroski, J.5    Hendrickson, W.A.6
  • 109
    • 13844302894 scopus 로고    scopus 로고
    • Structure of an unliganded simian immunodeficiency virus gp120 core
    • DOI 10.1038/nature03327
    • Chen, B., Vogan, E. M., Gong, H., Skehel, J. J., Wiley, D. C. & Harrison, S. C. (2005). Structure of an unliganded simian immunodeficiency virus gp120 core. Nature, 433, 834-841. (Pubitemid 40314887)
    • (2005) Nature , vol.433 , Issue.7028 , pp. 834-841
    • Chen, B.1    Vogan, E.M.2    Gong, H.3    Skehel, J.J.4    Wiley, D.C.5    Harrison, S.C.6
  • 113
    • 70450182950 scopus 로고    scopus 로고
    • Structural basis of immune evasion at the site of CD4 attachment on HIV-1 gp120
    • Chen, L., Kwon, Y. D., Zhou, T., Wu, X., O'Dell, S., Cavacini, L. et al. (2009). Structural basis of immune evasion at the site of CD4 attachment on HIV-1 gp120. Science, 326, 1123-1127.
    • (2009) Science , vol.326 , pp. 1123-1127
    • Chen, L.1    Kwon, Y.D.2    Zhou, T.3    Wu, X.4    O'Dell, S.5    Cavacini, L.6
  • 114
    • 75749133275 scopus 로고    scopus 로고
    • Structure of HIV-1 gp120 with gp41-interactive region reveals layered envelope architecture and basis of conformational mobility
    • Pancera, M., Majeed, S., Ban, Y.-E. A., Chen, L., Huang, C.-c., Kong, L. et al. (2010). Structure of HIV-1 gp120 with gp41-interactive region reveals layered envelope architecture and basis of conformational mobility. Proc. Natl Acad. Sci. USA, 107, 1166-1171.
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 1166-1171
    • Pancera, M.1    Majeed, S.2    Ban, Y.-E.A.3    Chen, L.4    Huang, C.-C.5    Kong, L.6
  • 116
    • 0024397095 scopus 로고
    • Single amino-acid changes in HIV envelope affect viral tropism and receptor binding
    • DOI 10.1038/340571a0
    • Cordonnier, A., Montagnier, L. & Emerman, M. (1989). Single amino-acid changes in HIV envelope affect viral tropism and receptor binding. Nature, 340, 571-574. (Pubitemid 19201701)
    • (1989) Nature , vol.340 , Issue.6234 , pp. 571-574
    • Cordonnier, A.1    Montagnier, L.2    Emerman, M.3
  • 118
    • 0025297179 scopus 로고
    • Characterization of the fusion domain of the human immunodeficiency virus type 1 envelope glycoprotein gp41
    • Freed, E. O., Myers, D. J. & Risser, R. (1990). Characterization of the fusion domain of the human immunodeficiency virus type 1 envelope glycoprotein gp41. Proc. Natl Acad. Sci. USA, 87, 4650-4654.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 4650-4654
    • Freed, E.O.1    Myers, D.J.2    Risser, R.3
  • 119
    • 0026544416 scopus 로고
    • A mutation in the human immunodeficiency virus type 1 transmembrane glycoprotein gp41 dominantly interferes with fusion and infectivity
    • Freed, E. O., Delwart, E. L., Buchschacher, G. L. & Panganiban, A. T. (1992). A mutation in the human immunodeficiency virus type 1 transmembrane glycoprotein gp41 dominantly interferes with fusion and infectivity. Proc. Natl Acad. Sci. USA, 89, 70-74.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 70-74
    • Freed, E.O.1    Delwart, E.L.2    Buchschacher, G.L.3    Panganiban, A.T.4
  • 120
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan, D. C., Fass, D., Berger, J. M. & Kim, P. S. (1997). Core structure of gp41 from the HIV envelope glycoprotein. Cell, 89, 263-273. (Pubitemid 27199898)
    • (1997) Cell , vol.89 , Issue.2 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 121
    • 0026652457 scopus 로고
    • Mutations in the leucine zipper of the human immunodeficiency virus type 1 transmembrane glycoprotein affect fusion and infectivity
    • Dubay, J. W., Roberts, S. J., Brody, B. & Hunter, E. (1992). Mutations in the leucine zipper of the human immunodeficiency virus type 1 transmembrane glycoprotein affect fusion and infectivity. J. Virol. 66, 4748-4756.
    • (1992) J. Virol. , vol.66 , pp. 4748-4756
    • Dubay, J.W.1    Roberts, S.J.2    Brody, B.3    Hunter, E.4
  • 122
    • 0028834461 scopus 로고
    • A trimeric structural domain of the HIV-1 transmembrane glycoprotein
    • Lu, M., Blacklow, S. C. & Kim, P. S. (1995). A trimeric structural domain of the HIV-1 transmembrane glycoprotein. Nat. Struct. Biol. 2, 1075-1082.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 1075-1082
    • Lu, M.1    Blacklow, S.C.2    Kim, P.S.3
  • 124
    • 0030962291 scopus 로고    scopus 로고
    • Atomic structure of the ectodomain from HIV-1 gp41
    • DOI 10.1038/387426a0
    • Weissenhorn, W., Dessen, A., Harrison, S. C., Skehel, J. J. & Wiley, D. C. (1997). Atomic structure of the ectodomain from HIV-1 gp41. Nature, 387, 426-430. (Pubitemid 27227210)
    • (1997) Nature , vol.387 , Issue.6631 , pp. 426-430
    • Weissenhorn, W.1    Dessen, A.2    Harrison, S.C.3    Skehel, J.J.4    Wiley, D.C.5
  • 125
    • 0343365487 scopus 로고    scopus 로고
    • Role of the membrane-proximal domain in the initial stages of human immunodeficiency virus type 1 envelope glycoprotein-mediated membrane fusion
    • Muñoz-Barroso, I., Salzwedel, K., Hunter, E. & Blumenthal, R. (1999). Role of the membrane-proximal domain in the initial stages of human immunodeficiency virus type 1 envelope glycopro-tein-mediated membrane fusion. J. Virol. 73, 6089-6092. (Pubitemid 29274898)
    • (1999) Journal of Virology , vol.73 , Issue.7 , pp. 6089-6092
    • Munoz-Barroso, I.1    Salzwedel, K.2    Hunter, E.3    Blumenthal, R.4
  • 126
    • 0032980413 scopus 로고    scopus 로고
    • A conserved tryptophan-rich motif in the membrane-proximal region of the human immunodeficiency virus type 1 gp41 ectodomain is important for Env- mediated fusion and virus infectivity
    • Salzwedel, K., West, J. T. & Hunter, E. (1999). A conserved tryptophan-rich motif in the membrane-proximal region of the human immunodeficiency virus type 1 gp41 ectodomain is important for Env-mediated fusion and virus infectivity. J. Virol. 73, 2469-2480. (Pubitemid 29098154)
    • (1999) Journal of Virology , vol.73 , Issue.3 , pp. 2469-2480
    • Salzwedel, K.1    West, J.T.2    Hunter, E.3
  • 127
    • 0025054302 scopus 로고
    • Orientation into the lipid bilayer of an asymmetric amphipathic helical peptide located at the N-terminus of viral fusion proteins
    • DOI 10.1016/0005-2736(90)90163-I
    • Brasseur, R., Vandenbranden, M., Cornet, B., Burny, A. & Ruysschaert, J. M. (1990). Orientation into the lipid bilayer of an asymmetric amphipathic helical peptide located at the N-terminus of viral fusion proteins. Biochim. Biophys. Acta, 1029, 267-273. (Pubitemid 20372063)
    • (1990) Biochimica et Biophysica Acta - Biomembranes , vol.1029 , Issue.2 , pp. 267-273
    • Brasseur, R.1    Vandenbranden, M.2    Cornet, B.3    Burny, A.4    Ruysschaert, J.-M.5
  • 128
    • 45849108331 scopus 로고    scopus 로고
    • Structures and mechanisms of viral membrane fusion proteins: Multiple variations on a common theme
    • DOI 10.1080/10409230802058320, PII 794225034
    • White, J. M., Delos, S. E., Brecher, M. & Schornberg, K. (2008). Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme. Crit. Rev. Biochem. Mol. Biol. 43, 189-219. (Pubitemid 351883153)
    • (2008) Critical Reviews in Biochemistry and Molecular Biology , vol.43 , Issue.3 , pp. 189-219
    • White, J.M.1    Delos, S.E.2    Brecher, M.3    Schornberg, K.4
  • 129
    • 58849092285 scopus 로고    scopus 로고
    • Membrane fusion: Grappling with SNARE and SM proteins
    • Südhof, T. C. & Rothman, J. E. (2009). Membrane fusion: grappling with SNARE and SM proteins. Science, 323, 474-477.
    • (2009) Science , vol.323 , pp. 474-477
    • Südhof, T.C.1    Rothman, J.E.2
  • 131
    • 0031959601 scopus 로고    scopus 로고
    • Capture of an early fusion-active conformation of HIV-1 gp41
    • DOI 10.1038/nsb0498-276
    • Furuta, R. A., Wild, C. T., Weng, Y. & Weiss, C. D. (1998). Capture of an early fusion-active conformation of HIV-1 gp41. Nat. Struct. Biol. 5, 276-279. (Pubitemid 28164878)
    • (1998) Nature Structural Biology , vol.5 , Issue.4 , pp. 276-279
    • Furuta, R.A.1    Wild, C.T.2    Weng, Y.3    Weiss, C.D.4
  • 134
    • 0028813111 scopus 로고
    • Determinants of human immunodeficiency virus type 1 envelope glycoprotein oligomeric structure
    • Poumbourios, P., el Ahmar, W., McPhee, D. A. & Kemp, B. E. (1995). Determinants of human immunodeficiency virus type 1 envelope glycoprotein oligomeric structure. J. Virol. 69, 1209-1218.
    • (1995) J. Virol. , vol.69 , pp. 1209-1218
    • Poumbourios, P.1    El Ahmar, W.2    McPhee, D.A.3    Kemp, B.E.4
  • 135
    • 0027499917 scopus 로고
    • Effects of amino acid changes in the extracellular domain of the human immunodeficiency virus type 1 gp41 envelope glycoprotein
    • Cao, J., Bergeron, L., Helseth, E., Thali, M., Repke, H. & Sodroski, J. (1993). Effects of amino acid changes in the extracellular domain of the human immunodeficiency virus type 1 gp41 envelope glycoprotein. J. Virol. 67, 2747-2755. (Pubitemid 23118873)
    • (1993) Journal of Virology , vol.67 , Issue.5 , pp. 2747-2755
    • Cao, J.1    Bergeron, L.2    Helseth, E.3    Thali, M.4    Repke, H.5    Sodroski, J.6
  • 137
    • 43949136434 scopus 로고    scopus 로고
    • Role of the membrane-spanning domain of human immunodeficiency virus type 1 envelope glycoprotein in cell-cell fusion and virus infection
    • DOI 10.1128/JVI.02666-07
    • Shang, L., Yue, L. & Hunter, E. (2008). Role of the membrane-spanning domain of human immunodeficiency virus type 1 envelope glycoprotein in cell-cell fusion and virus infection. J. Virol. 82, 5417-5428. (Pubitemid 351705249)
    • (2008) Journal of Virology , vol.82 , Issue.11 , pp. 5417-5428
    • Shang, L.1    Yue, L.2    Hunter, E.3
  • 138
    • 77954534917 scopus 로고    scopus 로고
    • Residues in the membrane-spanning domain core modulate conformation and fusogenicity of the HIV-1 envelope glycoprotein
    • Shang, L. & Hunter, E. (2010). Residues in the membrane-spanning domain core modulate conformation and fusogenicity of the HIV-1 envelope glycoprotein. Virology, 404, 158-167.
