메뉴 건너뛰기




Volumn 5, Issue JUN, 2014, Pages

New insights into retroviral Gag-Gag and Gag-membrane interactions

Author keywords

Deltaretrovirus; Lentivirus; Multimerization; Oligomerization; Plasma membrane; Spectroscopy

Indexed keywords

GAG PROTEIN; MEMBRANE LIPID; PHOSPHOLIPID; POLYPROTEIN; SUPPRESSOR OF CYTOKINE SIGNALING 1;

EID: 84904887065     PISSN: None     EISSN: 1664302X     Source Type: Journal    
DOI: 10.3389/fmicb.2014.00302     Document Type: Short Survey
Times cited : (32)

References (77)
  • 1
    • 0034088332 scopus 로고    scopus 로고
    • Efficient particle production by minimal Gag constructs which retain the carboxy-terminal domain of human immunodeficiency virus type 1 capsid-p2 and a late assembly domain
    • doi: 10.1128/JVI.74.12.5395-5402.2000
    • Accola, M. A., Strack, B., and Gottlinger, H. G. (2000). Efficient particle production by minimal Gag constructs which retain the carboxy-terminal domain of human immunodeficiency virus type 1 capsid-p2 and a late assembly domain. J. Virol. 74, 5395-5402. doi: 10.1128/JVI.74.12.5395-5402.2000
    • (2000) J. Virol. , vol.74 , pp. 5395-5402
    • Accola, M.A.1    Strack, B.2    Gottlinger, H.G.3
  • 2
    • 27144548783 scopus 로고    scopus 로고
    • The retroviral capsid domain dictates virion size, morphology, and coassembly of gag into virus-like particles
    • doi: 10.1128/JVI.79.21.13463-13472.2005
    • Ako-Adjei, D., Johnson, M. C., and Vogt, V. M. (2005). The retroviral capsid domain dictates virion size, morphology, and coassembly of gag into virus-like particles. J. Virol. 79, 13463-13472. doi: 10.1128/JVI.79.21.13463-13472.2005
    • (2005) J. Virol. , vol.79 , pp. 13463-13472
    • Ako-Adjei, D.1    Johnson, M.C.2    Vogt, V.M.3
  • 3
    • 27744515031 scopus 로고    scopus 로고
    • Analysis of human immunodeficiency virus type 1 Gag dimerization-induced assembly
    • doi: 10.1128/JVI.79.23.14498-14506.2005
    • Alfadhli, A., Dhenub, T. C., Still, A., and Barklis, E. (2005). Analysis of human immunodeficiency virus type 1 Gag dimerization-induced assembly. J. Virol. 79, 14498-14506. doi: 10.1128/JVI.79.23.14498-14506.2005
    • (2005) J. Virol. , vol.79 , pp. 14498-14506
    • Alfadhli, A.1    Dhenub, T.C.2    Still, A.3    Barklis, E.4
  • 4
    • 84861393911 scopus 로고    scopus 로고
    • Budding of retroviruses utilizing divergent L domains requires nucleocapsid
    • doi: 10.1128/JVI.07105-11
    • Bello, N. F., Dussupt, V., Sette, P., Rudd, V., Nagashima, K., Bibollet-Ruche, F.,et al. (2012). Budding of retroviruses utilizing divergent L domains requires nucleocapsid. J. Virol. 86, 4182-4193. doi: 10.1128/JVI.07105-11
    • (2012) J. Virol. , vol.86 , pp. 4182-4193
    • Bello, N.F.1    Dussupt, V.2    Sette, P.3    Rudd, V.4    Nagashima, K.5    Bibollet-Ruche, F.6
  • 5
    • 0031680643 scopus 로고    scopus 로고
    • The C-terminal half of the human immunodeficiency virus type 1 Gag precursor is sufficient for efficient particle assembly
    • Borsetti, A., Ohagen, A., and Gottlinger, H. G. (1998). The C-terminal half of the human immunodeficiency virus type 1 Gag precursor is sufficient for efficient particle assembly. J. Virol. 72, 9313-9317.
    • (1998) J. Virol. , vol.72 , pp. 9313-9317
    • Borsetti, A.1    Ohagen, A.2    Gottlinger, H.G.3
  • 6
    • 39349097864 scopus 로고    scopus 로고
    • Identification of host proteins required for HIV infection through a functional genomic screen
    • doi: 10.1126/science.1152725