    • (2010) Virology , vol.404 , pp. 158-167
    • Shang, L.1    Hunter, E.2
  • 139
    • 77952000064 scopus 로고    scopus 로고
    • Conformational changes of the HIV-1 envelope protein during membrane fusion are inhibited by the replacement of its membrane-spanning domain
    • Kondo, N., Miyauchi, K., Meng, F., Iwamoto, A. & Matsuda, Z. (2010). Conformational changes of the HIV-1 envelope protein during membrane fusion are inhibited by the replacement of its membrane-spanning domain. J. Biol. Chem. 285, 14681-14688.
    • (2010) J. Biol. Chem. , vol.285 , pp. 14681-14688
    • Kondo, N.1    Miyauchi, K.2    Meng, F.3    Iwamoto, A.4    Matsuda, Z.5
  • 142
    • 77649111767 scopus 로고    scopus 로고
    • Effect of mutations in the human immunodeficiency virus type 1 protease on cleavage of the gp41 cytoplasmic tail
    • Waheed, A. A., Ablan, S. D., Sowder, R. C., Roser, J. D., Schaffner, C. P., Chertova, E. & Freed, E. O. (2010). Effect of mutations in the human immunodeficiency virus type 1 protease on cleavage of the gp41 cytoplasmic tail. J. Virol. 84, 3121-3126.
    • (2010) J. Virol. , vol.84 , pp. 3121-3126
    • Waheed, A.A.1    Ablan, S.D.2    Sowder, R.C.3    Roser, J.D.4    Schaffner, C.P.5    Chertova, E.6    Freed, E.O.7
  • 143
    • 78650164019 scopus 로고    scopus 로고
    • Topology of the C-terminal tail of HIV-1 gp41: Differential exposure of the Kennedy epitope on cell and viral membranes
    • Steckbeck, J. D., Sun, C., Sturgeon, T. J. & Montelaro, R. C. (2010). Topology of the C-terminal tail of HIV-1 gp41: differential exposure of the Kennedy epitope on cell and viral membranes. PLoS ONE, 5, e15261.
    • (2010) PLoS ONE , vol.5
    • Steckbeck, J.D.1    Sun, C.2    Sturgeon, T.J.3    Montelaro, R.C.4
  • 144
    • 0022674568 scopus 로고
    • Antiserum to a synthetic peptide recognizes the HTLV-III envelope glycoprotein
    • Kennedy, R. C., Henkel, R. D., Pauletti, D., Allan, J. S., Lee, T. H., Essex, M. & Dreesman, G. R. (1986). Antiserum to a synthetic peptide recognizes the HTLV-III envelope glycoprotein. Science, 231, 1556-1559. (Pubitemid 16050724)
    • (1986) Science , vol.231 , Issue.4745 , pp. 1556-1559
    • Kennedy, R.C.1    Henkel, R.D.2    Pauletti, D.3
  • 146
    • 0037370395 scopus 로고    scopus 로고
    • A region of the C-terminal tail of the gp41 envelope glycoprotein of human immunodeficiency virus type 1 contains a neutralizing epitope: Evidence for its exposure on the surface of the virion
    • DOI 10.1099/vir.0.18630-0
    • Cleveland, S. M., McLain, L., Cheung, L., Jones, T. D., Hollier, M. & Dimmock, N. J. (2003). A region of the C-terminal tail of the gp41 envelope glycoprotein of human immunodeficiency virus type 1 contains a neutralizing epitope: evidence for its exposure on the surface of the virion. J. Gen. Virol. 84, 591-602. (Pubitemid 36267132)
    • (2003) Journal of General Virology , vol.84 , Issue.3 , pp. 591-602
    • Cleveland, S.M.1    McLain, L.2    Cheung, L.3    Jones, T.D.4    Hollier, M.5    Dimmock, N.J.6
  • 147
    • 20444419385 scopus 로고    scopus 로고
    • The C-terminal tail of the gp41 transmembrane envelope glycoprotein of HIV-1 clades A, B, C, and D may exist in two conformations: An analysis of sequence, structure, and function
    • DOI 10.1016/j.virol.2005.04.015, PII S0042682205002205
    • Hollier, M. J. & Dimmock, N. J. (2005). The C-terminal tail of the gp41 transmembrane envelope glycopro-tein of HIV-1 clades A, B, C, and D may exist in two conformations: an analysis of sequence, structure, and function. Virology, 337, 284-296. (Pubitemid 40798996)
    • (2005) Virology , vol.337 , Issue.2 , pp. 284-296
    • Hollier, M.J.1    Dimmock, N.J.2
  • 148
    • 47749086305 scopus 로고    scopus 로고
    • Surface exposure of the HIV-1 env cytoplasmic tail, LLP2 domain during the membrane fusion process: Interaction with gp41 fusion core
    • Lu, L., Zhu, Y., Huang, J., Chen, X., Yang, H., Jiang, S. & Chen, Y.-H. (2008). Surface exposure of the HIV-1 env cytoplasmic tail LLP2 domain during the membrane fusion process: interaction with gp41 fusion core. J. Biol. Chem. 283, 16723-16731.
    • (2008) J. Biol. Chem. , vol.283 , pp. 16723-16731
    • Lu, L.1    Zhu, Y.2    Huang, J.3    Chen, X.4    Yang, H.5    Jiang, S.6    Chen, Y.-H.7
  • 149
    • 0022864330 scopus 로고
    • Lentivirus genomic organization: The complete nucleotide sequence of the env gene region of equine infectious anemia virus
    • DOI 10.1016/0042-6822(86)90195-9
    • Rushlow, K., Olsen, K., Stiegler, G., Payne, S. L., Montelaro, R. C. & Issel, C. J. (1986). Lentivirus genomic organization: the complete nucleotide sequence of the env gene region of equine infectious anemia virus. Virology, 155, 309-321. (Pubitemid 17226238)
    • (1986) Virology , vol.155 , Issue.2 , pp. 309-321
    • Rushlow, K.1    Olsen, K.2    Stiegler, G.3
  • 150
    • 0025282289 scopus 로고
    • Synthesis and processing of the transmembrane envelope protein of equine infectious anemia virus
    • Rice, N. R., Henderson, L. E., Sowder, R. C., Copeland, T. D., Oroszlan, S. & Edwards, J. F. (1990). Synthesis and processing of the transmem-brane envelope protein of equine infectious anemia virus. J. Virol. 64, 3770-3778. (Pubitemid 20227201)
    • (1990) Journal of Virology , vol.64 , Issue.8 , pp. 3770-3778
    • Rice, N.R.1    Henderson, L.E.2    Sowder, R.C.3    Copeland, T.D.4    Oroszlan, S.5    Edward, J.F.6
  • 151
    • 0034044061 scopus 로고    scopus 로고
    • The intracytoplasmic domain of the Env transmembrane protein is a locus for attenuation of simian immunodeficiency virus SIVmac in rhesus macaques
    • DOI 10.1128/JVI.74.13.5836-5844.2000
    • Shacklett, B. L., Weber, C. J., Shaw, K. E., Keddie, E. M., Gardner, M. B., Sonigo, P. & Luciw, P. A. (2000). The intracytoplasmic domain of the Env transmembrane protein is a locus for attenuation of simian immunodeficiency virus SIVmac in rhesus macaques. J. Virol. 74, 5836-5844. (Pubitemid 30412951)
    • (2000) Journal of Virology , vol.74 , Issue.13 , pp. 5836-5844
    • Shacklett, B.L.1    Weber, C.J.2    Shaw, K.E.S.3    Keddie, E.M.4    Gardner, M.B.5    Sonigo, P.6    Luciw, P.A.7
  • 153
    • 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, 167-177.
    • (1992) Virology , vol.189 , pp. 167-177
    • Wilk, T.1    Pfeiffer, T.2    Bosch, V.3
  • 154
    • 0026755725 scopus 로고
    • Effects of deletions in the cytoplasmic domain on biological functions of human immunodeficiency virus type 1 envelope glycoproteins
    • Gabuzda, D. H., Lever, A., Terwilliger, E. & Sodroski, J. (1992). Effects of deletions in the cytoplasmic domain on biological functions 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
  • 155
    • 0027473610 scopus 로고
    • Mutations in the cytoplasmic domain of human immunodeficiency virus type 1 transmembrane protein impair the incorporation of Env proteins into mature virions
    • Yu, X., Yuan, X., McLane, M. F., Lee, T. H. & Essex, M. (1993). Mutations in the cytoplasmic domain of human immunodeficiency virus type 1 transmem-brane protein impair the incorporation of Env proteins into mature virions. J. Virol. 67, 213-221. (Pubitemid 23002981)
    • (1993) Journal of Virology , vol.67 , Issue.1 , pp. 213-221
    • Yu, X.1    Yuan, X.2    McLane, M.F.3    Lee, T.-H.4    Essex, M.5
  • 156
    • 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 adapter
    • DOI 10.1128/JVI.75.6.2982-2992.2001
    • Wyss, S., Berlioz-Torrent, C., Boge, M., Blot, G., Höning, 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 [correction of adapter]. J. Virol. 75, 2982-2992. (Pubitemid 32185063)
    • (2001) Journal of Virology , vol.75 , Issue.6 , 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
  • 157
    • 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, 1984-1989.
    • (1995) J. Virol. , vol.69 , pp. 1984-1989
    • Freed, E.O.1    Martin, M.A.2
  • 158
    • 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, 341-351. (Pubitemid 126508804)
    • (1996) Journal of Virology , vol.70 , Issue.1 , pp. 341-351
    • Freed, E.O.1    Martin, M.A.2
  • 159
    • 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
    • DOI 10.1073/pnas.97.1.343
    • 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, 343-348. (Pubitemid 30055833)
    • (2000) Proceedings of the National Academy of Sciences of the United States of America , vol.97 , Issue.1 , pp. 343-348
    • Murakami, T.1    Freed, E.O.2
  • 160
    • 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
    • DOI 10.1128/JVI.74.8.3548-3554.2000
    • Murakami, T. & Freed, E. O. (2000). Genetic evidence for an interaction between human immunodeficiency virus type 1 matrix and alpha-helix 2 of the gp41 cytoplasmic tail. J. Virol. 74, 3548-3554. (Pubitemid 30180297)
    • (2000) Journal of Virology , vol.74 , Issue.8 , pp. 3548-3554
    • Murakami, T.1    Freed, E.O.2
  • 161
    • 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
    • DOI 10.1128/JVI.77.6.3634-3646.2003
    • Kalia, V., Sarkar, S., Gupta, P. & Montelaro, R. C. (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. (Pubitemid 36297283)
    • (2003) Journal of Virology , vol.77 , Issue.6 , pp. 3634-3646
    • Kalia, V.1    Sarkar, S.2    Gupta, P.3    Montelaro, R.C.4
  • 162
    • 33645037042 scopus 로고    scopus 로고
    • Mutations at the C-terminus of the simian immunodeficiency virus envelope glycoprotein affect gp120-gp41 stability on virions
    • Affranchino, J. L. & González, S. A. (2006). Mutations at the C-terminus of the simian immunodeficiency virus envelope glycoprotein affect gp120-gp41 stability on virions. Virology, 347, 217-225.
    • (2006) Virology , vol.347 , pp. 217-225
    • Affranchino, J.L.1    González, S.A.2
  • 163
    • 0028054825 scopus 로고
    • Truncation of the cytoplasmic domain of the simian immunodeficiency virus envelope glycoprotein alters the conformation of the external domain
    • Spies, C. P., Ritter, G. D., Mulligan, M. J. & Compans, R. W. (1994). Truncation of the cytoplasmic domain of the simian immunodeficiency virus envelope glycoprotein alters the conformation of the external domain. J. Virol. 68, 585-591. (Pubitemid 24022156)
    • (1994) Journal of Virology , vol.68 , Issue.2 , pp. 585-591
    • Spies, C.P.1    Ritter Jr., G.D.2    Mulligan, M.J.3    Compans, R.W.4
  • 164
    • 0036187805 scopus 로고    scopus 로고
    • Truncation of the cytoplasmic domain induces exposure of conserved regions in the ectodomain of human immunodeficiency virus type 1 Envelope protein
    • DOI 10.1128/JVI.76.6.2683-2691.2002
    • Edwards, T. G., Wyss, S., Reeves, J. D., Zolla-Pazner, S., Hoxie, J. A., Doms, R. W. & Baribaud, F. (2002). Truncation of the cytoplasmic domain induces exposure of conserved regions in the ectodomain of human immunodeficiency virus type 1 envelope protein. J. Virol. 76, 2683-2691. (Pubitemid 34184854)
    • (2002) Journal of Virology , vol.76 , Issue.6 , pp. 2683-2691
    • Edwards, T.G.1    Wyss, S.2    Reeves, J.D.3    Zolla-Pazner, S.4    Hoxie, J.A.5    Doms, R.W.6    Baribaud, F.7
  • 165
    • 13444291135 scopus 로고    scopus 로고
    • Antibody neutralization escape mediated by point mutations in the intracytoplasmic tail of human immunodeficiency virus type 1 gp41
    • DOI 10.1128/JVI.79.4.2097-2107.2005
    • Kalia, V., Sarkar, S., Gupta, P. & Montelaro, R. C. (2005). Antibody neutralization escape mediated by point mutations in the intracytoplasmic tail of human immunodeficiency virus type 1 gp41. J. Virol. 79, 2097-2107. (Pubitemid 40204567)
    • (2005) Journal of Virology , vol.79 , Issue.4 , pp. 2097-2107
    • Kalia, V.1    Sarkar, S.2    Gupta, P.3    Montelaro, R.C.4
  • 166
    • 12344309918 scopus 로고    scopus 로고
    • Multiple domains of the SIV Env protein determine virus replication efficiency and neutralization sensitivity
    • DOI 10.1016/j.virol.2004.10.044, PII S004268220400741X
    • Vzorov, A. N., Gernert, K. M. & Compans, R. W. (2005). Multiple domains of the SIV Env protein determine virus replication efficiency and neutralization sensitivity. Virology, 332, 89-101. (Pubitemid 40127232)
    • (2005) Virology , vol.332 , Issue.1 , pp. 89-101
    • Vzorov, A.N.1    Gernert, K.M.2    Compans, R.W.3
  • 167
    • 0035035296 scopus 로고    scopus 로고
    • Relationships between CD4 independence, neutralization sensitivity, and exposure of a CD4-induced epitope in a human immunodeficiency virus type 1 envelope protein
    • DOI 10.1128/JVI.75.11.5230-5239.2001
    • Edwards, T. G., Hoffman, T. L., Baribaud, F., Wyss, S., LaBranche, C. C., Romano, J. et al. (2001). Relationships between CD4 independence, neutralization sensitivity, and exposure of a CD4-induced epitope in a human immunodeficiency virus type 1 envelope protein. J. Virol. 75, 5230-5239. (Pubitemid 32448546)
    • (2001) Journal of Virology , vol.75 , Issue.11 , pp. 5230-5239
    • Edwards, T.G.1    Hoffman, T.L.2    Baribaud, F.3    Wyss, S.4    Labranche, C.C.5    Romano, J.6    Adkinson, J.7    Sharron, M.8    Hoxie, J.A.9    Doms, R.W.10
  • 168
    • 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, 473-488.
    • (1995) J. Immunol. , vol.155 , pp. 473-488
    • Rowell, J.F.1    Stanhope, P.E.2    Siliciano, R.F.3
  • 169
    • 0031585539 scopus 로고    scopus 로고
    • Interaction of endocytic signals from the HIV-1 envelope glycoprotein complex with members of the adaptor medium chain family
    • DOI 10.1006/viro.1997.8839
    • 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 glyco-protein complex with members of the adaptor medium chain family. Virology, 238, 305-315. (Pubitemid 28218148)
    • (1997) Virology , vol.238 , Issue.2 , pp. 305-315
    • Ohno, H.1    Aguilar, R.C.2    Fournier, M.-C.3    Hennecke, S.4    Cosson, P.5    Bonifacino, J.S.6
  • 170
    • 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
    • DOI 10.1074/jbc.273.25.15773
    • 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, 15773-15778. (Pubitemid 28298198)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.25 , pp. 15773-15778
    • Boge, M.1    Wyss, S.2    Bonifacino, J.S.3    Thali, M.4
  • 171
    • 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. et al. (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. (Pubitemid 29036790)
    • (1999) Journal of Virology , vol.73 , Issue.2 , 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
  • 172
    • 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
    • DOI 10.1093/emboj/16.4.695
    • 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. (Pubitemid 27089517)
    • (1997) EMBO Journal , vol.16 , Issue.4 , pp. 695-705
    • Lodge, R.1    Lalonde, J.-P.2    Lemay, G.3    Cohen, E.A.4
  • 173
    • 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, 5010-5017. (Pubitemid 29246762)
    • (1999) Journal of Virology , vol.73 , Issue.6 , pp. 5010-5017
    • Deschambeault, J.1    Lalonde, J.-P.2    Cervantes-Acosta, G.3    Lodge, R.4    Cohen, E.A.5    Lemay, G.6
  • 174
    • 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
    • DOI 10.1128/JVI.78.3.1069-1079.2004
    • Day, J. R., Münk, C. & Guatelli, J. C. (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. (Pubitemid 38095817)
    • (2004) Journal of Virology , vol.78 , Issue.3 , pp. 1069-1079
    • Day, J.R.1    Munk, C.2    Guatelli, J.C.3
  • 175
    • 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
    • DOI 10.1128/JVI.76.7.3338-3349.2002
    • West, J. T., Weldon, S. K., Wyss, S., Lin, X., Yu, Q., Thali, M. & Hunter, E. (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. (Pubitemid 34224536)
    • (2002) Journal of Virology , vol.76 , Issue.7 , 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
  • 176
    • 0034749280 scopus 로고    scopus 로고
    • In vivo attenuation of simian immunodeficiency virus by disruption of a tyrosine-dependent sorting signal in the envelope glycoprotein cytoplasmic tail
    • Fultz, P. N., Vance, P. J., Endres, M. J., Tao, B., Dvorin, J. D., Davis, I. C. et al. (2001). In vivo attenuation of simian immunodeficiency virus by disruption of a tyrosine-dependent sorting signal in the envelope glycoprotein cytoplasmic tail. J. Virol. 75, 278-291.
    • (2001) J. Virol. , vol.75 , pp. 278-291
    • Fultz, P.N.1    Vance, P.J.2    Endres, M.J.3    Tao, B.4    Dvorin, J.D.5    Davis, I.C.6
  • 177
    • 33846821654 scopus 로고    scopus 로고
    • A conserved dileucine motif mediates clathrin and AP-2-dependent endocytosis of the HIV-1 envelope protein
    • DOI 10.1091/mbc.E06-06-0535
    • 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, 414-425. (Pubitemid 46213212)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.2 , pp. 414-425
    • Byland, R.1    Vance, P.J.2    Hoxie, J.A.3    Marsh, M.4
  • 178
    • 0025895768 scopus 로고
    • A structural correlation between lentivirus transmembrane proteins and natural cytolytic peptides
    • Miller, M. A., Garry, R. F., Jaynes, J. M. & Montelaro, R. C. (1991). A structural correlation between lentivirus transmembrane proteins and natural cytolytic peptides. AIDS Res. Hum. Retroviruses, 7, 511-519.
    • (1991) AIDS Res. Hum. Retroviruses , vol.7 , pp. 511-519
    • Miller, M.A.1    Garry, R.F.2    Jaynes, J.M.3    Montelaro, R.C.4
  • 179
    • 0027210033 scopus 로고
    • Alterations in cell membrane permeability by the lentivirus lytic peptide (LLP-1) of HIV-1 transmem-brane protein
    • Miller, M. A., Cloyd, M. W., Liebmann, J., Rinaldo, C. R., Islam, K. R., Wang, S. Z. et al. (1993). Alterations in cell membrane permeability by the lentivirus lytic peptide (LLP-1) of HIV-1 transmem-brane protein. Virology, 196, 89-100.
    • (1993) Virology , vol.196 , pp. 89-100
    • Miller, M.A.1    Cloyd, M.W.2    Liebmann, J.3    Rinaldo, C.R.4    Islam, K.R.5    Wang, S.Z.6
  • 180
    • 0025055304 scopus 로고
    • The most highly amphiphilic α-helices include two amino acid segments in human immunodeficiency virus glycoprotein 41
    • Eisenberg, D. & Wesson, M. (1990). The most highly amphiphilic alpha-helices include two amino acid segments in human immunodeficiency virus glyco-protein 41. Biopolymers, 29, 171-177. (Pubitemid 20055813)
    • (1990) Biopolymers , vol.29 , Issue.1 , pp. 171-177
    • Eisenberg, D.1    Wesson, M.2
  • 181
    • 0024515174 scopus 로고
    • Theoretically determined three-dimensional structures for amphipatic segments of the HIV-1 gp41 envelope protein
    • Venable, R. M., Pastor, R. W., Brooks, B. R. & Carson, F. W. (1989). Theoretically determined three-dimensional structures for amphipathic segments of the HIV-1 gp41 envelope protein. AIDS Res. Hum. Retroviruses, 5, 7-22. (Pubitemid 19079107)
    • (1989) AIDS Research and Human Retroviruses , vol.5 , Issue.1 , pp. 7-22
    • Venable, R.M.1    Pastor, R.W.2    Brooks, B.R.3    Carson, F.W.4
  • 182
    • 0037013258 scopus 로고    scopus 로고
    • Effect of point mutations in the N terminus of the lentivirus lytic peptide-1 sequence of human immunodeficiency virus type 1 transmembrane protein gp41 on Env stability
    • Lee, S. F., Ko, C. Y., Wang, C. T. & Chen, S. S.L. (2002). Effect of point mutations in the N terminus of the lentivirus lytic peptide-1 sequence of human immunodeficiency virus type 1 transmembrane protein gp41 on Env stability. J. Biol. Chem. 277, 15363-15375.