    • Brass, A. L., Dykxhoorn, D. M., Benita, Y., Yan, N., Engelman, A., Xavier, R. J.,et al. (2008). Identification of host proteins required for HIV infection through a functional genomic screen. Science 319, 921-926. doi: 10.1126/science.1152725
    • (2008) Science , vol.319 , pp. 921-926
    • Brass, A.L.1    Dykxhoorn, D.M.2    Benita, Y.3    Yan, N.4    Engelman, A.5    Xavier, R.J.6
  • 7
    • 80051713783 scopus 로고    scopus 로고
    • The molecular architecture of HIV
    • doi: 10.1016/j.jmb.2011.04.021
    • Briggs, J. A., and Krausslich, H. G. (2011). The molecular architecture of HIV. J. Mol. Biol. 410, 491-500. doi: 10.1016/j.jmb.2011.04.021
    • (2011) J. Mol. Biol. , vol.410 , pp. 491-500
    • Briggs, J.A.1    Krausslich, H.G.2
  • 9
    • 0025176624 scopus 로고
    • Myristoylation-dependent replication and assembly of human immunodeficiency virus 1
    • doi: 10.1073/pnas.87.2.523
    • Bryant, M., and Ratner, L. (1990). Myristoylation-dependent replication and assembly of human immunodeficiency virus 1. Proc. Natl. Acad. Sci. U.S.A. 87, 523-527. doi: 10.1073/pnas.87.2.523
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 523-527
    • Bryant, M.1    Ratner, L.2
  • 10
    • 80054992503 scopus 로고    scopus 로고
    • Rous sarcoma virus gag has no specific requirement for phosphatidylinositol-(4,5)-bisphosphate for plasma membrane association in vivo or for liposome interaction in vitro
    • doi: 10.1128/JVI.00760-11
    • Chan, J., Dick, R. A., and Vogt, V. M. (2011). Rous sarcoma virus gag has no specific requirement for phosphatidylinositol-(4,5)-bisphosphate for plasma membrane association in vivo or for liposome interaction in vitro. J. Virol. 85, 10851-10860. doi: 10.1128/JVI.00760-11
    • (2011) J. Virol. , vol.85 , pp. 10851-10860
    • Chan, J.1    Dick, R.A.2    Vogt, V.M.3
  • 11
    • 65549100184 scopus 로고    scopus 로고
    • Fluorescence fluctuation spectroscopy on viral-like particles reveals variable gag stoichiometry
    • doi: 10.1016/j.bpj.2008.10.067
    • Chen, Y., Wu, B., Musier-Forsyth, K., Mansky, L. M., and Mueller, J. D. (2009). Fluorescence fluctuation spectroscopy on viral-like particles reveals variable gag stoichiometry. Biophys. J. 96, 1961-1969. doi: 10.1016/j.bpj.2008.10.067
    • (2009) Biophys. J. , vol.96 , pp. 1961-1969
    • Chen, Y.1    Wu, B.2    Musier-Forsyth, K.3    Mansky, L.M.4    Mueller, J.D.5
  • 12
    • 39749170507 scopus 로고    scopus 로고
    • Interaction between the human immunodeficiency virus type 1 Gag matrix domain and phosphatidylinositol-(4,5)-bisphosphate is essential for efficient gag membrane binding
    • doi: 10.1128/JVI.01614-07
    • Chukkapalli, V., Hogue, I. B., Boyko, V., Hu, W. S., and Ono, A. (2008). Interaction between the human immunodeficiency virus type 1 Gag matrix domain and phosphatidylinositol-(4,5)-bisphosphate is essential for efficient gag membrane binding. J. Virol. 82, 2405-2417. doi: 10.1128/JVI.01614-07
    • (2008) J. Virol. , vol.82 , pp. 2405-2417
    • Chukkapalli, V.1    Hogue, I.B.2    Boyko, V.3    Hu, W.S.4    Ono, A.5
  • 13
    • 80051718223 scopus 로고    scopus 로고
    • Molecular determinants that regulate plasma membrane association of HIV-1 Gag
    • doi: 10.1016/j.jmb.2011.04.015
    • Chukkapalli, V., and Ono, A. (2011). Molecular determinants that regulate plasma membrane association of HIV-1 Gag. J. Mol. Biol. 410, 512-524. doi: 10.1016/j.jmb.2011.04.015
    • (2011) J. Mol. Biol. , vol.410 , pp. 512-524
    • Chukkapalli, V.1    Ono, A.2
  • 14
    • 0034011267 scopus 로고    scopus 로고
    • Basic residues in human immunodeficiency virus type 1 nucleocapsid promote virion assembly via interaction with RNA