    • (2002) J. Biol. Chem. , vol.277 , pp. 15363-15375
    • Lee, S.F.1    Ko, C.Y.2    Wang, C.T.3    Chen, S.S.L.4
  • 183
    • 0034717055 scopus 로고    scopus 로고
    • Multimerization potential of the cytoplasmic domain of the human immunodeficiency virus type 1 transmembrane glycoprotein gp41
    • DOI 10.1074/jbc.M000601200
    • Lee, S. F., Wang, C. T., Liang, J. Y., Hong, S. L., Huang, C. C. & Chen, S. S. (2000). Multimerization potential of the cytoplasmic domain of the human immunodeficiency virus type 1 transmembrane glycoprotein gp41. J. Biol. Chem. 275, 15809-15819. (Pubitemid 30366880)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.21 , pp. 15809-15819
    • Lee, S.-F.1    Wang, C.-T.2    Liang, J.Y.-P.3    Hong, S.-L.4    Huang, C.-C.5    Chen, S.S.-L.6
  • 184
    • 0343462450 scopus 로고    scopus 로고
    • Identification of two sequences in the cytoplasmic tail of the human immunodeficiency virus type 1 envelope glycoprotein that inhibit cell surface expression
    • DOI 10.1128/JVI.75.11.5263-5276.2001
    • Bültmann, A., Muranyi, W., Seed, B. & Haas, J. (2001). Identification of two sequences in the cytoplasmic tail of the human immunodeficiency virus type 1 envelope glycoprotein that inhibit cell surface expression. J. Virol. 75, 5263-5276. (Pubitemid 32448549)
    • (2001) Journal of Virology , vol.75 , Issue.11 , pp. 5263-5276
    • Bultmann, A.1    Muranyi, W.2    Seed, B.3    Haas, J.4
  • 185
    • 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, 5783-5788. (Pubitemid 26375499)
    • (1996) EMBO Journal , vol.15 , Issue.21 , pp. 5783-5788
    • Cosson, P.1
  • 186
    • 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
    • DOI 10.1128/JVI.74.24.11717-11723.2000
    • Piller, S. C., Dubay, J. W., Derdeyn, C. A. & Hunter, E. (2000). Mutational analysis of conserved domains within the cytoplasmic tail of gp41 from human immunodeficiency virus type 1: effects on glycopro-tein incorporation and infectivity. J. Virol. 74, 11717-11723. (Pubitemid 32222321)
    • (2000) Journal of Virology , vol.74 , Issue.24 , pp. 11717-11723
    • Piller, S.C.1    Dubay, J.W.2    Derdeyn, C.A.3    Hunter, E.4
  • 187
    • 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
    • DOI 10.1128/JVI.75.20.9925-9938.2001
    • Chen, S. S., Lee, S. F. & Wang, C. T. (2001). Cellular membrane-binding ability of the C-terminal cyto-plasmic domain of human immunodeficiency virus type 1 envelope transmembrane protein gp41. J. Virol. 75, 9925-9938. (Pubitemid 32900127)
    • (2001) Journal of Virology , vol.75 , Issue.20 , pp. 9925-9938
    • Chen, S.S.-L.1    Lee, S.-F.2    Wang, C.-T.3
  • 188
    • 0028007195 scopus 로고
    • An amphipathic peptide from the C-terminal region of the human immunodeficiency virus envelope glycoprotein causes pore formation in membranes
    • Chernomordik, L., Chanturiya, A. N., Suss-Toby, E., Nora, E. & Zimmerberg, J. (1994). An amphipathic peptide from the C-terminal region of the human immunodeficiency virus envelope glycoprotein causes pore formation in membranes. J. Virol. 68, 7115-7123. (Pubitemid 24328763)
    • (1994) Journal of Virology , vol.68 , Issue.11 , pp. 7115-7123
    • Chernomordik, L.1    Chanturiya, A.N.2    Suss-Toby, E.3    Nora, E.4    Zimmerberg, J.5
  • 189
    • 0027523631 scopus 로고
    • Interaction of peptide fragment 828-848 of the envelope glycoprotein of human immunodeficiency virus type I with lipid bilayers
    • Gawrisch, K., Han, K. H., Yang, J. S., Bergelson, L. D. & Ferretti, J. A. (1993). Interaction of peptide fragment 828-848 of the envelope glycoprotein of human immunodeficiency virus type I with lipid bilayers. Biochemistry, 32, 3112-3118. (Pubitemid 23110155)
    • (1993) Biochemistry , vol.32 , Issue.12 , pp. 3112-3118
    • Gawrisch, K.1    Han, K.-H.2    Yang, J.-S.3    Bergelson, L.D.4    Ferretti, J.A.5
  • 191
    • 0029037538 scopus 로고
    • Effect of amino acid substitutions on calmodulin binding and cytolytic properties of the LLP-1 peptide segment of human immunodeficiency virus type 1 transmembrane protein
    • Tencza, S. B., Miller, M. A., Islam, K., Mietzner, T. A. & Montelaro, R. C. (1995). Effect of amino acid substitutions on calmodulin binding and cytolytic properties of the LLP-1 peptide segment of human immunodeficiency virus type 1 transmembrane protein. J. Virol. 69, 5199-5202.
    • (1995) J. Virol. , vol.69 , pp. 5199-5202
    • Tencza, S.B.1    Miller, M.A.2    Islam, K.3    Mietzner, T.A.4    Montelaro, R.C.5
  • 192
    • 0034610368 scopus 로고    scopus 로고
    • Palmitoylation of the HIV-1 envelope glyco-protein is critical for viral infectivity
    • Rousso, I., Mixon, M. B., Chen, B. K. & Kim, P. S. (2000). Palmitoylation of the HIV-1 envelope glyco-protein is critical for viral infectivity. Proc. Natl Acad. Sci. USA, 97, 13523-13525.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 13523-13525
    • Rousso, I.1    Mixon, M.B.2    Chen, B.K.3    Kim, P.S.4
  • 193
    • 72849138124 scopus 로고    scopus 로고
    • The cytoplasmic domain of human immunodeficiency virus type 1 transmembrane protein gp41 harbors lipid raft association determinants
    • Yang, P., Ai, L.-S., Huang, S.-C., Li, H.-F., Chan, W.-E., Chang, C.-W. et al. (2010). The cytoplasmic domain of human immunodeficiency virus type 1 transmembrane protein gp41 harbors lipid raft association determinants. J. Virol. 84, 59-75.
    • (2010) J. Virol. , vol.84 , pp. 59-75
    • Yang, P.1    Ai, L.-S.2    Huang, S.-C.3    Li, H.-F.4    Chan, W.-E.5    Chang, C.-W.6
  • 194
    • 0029052283 scopus 로고
    • Low pH induces swiveling of the glycoprotein heterodimers in the Semliki Forest virus spike complex
    • Fuller, S. D., Berriman, J. A., Butcher, S. J. & Gowen, B. E. (1995). Low pH induces swiveling of the glycoprotein heterodimers in the Semliki Forest virus spike complex. Cell, 81, 715-725.
    • (1995) Cell , vol.81 , pp. 715-725
    • Fuller, S.D.1    Berriman, J.A.2    Butcher, S.J.3    Gowen, B.E.4
  • 195
    • 9644260512 scopus 로고    scopus 로고
    • Budding of alphaviruses
    • DOI 10.1016/j.virusres.2004.08.008, PII S0168170204003193
    • Garoff, H., Sjöberg, M. & Cheng, R. H. (2004). Budding of alphaviruses. Virus Res. 106, 103-116. (Pubitemid 39572959)
    • (2004) Virus Research , vol.106 , Issue.2 SPEC.ISS. , pp. 103-116
    • Garoff, H.1    Sjoberg, M.2    Cheng, R.H.3
  • 196
    • 0025181513 scopus 로고
    • Expanded HIV-1 cellular tropism by phenotypic mixing with murine endogenous retroviruses
    • Lusso, P., di Marzo Veronese, F., Ensoli, B., Franchini, G., Jemma, C., DeRocco, S. E. et al. (1990). Expanded HIV-1 cellular tropism by phenotypic mixing with murine endogenous retroviruses. Science, 247, 848-852.
    • (1990) Science , vol.247 , pp. 848-852
    • Lusso, P.1    Di Marzo Veronese, F.2    Ensoli, B.3    Franchini, G.4    Jemma, C.5    Derocco, S.E.6
  • 197
    • 0027049212 scopus 로고
    • Cellular proteins bound to immunodeficiency viruses: Implications for pathogenesis and vaccines
    • Arthur, L. O., Bess, J. W., Sowder, R. C., Benveniste, R. E., Mann, D. L., Chermann, J. C. & Henderson, L. E. (1992). Cellular proteins bound to immunodeficiency viruses: implications for pathogenesis and vaccines. Science, 258, 1935-1938. (Pubitemid 23026732)
    • (1992) Science , vol.258 , Issue.5090 , pp. 1935-1938
    • Arthur, L.O.1    Bess Jr., J.W.2    Sowder II, R.C.3    Benveniste, R.E.4    Mann, D.L.5    Chermann, J.-C.6    Henderson, L.E.7
  • 198
    • 43749122571 scopus 로고    scopus 로고
    • Cellular proteins detected in HIV-1
    • DOI 10.1002/rmv.570
    • Ott, D. E. (2008). Cellular proteins detected in HIV-1. Rev. Med. Virol. 18, 159-175. (Pubitemid 351693494)
    • (2008) Reviews in Medical Virology , vol.18 , Issue.3 , pp. 159-175
    • Ott, D.E.1
  • 199
    • 0025005828 scopus 로고
    • Construction and use of a human immunodeficiency virus vector for analysis of virus infectivity
    • Page, K. A., Landau, N. R. & Littman, D. R. (1990). Construction and use of a human immunodeficiency virus vector for analysis of virus infectivity. J. Virol. 64, 5270-5276. (Pubitemid 20364514)
    • (1990) Journal of Virology , vol.64 , Issue.11 , pp. 5270-5276
    • Page, K.A.1    Landau, N.R.2    Littman, D.R.3
  • 200
    • 22944458202 scopus 로고    scopus 로고
    • Altering the tropism of lentiviral vectors through pseudotyping
    • DOI 10.2174/1566523054546224
    • Cronin, J., Zhang, X.-Y. & Reiser, J. (2005). Altering the tropism of lentiviral vectors through pseudotyp-ing. Curr. Gene Ther. 5, 387-398. (Pubitemid 41052430)
    • (2005) Current Gene Therapy , vol.5 , Issue.4 , pp. 387-398
    • Cronin, J.1    Zhang, X.-Y.2    Reiser, J.3
  • 201
    • 0030589456 scopus 로고    scopus 로고
    • Characterization of an envelope mutant of HIV-1 that interferes with viral infectivity
    • DOI 10.1006/viro.1996.0654
    • Chen, S. S., Ferrante, A. A. & Terwilliger, E. F. (1996). Characterization of an envelope mutant of HIV-1 that interferes with viral infectivity. Virology, 226, 260-268. (Pubitemid 27025806)
    • (1996) Virology , vol.226 , Issue.2 , pp. 260-268
    • Chen, S.S.-L.1    Ferrante, A.A.2    Terwilliger, E.F.3
  • 202
    • 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, 4966-4971.
    • (1992) J. Virol. , vol.66 , pp. 4966-4971
    • Yu, X.1    Yuan, X.2    Matsuda, Z.3    Lee, T.H.4    Essex, M.5
  • 203
    • 0027979135 scopus 로고
    • Role of the matrix protein in the virion association of the human immunodeficiency virus type 1 envelope glycoprotein
    • Dorfman, T., Mammano, F., Haseltine, W. 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, 1689-1696. (Pubitemid 24065736)
    • (1994) Journal of Virology , vol.68 , Issue.3 , pp. 1689-1696
    • Dorfman, T.1    Mammano, F.2    Haseltine, W.A.3    Gottlinger, H.G.4
  • 204
    • 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, 3824-3830.
    • (1995) J. Virol. , vol.69 , pp. 3824-3830
    • Mammano, F.1    Kondo, E.2    Sodroski, J.3    Bukovsky, A.4    Gottlinger, H.G.5
  • 205
    • 0032079344 scopus 로고    scopus 로고
    • Efficient HIV-1 replication can occur in the absence of the viral matrix protein
    • DOI 10.1093/emboj/17.9.2699
    • Reil, H., Bukovsky, A. A., Gelderblom, H. R. & Gottlinger, H. G. (1998). Efficient HIV-1 replication can occur in the absence of the viral matrix protein. EMBO J. 17, 2699-2708. (Pubitemid 28221204)
    • (1998) EMBO Journal , vol.17 , Issue.9 , pp. 2699-2708
    • Reil, H.1    Bukovsky, A.A.2    Gelderblom, H.R.3    Gottlinger, H.4
  • 206
    • 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, 6616-6625.
    • (1992) J. Virol. , vol.66 , pp. 6616-6625
    • Dubay, J.W.1    Roberts, S.J.2    Hahn, B.H.3    Hunter, E.4
  • 207
    • 0035110907 scopus 로고    scopus 로고
    • Modification of virus infectivity by cytoplasmic tail of HIV-1 TM protein
    • DOI 10.1016/S0168-1702(00)00249-5, PII S0168170200002495
    • Iwatani, Y., Ueno, T., Nishimura, A., Zhang, X., Hattori, T., Ishimoto, A. et al. (2001). Modification of virus infectivity by cytoplasmic tail of HIV-1 TM protein. Virus Res. 74, 75-87. (Pubitemid 32168195)
    • (2001) Virus Research , vol.74 , Issue.1-2 , pp. 75-87
    • Iwatani, Y.1    Ueno, T.2    Nishimura, A.3    Zhang, X.4    Hattori, T.5    Ishimoto, A.6    Ito, M.7    Sakai, H.8
  • 208
    • 0029565831 scopus 로고
    • Crystal structure of SIV matrix antigen and implications for virus assembly
    • DOI 10.1038/378743a0
    • Rao, Z., Belyaev, A. S., Fry, E., Roy, P., Jones, I. M. & Stuart, D. I. (1995). Crystal structure of SIV matrix antigen and implications for virus assembly. Nature, 378, 743-747. (Pubitemid 26001950)
    • (1995) Nature , vol.378 , Issue.6558 , pp. 743-747
    • Rao, Z.1    Belyaev, A.S.2    Fry, E.3    Roy, P.4    Jonest, I.M.5    Stuart, D.I.6
  • 209
    • 0029062117 scopus 로고
    • Role of the basic domain of human immunodeficiency virus type 1 matrix in macrophage infection
    • Freed, E. O., Englund, G. & Martin, M. A. (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
  • 210
    • 0024498289 scopus 로고
    • Expression of the human immunodeficiency virus envelope glycoprotein is restricted to basolateral surfaces of polarized epithelial cells
    • Owens, R. J. & Compans, R. W. (1989). Expression of the human immunodeficiency virus envelope glyco-protein is restricted to basolateral surfaces of polarized epithelial cells. J. Virol. 63, 978-982. (Pubitemid 19057274)
    • (1989) Journal of Virology , vol.63 , Issue.2 , pp. 978-982
    • Owens, R.J.1    Compans, R.W.2
  • 212
    • 0028229632 scopus 로고
    • The intracytoplasmic domain of gp41 mediates polarized budding of human immunodeficiency virus type 1 in MDCK cells
    • Lodge, R., Gottlinger, H. G., 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, 4857-4861. (Pubitemid 24226550)
    • (1994) Journal of Virology , vol.68 , Issue.8 , pp. 4857-4861
    • Lodge, R.1    Gottlinger, H.2    Gabuzda, D.3    Cohen, E.A.4    Lemay, G.5
  • 213
    • 1842457792 scopus 로고    scopus 로고
    • Coupling of Human Immunodeficiency Virus Type 1 Fusion to Virion Maturation: A Novel Role of the gp41 Cytoplasmic Tail
    • DOI 10.1128/JVI.78.7.3429-3435.2004
    • 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 cytoplas-mic tail. J. Virol. 78, 3429-3435. (Pubitemid 38568284)
    • (2004) Journal of Virology , vol.78 , Issue.7 , 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
  • 214
    • 0347319099 scopus 로고    scopus 로고
    • Regulation of human immunodeficiency virus type 1 Env-mediated membrane fusion by viral protease activity
    • DOI 10.1128/JVI.78.2.1026-1031.2004
    • Murakami, T., Ablan, S. D., Freed, E. O. & Tanaka, Y. (2004). Regulation of human immunodeficiency virus type 1 Env-mediated membrane fusion by viral protease activity. J. Virol. 78, 1026-1031. (Pubitemid 38067625)
    • (2004) Journal of Virology , vol.78 , Issue.2 , pp. 1026-1031
    • Murakami, T.1    Ablan, S.2    Freed, E.O.3    Tanaka, Y.4
  • 215
    • 35348908350 scopus 로고    scopus 로고
    • Maturation-dependent human immunodeficiency virus type 1 particle fusion requires a carboxyl-terminal region of the gp41 cytoplasmic tail
    • DOI 10.1128/JVI.00592-07
    • 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. (Pubitemid 350067703)
    • (2007) Journal of Virology , vol.81 , Issue.18 , pp. 9999-10008
    • Jiang, J.1    Aiken, C.2
  • 217
    • 0033035418 scopus 로고    scopus 로고
    • Reversion of a human immunodeficiency virus type 1 matrix mutation affecting Gag membrane binding, endogenous reverse transcriptase activity, and virus infectivity
    • Kiernan, R. E., Ono, A. & Freed, E. O. (1999). Reversion of a human immunodeficiency virus type 1 matrix mutation affecting Gag membrane binding, endogenous reverse transcriptase activity, and virus infectivity. J. Virol. 73, 4728-4737. (Pubitemid 29246732)
    • (1999) Journal of Virology , vol.73 , Issue.6 , pp. 4728-4737
    • Kiernan, R.E.1    Ono, A.2    Freed, E.O.3
  • 218
    • 33144475031 scopus 로고    scopus 로고
    • A mutation in the human immunodeficiency virus type 1 Gag protein destabilizes the interaction of the envelope protein subunits gp120 and gp41
    • DOI 10.1128/JVI.80.5.2405-2417.2006
    • Davis, M. R., Jiang, J., Zhou, J., Freed, E. O. & Aiken, C. (2006). A mutation in the human immunodeficiency virus type 1 Gag protein destabilizes the interaction of the envelope protein subunits gp120 and gp41. J. Virol. 80, 2405-2417. (Pubitemid 43271546)
    • (2006) Journal of Virology , vol.80 , Issue.5 , pp. 2405-2417
    • Davis, M.R.1    Jiang, J.2    Zhou, J.3    Freed, E.O.4    Aiken, C.5
  • 219
    • 0034632924 scopus 로고    scopus 로고
    • Identification of the glycoprotein 41(TM) cytoplasmic tail domains of human immunodeficiency virus type 1 that interact with Pr55(Gag) particles
    • DOI 10.1089/088922200414983
    • Hourioux, C., Brand, D., Sizaret, P. Y., Lemiale, F., Lebigot, S., Barin, F. & Roingeard, P. (2000). Identification of the glycoprotein 41(TM) cytoplas-mic tail domains of human immunodeficiency virus type 1 that interact with Pr55Gag particles. AIDS Res. Hum. Retroviruses, 16, 1141-1147. (Pubitemid 30637015)
    • (2000) AIDS Research and Human Retroviruses , vol.16 , Issue.12 , pp. 1141-1147
    • Hourioux, C.1    Brand, D.2    Sizaret, P.-Y.3    Lemiale, F.4    Lebigot, S.5    Barin, F.6    Roingeard, P.7
  • 220
    • 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, 9381-9387.
    • (2000) J. Virol. , vol.74 , pp. 9381-9387
    • Wyma, D.J.1    Kotov, A.2    Aiken, C.3
  • 221
    • 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, 8138-8144. (Pubitemid 29441674)
    • (1999) Journal of Virology , vol.73 , Issue.10 , pp. 8138-8144
    • Vincent, M.J.1    Melsen, L.R.2    Martin, A.S.3    Compans, R.W.4
  • 222
    • 0034000261 scopus 로고    scopus 로고
    • Cell-dependent requirement of human immunodeficiency virus type 1 gp41 cytoplasmic tail for Env incorporation into virions
    • DOI 10.1128/JVI.74.10.4891-4893.2000
    • 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, 4891-4893 (Pubitemid 30237919)
    • (2000) Journal of Virology , vol.74 , Issue.10 , pp. 4891-4893
    • Akari, H.1    Fukumori, T.2    Adachi, A.3
  • 225
    • 0032488222 scopus 로고    scopus 로고
    • Importance of the intracytoplasmic domain of the simian immunodeficiency virus (SIV) envelope glycoprotein for pathogenesis
    • DOI 10.1006/viro.1998.9467
    • Luciw, P. A., Shaw, K. E., Shacklett, B. L. & Marthas, M. L. (1998). Importance of the intracytoplasmic domain of the simian immunodeficiency virus (SIV) envelope glycoprotein for pathogenesis. Virology, 252, 9-16. (Pubitemid 28564127)
    • (1998) Virology , vol.252 , Issue.1 , pp. 9-16
    • Luciw, P.A.1    Shaw, K.E.S.2    Shacklett, B.L.3    Marthas, M.L.4
  • 226
    • 39449085222 scopus 로고    scopus 로고
    • Role of the long cytoplasmic domain of the SIV Env glycoprotein in early and late stages of infection
    • Vzorov, A. N., Weidmann, A., Kozyr, N. L., Khaoustov, V., Yoffe, B. & Compans, R. W. (2007). Role of the long cytoplasmic domain of the SIV Env glycoprotein in early and late stages of infection. Retrovirology, 4, 94.
    • (2007) Retrovirology , vol.4 , pp. 94
    • Vzorov, A.N.1    Weidmann, A.2    Kozyr, N.L.3    Khaoustov, V.4    Yoffe, B.5    Compans, R.W.6
  • 227
    • 33746085241 scopus 로고    scopus 로고
    • Rafts defined: A report on the Keystone symposium on lipid rafts and cell function
    • DOI 10.1194/jlr.E600002-JLR200
    • Pike, L. J. (2006). Rafts defined: a report on the Keystone Symposium on Lipid Rafts and Cell Function. J. Lipid Res. 47, 1597-1598. (Pubitemid 44079915)
    • (2006) Journal of Lipid Research , vol.47 , Issue.7 , pp. 1597-1598
    • Pike, L.J.1
  • 228
    • 77957167810 scopus 로고    scopus 로고
    • Revitalizing membrane rafts: New tools and insights
    • Simons, K. & Gerl, M. J. (2010). Revitalizing membrane rafts: new tools and insights. Nat. Rev., Mol. Cell Biol. 11, 688-699.
    • (2010) Nat. Rev., Mol. Cell Biol. , vol.11 , pp. 688-699
    • Simons, K.1    Gerl, M.J.2
  • 229
    • 0344585437 scopus 로고    scopus 로고
    • Lipid rafts: Elusive or illusive?
    • DOI 10.1016/S0092-8674(03)00882-1
    • Munro, S. (2003). Lipid rafts: elusive or illusive? Cell, 115, 377-388. (Pubitemid 37456801)
    • (2003) Cell , vol.115 , Issue.4 , pp. 377-388
    • Munro, S.1
  • 230
    • 68749106894 scopus 로고    scopus 로고
    • Lipids and membrane microdomains in HIV-1 replication
    • Waheed, A. A. & Freed, E. O. (2009). Lipids and membrane microdomains in HIV-1 replication. Virus Res. 143, 162-176.