    • doi: 10.1128/JVI.74.7.3046-3057.2000
    • Cimarelli, A., Sandin, S., Hoglund, S., and Luban, J. (2000). Basic residues in human immunodeficiency virus type 1 nucleocapsid promote virion assembly via interaction with RNA. J. Virol. 74, 3046-3057. doi: 10.1128/JVI.74.7.3046-3057.2000
    • (2000) J. Virol. , vol.74 , pp. 3046-3057
    • Cimarelli, A.1    Sandin, S.2    Hoglund, S.3    Luban, J.4
  • 15
    • 34249937903 scopus 로고    scopus 로고
    • Electrostatic interactions drive membrane association of the human immunodeficiency virus type 1 Gag MA domain
    • doi: 10.1128/JVI.02757-06
    • Dalton, A. K., Ako-Adjei, D., Murray, P. S., Murray, D., and Vogt, V. M. (2007). Electrostatic interactions drive membrane association of the human immunodeficiency virus type 1 Gag MA domain. J. Virol. 81, 6434-6445. doi: 10.1128/JVI.02757-06
    • (2007) J. Virol. , vol.81 , pp. 6434-6445
    • Dalton, A.K.1    Ako-Adjei, D.2    Murray, P.S.3    Murray, D.4    Vogt, V.M.5
  • 16
    • 79251596756 scopus 로고    scopus 로고
    • HIV-1 Gag extension: conformational changes require simultaneous interaction with membrane and nucleic acid
    • doi: 10.1016/j.jmb.2010.11.051
    • Datta, S. A., Heinrich, F., Raghunandan, S., Krueger, S., Curtis, J. E., Rein, A.,et al. (2011). HIV-1 Gag extension: conformational changes require simultaneous interaction with membrane and nucleic acid. J. Mol. Biol. 406, 205-214. doi: 10.1016/j.jmb.2010.11.051
    • (2011) J. Mol. Biol. , vol.406 , pp. 205-214
    • Datta, S.A.1    Heinrich, F.2    Raghunandan, S.3    Krueger, S.4    Curtis, J.E.5    Rein, A.6
  • 17
    • 33845676742 scopus 로고    scopus 로고
    • Interactions between HIV-1 Gag molecules in solution: an inositol phosphate-mediated switch
    • doi: 10.1016/j.jmb.2006.10.072
    • Datta, S. A., Zhao, Z., Clark, P. K., Tarasov, S., Alexandratos, J. N., Campbell, S. J.,et al. (2007). Interactions between HIV-1 Gag molecules in solution: an inositol phosphate-mediated switch. J. Mol. Biol. 365, 799-811. doi: 10.1016/j.jmb.2006.10.072
    • (2007) J. Mol. Biol. , vol.365 , pp. 799-811
    • Datta, S.A.1    Zhao, Z.2    Clark, P.K.3    Tarasov, S.4    Alexandratos, J.N.5    Campbell, S.J.6
  • 18
    • 84869217910 scopus 로고    scopus 로고
    • HIV-1 Gag protein can sense the cholesterol and acyl chain environment in model membranes
    • doi: 10.1073/pnas.1209408109
    • Dick, R. A., Goh, S. L., Feigenson, G. W., and Vogt, V. M. (2012). HIV-1 Gag protein can sense the cholesterol and acyl chain environment in model membranes. Proc. Natl. Acad. Sci. U.S.A. 109, 18761-18766. doi: 10.1073/pnas.1209408109
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 18761-18766
    • Dick, R.A.1    Goh, S.L.2    Feigenson, G.W.3    Vogt, V.M.4
  • 19
    • 0027997831 scopus 로고
    • Functional domains of the capsid protein of human immunodeficiency virus type 1
    • Dorfman, T., Bukovsky, A., Ohagen, A., Hoglund, S., and Gottlinger, H. G. (1994). Functional domains of the capsid protein of human immunodeficiency virus type 1. J. Virol. 68, 8180-8187.
    • (1994) J. Virol. , vol.68 , pp. 8180-8187
    • Dorfman, T.1    Bukovsky, A.2    Ohagen, A.3    Hoglund, S.4    Gottlinger, H.G.5
  • 20
    • 79551702980 scopus 로고    scopus 로고
    • Basic residues in the nucleocapsid domain of Gag are critical for late events of HIV-1 budding
    • doi: 10.1128/JVI.01562-10
    • Dussupt, V., Sette, P., Bello, N. F., Javid, M. P., Nagashima, K., and Bouamr, F. (2011). Basic residues in the nucleocapsid domain of Gag are critical for late events of HIV-1 budding. J. Virol. 85, 2304-2315. doi: 10.1128/JVI.01562-10