    • (2009) Virus Res. , vol.143 , pp. 162-176
    • Waheed, A.A.1    Freed, E.O.2
  • 231
    • 79952088584 scopus 로고    scopus 로고
    • The role of lipids in retrovirus replication
    • Waheed, A. A. & Freed, E. O. (2010). The role of lipids in retrovirus replication. Viruses, 2, 1146-1180.
    • (2010) Viruses , vol.2 , pp. 1146-1180
    • Waheed, A.A.1    Freed, E.O.2
  • 232
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown, D. A. & Rose, J. K. (1992). Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell, 68, 533-544.
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 233
    • 0034625373 scopus 로고    scopus 로고
    • Structure and function of sphingolipid- and cholesterol-rich membrane rafts
    • DOI 10.1074/jbc.R000005200
    • Brown, D. A. & London, E. (2000). Structure and function of sphingolipid-and cholesterol-rich membrane rafts. J. Biol. Chem. 275, 17221-17224. (Pubitemid 30430750)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.23 , pp. 17221-17224
    • Brown, D.A.1    London, E.2
  • 235
    • 0034015604 scopus 로고    scopus 로고
    • Evidence for budding of human immunodeficiency virus type 1 selectively from glycolipid-enriched membrane lipid rafts
    • DOI 10.1128/JVI.74.7.3264-3272.2000
    • 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, 3264-3272. (Pubitemid 30143751)
    • (2000) Journal of Virology , vol.74 , Issue.7 , pp. 3264-3272
    • Nguyen, D.H.1    Hildreth, J.E.K.2
  • 237
    • 0034951851 scopus 로고    scopus 로고
    • Lipid rafts and pseudotyping
    • DOI 10.1128/JVI.75.15.7175-7183.2001
    • Pickl, W. F., Pimentel-Muiños, F. X. & Seed, B. (2001). Lipid rafts and pseudotyping. J. Virol. 75, 7175-7183. (Pubitemid 32641605)
    • (2001) Journal of Virology , vol.75 , Issue.15 , pp. 7175-7183
    • Pickl, W.F.1    Pimentel-Muinios, F.X.2    Seed, B.3
  • 238
    • 0034864631 scopus 로고    scopus 로고
    • Multimerization of human immunodeficiency virus type 1 Gag promotes its localization to barges, raft-like membrane microdomains
    • DOI 10.1128/JVI.75.17.7913-7924.2001
    • Lindwasser, O. W. & Resh, M. D. (2001). Multi-merization of human immunodeficiency virus type 1 Gag promotes its localization to barges, raft-like membrane microdomains. J. Virol. 75, 7913-7924. (Pubitemid 32743663)
    • (2001) Journal of Virology , vol.75 , Issue.17 , pp. 7913-7924
    • Lindwasser, O.W.1    Resh, M.D.2
  • 239
    • 0037384986 scopus 로고    scopus 로고
    • gag associates with membrane domains that are largely resistant to Brij98 but sensitive to triton X-100
    • DOI 10.1128/JVI.77.8.4805-4817.2003
    • Holm, K., Weclewicz, K., Hewson, R.& Suomalainen, M. (2003). Human immunodeficiency virus type 1 assembly and lipid rafts: Pr55(gag) associates with membrane domains that are largely resistant to Brij98 but sensitive to Triton X-100. J. Virol. 77, 4805-4817. (Pubitemid 36402830)
    • (2003) Journal of Virology , vol.77 , Issue.8 , pp. 4805-4817
    • Holm, K.1    Weclewicz, K.2    Hewson, R.3    Suomalainen, M.4
  • 240
    • 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
  • 241
    • 52649145364 scopus 로고    scopus 로고
    • Inhibition of human immunodeficiency virus type 1 assembly and release by the cholesterol-binding compound amphotericin B methyl ester: Evidence for Vpu dependence
    • Waheed, A. A., Ablan, S. D., Soheilian, F., Nagashima, K., Ono, A., Schaffner, C. P. & Freed, E. O. (2008). Inhibition of human immunodeficiency virus type 1 assembly and release by the cholesterol-binding compound amphotericin B methyl ester: evidence for Vpu dependence. J. Virol. 82, 9776-9781.
    • (2008) J. Virol. , vol.82 , pp. 9776-9781
    • Waheed, A.A.1    Ablan, S.D.2    Soheilian, F.3    Nagashima, K.4    Ono, A.5    Schaffner, C.P.6    Freed, E.O.7
  • 242
    • 0037379284 scopus 로고    scopus 로고
    • Rapid localization of Gag/GagPol complexes to detergent-resistant membrane during the assembly of human immunodeficiency virus type 1
    • DOI 10.1128/JVI.77.7.3973-3984.2003
    • 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, 3973-3984. (Pubitemid 36350938)
    • (2003) Journal of Virology , vol.77 , Issue.7 , pp. 3973-3984
    • Halwani, R.1    Khorchid, A.2    Cen, S.3    Kleiman, L.4
  • 244
    • 55549118226 scopus 로고    scopus 로고
    • Retroviruses human immunodeficiency virus and murine leukemia virus are enriched in phosphoinositides
    • Chan, R., Uchil, P. D., Jin, J., Shui, G., Ott, D. E., Mothes, W. & Wenk, M. R. (2008). Retroviruses human immunodeficiency virus and murine leukemia virus are enriched in phosphoinositides. J. Virol. 82, 11228-11238.
    • (2008) J. Virol. , vol.82 , pp. 11228-11238
    • Chan, R.1    Uchil, P.D.2    Jin, J.3    Shui, G.4    Ott, D.E.5    Mothes, W.6    Wenk, M.R.7
  • 245
    • 20744433027 scopus 로고    scopus 로고
    • Wild-type-like viral replication potential of human immunodeficiency virus type 1 envelope mutants lacking palmitoylation signals
    • DOI 10.1128/JVI.79.13.8374-8387.2005
    • Chan, W.-E., Lin, H.-H. & Chen, S. S.-L. (2005). Wild-type-like viral replication potential of human immunodeficiency virus type 1 envelope mutants lacking palmitoylation signals. J. Virol. 79, 8374-8387. (Pubitemid 40853540)
    • (2005) Journal of Virology , vol.79 , Issue.13 , pp. 8374-8387
    • Chan, W.-E.1    Lin, H.-H.2    Chen, S.S.-L.3
  • 246
    • 2342539802 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 envelope glycoproteins that lack cytoplasmic domain cyste-ines: Impact on association with membrane lipid rafts and incorporation onto budding virus particles
    • DOI 10.1128/JVI.78.10.5500-5506.2004
    • Bhattacharya, J., Peters, P. J. & Clapham, P. R. (2004). Human immunodeficiency virus type 1 envelope glycoproteins that lack cytoplasmic domain cyste-ines: impact on association with membrane lipid rafts and incorporation onto budding virus particles. J. Virol. 78, 5500-5506. (Pubitemid 38581500)
    • (2004) Journal of Virology , vol.78 , Issue.10 , pp. 5500-5506
    • Bhattacharya, J.1    Peters, P.J.2    Clapham, P.R.3
  • 247
    • 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, 5292-5300.
    • (2006) J. Virol. , vol.80 , pp. 5292-5300
    • Bhattacharya, J.1    Repik, A.2    Clapham, P.R.3
  • 248
    • 43049168496 scopus 로고    scopus 로고
    • HIV-1 Assembly: Viral Glycoproteins Segregate Quantally to Lipid Rafts that Associate Individually with HIV-1 Capsids and Virions
    • DOI 10.1016/j.chom.2008.04.004, PII S1931312808001224
    • Leung, K., Kim, J.-O., Ganesh, L., Kabat, J., Schwartz, O. & Nabel, G. J. (2008). HIV-1 assembly: viral glycoproteins segregate quantally to lipid rafts that associate individually with HIV-1 capsids and virions. Cell Host Microbe, 3, 285-292. (Pubitemid 351636000)
    • (2008) Cell Host and Microbe , vol.3 , Issue.5 , pp. 285-292
    • Leung, K.1    Kim, J.-O.2    Ganesh, L.3    Kabat, J.4    Schwartz, O.5    Nabel, G.J.6
  • 249
    • 66149156145 scopus 로고    scopus 로고
    • Foreign glycoproteins can be actively recruited to virus assembly sites during pseudotyping
    • Jorgenson, R. L., Vogt, V. M. & Johnson, M. C. (2009). Foreign glycoproteins can be actively recruited to virus assembly sites during pseudotyping. J. Virol. 83, 4060-4067.
    • (2009) J. Virol. , vol.83 , pp. 4060-4067
    • Jorgenson, R.L.1    Vogt, V.M.2    Johnson, M.C.3
  • 251
    • 27644598271 scopus 로고    scopus 로고
    • Interaction of HIV-1 Gag with the clathrin-associated adaptor AP-2
    • DOI 10.1016/j.virol.2005.08.001, PII S0042682205004538
    • Batonick, M., Favre, M., Boge, M., Spearman, P., Höning, S. & Thali, M. (2005). Interaction of HIV-1 Gag with the clathrin-associated adaptor AP-2. Virology, 342, 190-200. (Pubitemid 41566652)
    • (2005) Virology , vol.342 , Issue.2 , pp. 190-200
    • Batonick, M.1    Favre, M.2    Boge, M.3    Spearman, P.4    Honing, S.5    Thali, M.6
  • 252
    • 0032076636 scopus 로고    scopus 로고
    • Tip47: A cargo selection device for mannose 6-phosphate receptor trafficking
    • DOI 10.1016/S0092-8674(00)81171-X
    • Díaz, E. & Pfeffer, S. R. (1998). TIP47: a cargo selection device for mannose 6-phosphate receptor trafficking. Cell, 93, 433-443. (Pubitemid 28232087)
    • (1998) Cell , vol.93 , Issue.3 , pp. 433-443
    • Diaz, E.1    Pfeffer, S.R.2
  • 253
    • 0035906951 scopus 로고    scopus 로고
    • Role of Rab9 GTPase in facilitating receptor recruitment by TIP47
    • DOI 10.1126/science.1056791
    • Carroll, K. S., Hanna, J., Simon, I., Krise, J., Barbero, P. & Pfeffer, S. R. (2001). Role of Rab9 GTPase in facilitating receptor recruitment by TIP47. Science, 292, 1373-1376. (Pubitemid 32476223)
    • (2001) Science , vol.292 , Issue.5520 , pp. 1373-1376
    • Carroll, K.S.1    Hanna, J.2    Simon, I.3    Krise, J.4    Barbero, P.5    Pfeffer, S.R.6
  • 254
    • 0035895982 scopus 로고    scopus 로고
    • TIP47 associates with lipid droplets
    • Wolins, N. E., Rubin, B. & Brasaemle, D. L. (2001). TIP47 associates with lipid droplets. J. Biol. Chem. 276, 5101-5108.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5101-5108
    • Wolins, N.E.1    Rubin, B.2    Brasaemle, D.L.3
  • 255
    • 0037200026 scopus 로고    scopus 로고
    • Functional conservation for lipid storage droplet association among perilipin, ADRP, and TIP47 (PAT)-related proteins in mammals, Drosophila, and Dictyostelium
    • DOI 10.1074/jbc.M204410200
    • Miura, S., Gan, J.-W., Brzostowski, J., Parisi, M. J., Schultz, C. J., Londos, C. et al. (2002). Functional conservation for lipid storage droplet association among Perilipin, ADRP, and TIP47 (PAT)-related proteins in mammals, Drosophila, and Dictyostelium. J. Biol. Chem. 277, 32253-32257. (Pubitemid 34969041)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.35 , pp. 32253-32257
    • Miura, S.1    Gan, J.-W.2    Brzostowski, J.3    Parisi, M.J.4    Schultz, C.J.5    Londos, C.6    Oliver, B.7    Kimmel, A.R.8
  • 257
  • 258
    • 66349128492 scopus 로고    scopus 로고
    • PAT proteins an ancient family of lipid droplet proteins that regulate cellular lipid stores
    • Bickel, P. E., Tansey, J. T. & Welte, M. A. (2009). PAT proteins, an ancient family of lipid droplet proteins that regulate cellular lipid stores. Biochim. Biophys. Acta, 1791, 419-440.
    • (2009) Biochim. Biophys. Acta , vol.1791 , pp. 419-440
    • Bickel, P.E.1    Tansey, J.T.2    Welte, M.A.3
  • 259
    • 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
    • DOI 10.1128/JVI.77.12.6931-6945.2003
    • 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, 6931-6945. (Pubitemid 36666886)
    • (2003) Journal of Virology , vol.77 , Issue.12 , pp. 6931-6945
    • Blot, G.1    Janvier, K.2    Le Panse, S.3    Benarous, R.4    Berlioz-Torrent, C.5
  • 261
    • 77951793799 scopus 로고    scopus 로고
    • TIP47 is required for the production of infectious HIV-1 particles from primary macrophages
    • Bauby, H., Lopez-Vergès, S., Hoeffel, G., Delcroix-Genête, D., Janvier, K., Mammano, F. et al. (2010). TIP47 is required for the production of infectious HIV-1 particles from primary macrophages. Traffic, 11, 455-467.
    • (2010) Traffic , vol.11 , pp. 455-467
    • Bauby, H.1    Lopez-Vergès, S.2    Hoeffel, G.3    Delcroix-Genête, D.4    Janvier, K.5    Mammano, F.6
  • 262
    • 13644268540 scopus 로고    scopus 로고
    • Dlgh1 coordinates actin polymerization, synaptic T cell receptor and lipid raft aggregation, and effector function in T cells
    • DOI 10.1084/jem.20041428
    • Round, J. L., Tomassian, T., Zhang, M., Patel, V., Schoenberger, S. P. & Miceli, M. C. (2005). Dlgh1 coordinates actin polymerization, synaptic T cell receptor and lipid raft aggregation, and effector function in T cells. J. Exp. Med. 201, 419-430. (Pubitemid 40229416)
    • (2005) Journal of Experimental Medicine , vol.201 , Issue.3 , pp. 419-430
    • Round, J.L.1    Tomassian, T.2    Zhang, M.3    Patel, V.4    Schoenberger, S.P.5    Miceli, M.C.6
  • 263
    • 4444251676 scopus 로고    scopus 로고
    • Human Dlg protein binds to the envelope glycoproteins of human T-cell leukemia virus type 1 and regulates envelope mediated cell-cell fusion in T lymphocytes
    • DOI 10.1242/jcs.01266
    • Blot, V., Delamarre, L., Perugi, F., Pham, D., Bénichou, S., Benarous, R. et al. (2004). Human Dlg protein binds to the envelope glycoproteins of human T-cell leukemia virus type 1 and regulates envelope mediated cell-cell fusion in T lymphocytes. J. Cell Sci. 117, 3983-3993. (Pubitemid 39207334)
    • (2004) Journal of Cell Science , vol.117 , Issue.17 , pp. 3983-3993
    • Blot, V.1    Delamarre, L.2    Perugi, F.3    Pham, D.4    Benichou, S.5    Benarous, R.6    Hanada, T.7    Chishti, A.H.8    Dokhelar, M.-C.9    Pique, C.10
  • 264
    • 63049134547 scopus 로고    scopus 로고
    • Human Discs Large is a new negative regulator of human immunodeficiency virus-1 infectivity
    • Perugi, F., Muriaux, D., Ramirez, B. C., Chabani, S., Decroly, E., Darlix, J.-L. et al. (2009). Human Discs Large is a new negative regulator of human immunodeficiency virus-1 infectivity. Mol. Biol. Cell, 20, 498-508.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 498-508
    • Perugi, F.1    Muriaux, D.2    Ramirez, B.C.3    Chabani, S.4    Decroly, E.5    Darlix, J.-L.6
  • 266
    • 0027505042 scopus 로고
    • Cytosolic domain of the human immunodeficiency virus envelope glycoproteins binds to calmodulin and inhibits calmodulin-regulated proteins
    • Srinivas, S. K., Srinivas, R. V., Anantharamaiah, G. M., Compans, R. W. & Segrest, J. P. (1993). Cytosolic domain of the human immunodeficiency virus envelope glycoproteins binds to calmodulin and inhibits calmodulin-regulated proteins. J. Biol. Chem. 268, 22895-22899. (Pubitemid 23318354)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.30 , pp. 22895-22899
    • Srinivas, S.K.1    Srinivas, R.V.2    Anantharamaiah, G.M.3    Compans, R.W.4    Segrest, J.P.5
  • 267
    • 0027421380 scopus 로고
    • Identification of a calmodulin-binding and inhibitory peptide domain in the HIV-1 transmembrane glycoprotein
    • Miller, M. A., Mietzner, T. A., Cloyd, M. W., Robey, W. G. & Montelaro, R. C. (1993). Identification of a calmodulin-binding and inhibitory peptide domain in the HIV-1 transmembrane glycoprotein. AIDS Res. Hum. Retroviruses, 9, 1057-1066. (Pubitemid 23347339)
    • (1993) AIDS Research and Human Retroviruses , vol.9 , Issue.11 , pp. 1057-1066
    • Miller, M.A.1    Mietzner, T.A.2    Cloyd, M.W.3    Robey, W.G.4    Montelaro, R.C.5
  • 268
    • 0031039143 scopus 로고    scopus 로고
    • Calmodulin-binding function of LLP segments from the HIV type 1 transmembrane protein is conserved among natural sequence variants
    • Tencza, S. B., Mietzner, T. A. & Montelaro, R. C. (1997). Calmodulin-binding function of LLP segments from the HIV type 1 transmembrane protein is conserved among natural sequence variants. AIDS Res. Hum. Retroviruses, 13, 263-269. (Pubitemid 27076272)
    • (1997) AIDS Research and Human Retroviruses , vol.13 , Issue.3 , pp. 263-269
    • Tencza, S.B.1    Mietzner, T.A.2    Montelaro, R.C.3
  • 269
    • 0033972086 scopus 로고    scopus 로고
    • Requirement of calmodulin binding by HIV-1 gp160 for enhanced FAS- mediated apoptosis
    • DOI 10.1074/jbc.275.2.1233
    • Micoli, K. J., Pan, G., Wu, Y., Williams, J. P., Cook, W. J. & McDonald, J. M. (2000). Requirement of calmodulin binding by HIV-1 gp160 for enhanced FAS-mediated apoptosis. J. Biol. Chem. 275, 1233-1240. (Pubitemid 30051176)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.2 , pp. 1233-1240
    • Micoli, K.J.1    Pan, G.2    Wu, Y.3    Williams, J.P.4    Cook, W.J.5    McDonald, J.M.6
  • 271
    • 0031903411 scopus 로고    scopus 로고
    • Apoptosis induction by the binding of the carboxyl terminus of human immunodeficiency virus type 1 gp160 to calmodulin
    • Ishikawa, H., Sasaki, M., Noda, S. & Koga, Y. (1998). Apoptosis induction by the binding of the carboxyl terminus of human immunodeficiency virus type 1 gp160 to calmodulin. J. Virol. 72, 6574-6580. (Pubitemid 28323973)
    • (1998) Journal of Virology , vol.72 , Issue.8 , pp. 6574-6580
    • Ishikawa, H.1    Sasaki, M.2    Noda, S.3    Koga, Y.4
  • 272
    • 30044444606 scopus 로고    scopus 로고
    • Point mutations in the C-terminus of HIV-1 gp160 reduce apoptosis and calmodulin binding without affecting viral replication
    • DOI 10.1016/j.virol.2005.08.033, PII S0042682205005271
    • Micoli, K. J., Mamaeva, O., Piller, S. C., Barker, J. L., Pan, G., Hunter, E. & McDonald, J. M. (2006). Point mutations in the C-terminus of HIV-1 gp160 reduce apoptosis and calmodulin binding without affecting viral replication. Virology, 344, 468-479. (Pubitemid 43049633)
    • (2006) Virology , vol.344 , Issue.2 , pp. 468-479
    • Micoli, K.J.1    Mamaeva, O.2    Piller, S.C.3    Barker, J.L.4    Pan, G.5    Hunter, E.6    McDonald, J.M.7
  • 273
    • 0031908105 scopus 로고    scopus 로고
    • Interruption of T-cell signal transduction by lentivirus lytic peptides from HIV-1 transmembrane protein
    • Beary, T. P., Tencza, S. B., Mietzner, T. A. & Montelaro, R. C. (1998). Interruption of T-cell signal transduction by lentivirus lytic peptides from HIV-1 transmembrane protein. J. Pept. Res. 51, 75-79. (Pubitemid 28065200)
    • (1998) Journal of Peptide Research , vol.51 , Issue.1 , pp. 75-79
    • Beary, T.P.1    Tencza, S.B.2    Mietzner, T.A.3    Montelaro, R.C.4
  • 275
    • 78650636013 scopus 로고    scopus 로고
    • Binding of calmodulin to the HIV-1 matrix protein triggers myristate exposure
    • Ghanam, R. H., Fernandez, T. F., Fledderman, E. L. & Saad, J. S. (2010). Binding of calmodulin to the HIV-1 matrix protein triggers myristate exposure. J. Biol. Chem. 285, 41911-41920.
    • (2010) J. Biol. Chem. , vol.285 , pp. 41911-41920
    • Ghanam, R.H.1    Fernandez, T.F.2    Fledderman, E.L.3    Saad, J.S.4
  • 277
    • 0033617769 scopus 로고    scopus 로고
    • The cytoplasmic domain of HIV-1 gp41 interacts with the carboxyl-terminal region of α-catenin
    • Kim, E. M., Lee, K. H. & Kim, J. W. (1999). The cytoplasmic domain of HIV-1 gp41 interacts with the carboxyl-terminal region of alpha-catenin. Mol. Cell, 9, 281-285. (Pubitemid 129555793)
    • (1999) Molecules and Cells , vol.9 , Issue.3 , pp. 281-285
    • Kim, E.M.1    Lee, K.H.2    Kim, J.W.3
  • 278
    • 28344439885 scopus 로고    scopus 로고
    • α-catenin is a molecular switch that binds E-cadherin-β- catenin and regulates actin-filament assembly
    • DOI 10.1016/j.cell.2005.09.021, PII S009286740500975X
    • Drees, F., Pokutta, S., Yamada, S., Nelson, W. J. & Weis, W. I. (2005). Alpha-catenin is a molecular switch that binds E-cadherin-beta-catenin and regulates actin-filament assembly. Cell, 123, 903-915. (Pubitemid 41721035)
    • (2005) Cell , vol.123 , Issue.5 , pp. 903-915
    • Drees, F.1    Pokutta, S.2    Yamada, S.3    Nelson, W.J.4    Weis, W.I.5
  • 279
    • 42449102211 scopus 로고    scopus 로고
    • Biochemical and structural analysis of α-catenin in cell-cell contacts
    • DOI 10.1042/BST0360141
    • Pokutta, S., Drees, F., Yamada, S., Nelson, W. J. & Weis, W. I. (2008). Biochemical and structural analysis of alpha-catenin in cell-cell contacts. Bio-chem. Soc. Trans. 36, 141-147. (Pubitemid 351570583)
    • (2008) Biochemical Society Transactions , vol.36 , Issue.2 , pp. 141-147
    • Pokutta, S.1    Drees, F.2    Yamada, S.3    Nelson, W.J.4    Weis, W.I.5
  • 282
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley, A. J. & Hall, A. (1992). The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell, 70, 389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 283
    • 0028961293 scopus 로고
    • Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes, C. D. & Hall, A. (1995). Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell, 81, 53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 284
    • 0029015774 scopus 로고
    • The Rho family GTPases RhoA, Rac1, and CDC42Hs regulate transcriptional activation by SRF
    • Hill, C. S., Wynne, J. & Treisman, R. (1995). The Rho family GTPases RhoA, Rac1, and CDC42Hs regulate transcriptional activation by SRF. Cell, 81, 1159-1170.
    • (1995) Cell , vol.81 , pp. 1159-1170
    • Hill, C.S.1    Wynne, J.2    Treisman, R.3
  • 286
    • 0029101360 scopus 로고
    • An essential role for Rho, Rac, and Cdc42 GTPases in cell cycle progression through G1
    • Olson, M. F., Ashworth, A. & Hall, A. (1995). An essential role for Rho, Rac, and Cdc42 GTPases in cell cycle progression through G1. Science, 269, 1270-1272.
    • (1995) Science , vol.269 , pp. 1270-1272
    • Olson, M.F.1    Ashworth, A.2    Hall, A.3
  • 287
    • 79951710855 scopus 로고    scopus 로고
    • A RhoA-derived peptide inhibits human immunodeficiency virus-1 entry in vitro
    • Maselko, M., Ward, C. & Pastey, M. (2011). A RhoA-derived peptide inhibits human immunodeficiency virus-1 entry in vitro. Curr. HIV Res. 9, 1-5.
    • (2011) Curr. HIV Res. , vol.9 , pp. 1-5
    • Maselko, M.1    Ward, C.2    Pastey, M.3
  • 288
    • 0035958898 scopus 로고    scopus 로고
    • Prenylated Rab acceptor protein is a receptor for prenylated small GTPases
    • Figueroa, C., Taylor, J. & Vojtek, A. B. (2001). Prenylated Rab acceptor protein is a receptor for prenylated small GTPases. J. Biol. Chem. 276, 28219-28225.
    • (2001) J. Biol. Chem. , vol.276 , pp. 28219-28225
    • Figueroa, C.1    Taylor, J.2    Vojtek, A.B.3
  • 291
    • 0030783121 scopus 로고    scopus 로고
    • Isolation and characterization of a dual prenylated Rab and VAMP2 receptor
    • DOI 10.1074/jbc.272.43.26991
    • Martincic, I., Peralta, M. E. & Ngsee, J. K. (1997). Isolation and characterization of a dual prenylated Rab and VAMP2 receptor. J. Biol. Chem. 272, 26991-26998. (Pubitemid 27452653)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.43 , pp. 26991-26998
    • Martincic, I.1    Peralta, M.E.2    Ngsee, J.K.3
  • 292
    • 0036133040 scopus 로고    scopus 로고
    • Envelope glycoprotein cytoplasmic domains from diverse lentiviruses interact with the prenylated rab acceptor
    • DOI 10.1128/JVI.76.1.327-337.2002
    • Evans, D. T., Tillman, K. C. & Desrosiers, R. C. (2002). Envelope glycoprotein cytoplasmic domains from diverse lentiviruses interact with the prenylated Rab acceptor. J. Virol. 76, 327-337. (Pubitemid 33139017)
    • (2002) Journal of Virology , vol.76 , Issue.1 , pp. 327-337
    • Evans, D.T.1    Tillman, K.C.2    Desrosiers, R.C.3
  • 293
    • 20044370465 scopus 로고    scopus 로고
    • PRA1 co-localizes with envelope but does not influence primate lentivirus production, infectivity or envelope incorporation
    • DOI 10.1099/vir.0.80873-0
    • Blancou, P., Evans, D. T. & Desrosiers, R. C. (2005). PRA1 co-localizes with envelope but does not influence primate lentivirus production, infectivity or envelope incorporation. J. Gen. Virol. 86, 1785-1790. (Pubitemid 40766891)
    • (2005) Journal of General Virology , vol.86 , Issue.6 , pp. 1785-1790
    • Blancou, P.1    Evans, D.T.2    Desrosiers, R.C.3
  • 294
    • 0037604497 scopus 로고    scopus 로고
    • Interactions of rotavirus VP4 spike protein with the endosomal protein Rab5 and the prenylated Rab acceptor PRA1
    • DOI 10.1128/JVI.77.12.7041-7047.2003
    • Enouf, V., Chwetzoff, S., Trugnan, G. & Cohen, J. (2003). Interactions of rotavirus VP4 spike protein with the endosomal protein Rab5 and the prenylated Rab acceptor PRA1. J. Virol. 77, 7041-7047. (Pubitemid 36666897)
    • (2003) Journal of Virology , vol.77 , Issue.12 , pp. 7041-7047
    • Enouf, V.1    Chwetzoff, S.2    Trugnan, G.3    Cohen, J.4
  • 295
    • 33645755879 scopus 로고    scopus 로고
    • Dissecting rotavirus particle-raft interaction with small interfering RNAs: Insights into rotavirus transit through the secretory pathway
    • Cuadras, M. A., Bordier, B. B., Zambrano, J. L., Ludert, J. E. & Greenberg, H. B. (2006). Dissecting rotavirus particle-raft interaction with small interfering RNAs: insights into rotavirus transit through the secretory pathway. J. Virol. 80, 3935-3946.
    • (2006) J. Virol. , vol.80 , pp. 3935-3946
    • Cuadras, M.A.1    Bordier, B.B.2    Zambrano, J.L.3    Ludert, J.E.4    Greenberg, H.B.5
  • 296
    • 33748340652 scopus 로고    scopus 로고
    • PRA1 promotes the intracellular trafficking and NF-κB signaling of EBV latent membrane protein 1
    • DOI 10.1038/sj.emboj.7601282, PII 7601282
    • Liu, H.-P., Wu, C.-C. & Chang, Y.-S. (2006). PRA1 promotes the intracellular trafficking and NF-kap-paB signaling of EBV latent membrane protein 1. EMBO J. 25, 4120-4130. (Pubitemid 44338752)
    • (2006) EMBO Journal , vol.25 , Issue.17 , pp. 4120-4130
    • Liu, H.-P.1    Wu, C.-C.2    Chang, Y.-S.3
  • 297
    • 33947429722 scopus 로고    scopus 로고
    • PRAF1: A Golgi complex transmembrane protein that interacts with viruses
    • DOI 10.1139/O06-176
    • Compton, S. L. & Behrend, E. N. (2006). PRAF1: a Golgi complex transmembrane protein that interacts with viruses. Biochem. Cell Biol. 84, 940-948. (Pubitemid 46450694)
    • (2006) Biochemistry and Cell Biology , vol.84 , Issue.6 , pp. 940-948
    • Compton, S.L.1    Behrend, E.N.2
  • 298
    • 33750350899 scopus 로고    scopus 로고
    • Luman/CREB3 induces transcription of the endoplasmic reticulum (ER) stress response protein herp through an ER stress response element
    • DOI 10.1128/MCB.01046-06
    • Liang, G., Audas, T. E., Li, Y., Cockram, G. P., Dean, J. D., Martyn, A. C. et al. (2006). Luman/CREB3 induces transcription of the endoplasmic reticulum (ER) stress response protein Herp through an ER stress response element. Mol. Cell. Biol. 26, 7999-8010. (Pubitemid 44630999)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.21 , pp. 7999-8010
    • Liang, G.1    Audas, T.E.2    Li, Y.3    Cockram, G.P.4    Dean, J.D.5    Martyn, A.C.6    Kokame, K.7    Lu, R.8
  • 301
    • 73949150062 scopus 로고    scopus 로고
    • Identification of the cellular prohibitin 1/prohibitin 2 heterodimer as an interaction partner of the C-terminal cytoplasmic domain of the HIV-1 glycopro-tein
    • Emerson, V., Holtkotte, D., Pfeiffer, T., Wang, I.-H., Schnölzer, M., Kempf, T. & Bosch, V. (2010). Identification of the cellular prohibitin 1/prohibitin 2 heterodimer as an interaction partner of the C-terminal cytoplasmic domain of the HIV-1 glycopro-tein. J. Virol. 84, 1355-1365.
    • (2010) J. Virol. , vol.84 , pp. 1355-1365
    • Emerson, V.1    Holtkotte, D.2    Pfeiffer, T.3    Wang, I.-H.4    Schnölzer, M.5    Kempf, T.6    Bosch, V.7
  • 302
    • 77956632914 scopus 로고    scopus 로고
    • The role of prohibitin in cell signaling
    • Mishra, S., Ande, S. R. & Nyomba, B. L. G. (2010). The role of prohibitin in cell signaling. FEBS J. 277, 3937-3946.
    • (2010) FEBS J. , vol.277 , pp. 3937-3946
    • Mishra, S.1    Ande, S.R.2    Nyomba, B.L.G.3
  • 303
    • 56349102165 scopus 로고    scopus 로고
    • Prohibitin function within mitochondria: Essential roles for cell proliferation and cristae morphogenesis
    • Merkwirth, C. & Langer, T. (2009). Prohibitin function within mitochondria: essential roles for cell proliferation and cristae morphogenesis. Biochim. Biophys. Acta, 1793, 27-32.
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 27-32
    • Merkwirth, C.1    Langer, T.2
  • 304
    • 23844462163 scopus 로고    scopus 로고
    • Flotillins and the PHB domain protein family: Rafts worms and anaesthetics
    • DOI 10.1111/j.1600-0854.2005.00318.x
    • Morrow I. C. & Parton, R. G. (2005). Flotillins and the PHB domain protein family: rafts, worms and anaesthetics. Traffic 6, 725-740. (Pubitemid 41179406)
    • (2005) Traffic , vol.6 , Issue.9 , pp. 725-740
    • Morrow, I.C.1    Parton, R.G.2
  • 305
    • 74549167295 scopus 로고    scopus 로고
    • A method for solution NMR structural studies of large integral membrane proteins: Reverse micelle encapsulation
    • Kielec, J. M., Valentine, K. G. & Wand, A. J. (2010). A method for solution NMR structural studies of large integral membrane proteins: reverse micelle encapsulation. Biochim. Biophys. Acta, 1798, 150-160.
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 150-160
    • Kielec, J.M.1    Valentine, K.G.2    Wand, A.J.3
  • 306
    • 78649684704 scopus 로고    scopus 로고
    • Present and future of membrane protein structure determination by electron crystallography
    • Ubarretxena-Belandia, I. & Stokes, D. L. (2010). Present and future of membrane protein structure determination by electron crystallography. Adv. Protein Chem. Struct. Biol. 81, 33-60.
    • (2010) Adv. Protein Chem. Struct. Biol. , vol.81 , pp. 33-60
    • Ubarretxena-Belandia, I.1    Stokes, D.L.2
  • 307
    • 79954454533 scopus 로고    scopus 로고
    • Structural physiology based on electron crystallography
    • [Electronic publication ahead of print]
    • Fujiyoshi, Y. (2011). Structural physiology based on electron crystallography. Protein Sci. [Electronic publication ahead of print].
    • (2011) Protein Sci
    • Fujiyoshi, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.