    • (2011) J. Virol. , vol.85 , pp. 2304-2315
    • Dussupt, V.1    Sette, P.2    Bello, N.F.3    Javid, M.P.4    Nagashima, K.5    Bouamr, F.6
  • 21
    • 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., and Cohen, E. A. (2007). Productive human immunodeficiency virus type 1 assembly takes place at the plasma membrane. J. Virol. 81, 7476-7490. doi: 10.1128/JVI.00308-07
    • (2007) J. Virol. , vol.81 , pp. 7476-7490
    • Finzi, A.1    Orthwein, A.2    Mercier, J.3    Cohen, E.A.4
  • 22
    • 84876323879 scopus 로고    scopus 로고
    • Major histocompatibility complex class-II molecules promote targeting of human immunodeficiency virus type 1 virions in late endosomes by enhancing internalization of nascent particles from the plasma membrane
    • doi: 10.1111/cmi.12074
    • Finzi, A., Perlman, M., Bourgeois-Daigneault, M. C., Thibodeau, J., and Cohen, E. A. (2013). Major histocompatibility complex class-II molecules promote targeting of human immunodeficiency virus type 1 virions in late endosomes by enhancing internalization of nascent particles from the plasma membrane. Cell. Microbiol. 15, 809-822. doi: 10.1111/cmi.12074
    • (2013) Cell. Microbiol. , vol.15 , pp. 809-822
    • Finzi, A.1    Perlman, M.2    Bourgeois-Daigneault, M.C.3    Thibodeau, J.4    Cohen, E.A.5
  • 23
    • 84895925747 scopus 로고    scopus 로고
    • Interrelationship between cytoplasmic retroviral Gag concentration and Gag-membrane association
    • doi: 10.1016/j.jmb.2013.11.025
    • Fogarty, K. H., Berk, S., Grigsby, I. F., Chen, Y., Mansky, L. M., and Mueller, J. D. (2013). Interrelationship between cytoplasmic retroviral Gag concentration and Gag-membrane association. J. Mol. Biol. 426, 1611-1624. doi: 10.1016/j.jmb.2013.11.025
    • (2013) J. Mol. Biol. , vol.426 , pp. 1611-1624
    • Fogarty, K.H.1    Berk, S.2    Grigsby, I.F.3    Chen, Y.4    Mansky, L.M.5    Mueller, J.D.6
  • 24
    • 79953896583 scopus 로고    scopus 로고
    • Characterization of cytoplasmic Gag-gag interactions by dual-color z-scan fluorescence fluctuation spectroscopy
    • doi: 10.1016/j.bpj.2011.02.008
    • Fogarty, K. H., Chen, Y., Grigsby, I. F., Macdonald, P. J., Smith, E. M., Johnson, J. L.,et al. (2011). Characterization of cytoplasmic Gag-gag interactions by dual-color z-scan fluorescence fluctuation spectroscopy. Biophys. J. 100, 1587-1595. doi: 10.1016/j.bpj.2011.02.008
    • (2011) Biophys. J. , vol.100 , pp. 1587-1595
    • Fogarty, K.H.1    Chen, Y.2    Grigsby, I.F.3    Macdonald, P.J.4    Smith, E.M.5    Johnson, J.L.6
  • 25
    • 0030693391 scopus 로고    scopus 로고
    • Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein
    • doi: 10.1126/science.278.5339.849
    • Gamble, T. R., Yoo, S., Vajdos, F. F., von Schwedler, U. K., Worthylake, D. K., Wang, H.,et al. (1997). Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein. Science 278, 849-853. doi: 10.1126/science.278.5339.849
    • (1997) Science , vol.278 , pp. 849-853
    • Gamble, T.R.1    Yoo, S.2    Vajdos, F.F.3    von Schwedler, U.K.4    Worthylake, D.K.5    Wang, H.6
  • 26
    • 0032930797 scopus 로고    scopus 로고
    • Assembly and analysis of conical models for the HIV-1 core
    • doi: 10.1126/science.283.5398.80
    • Ganser, B. K., Li, S., Klishko, V. Y., Finch, J. T., and Sundquist, W. I.(1999). Assembly and analysis of conical models for the HIV-1 core. Science 283, 80-83. doi: 10.1126/science.283.5398.80
    • (1999) Science , vol.283 , pp. 80-83
    • Ganser, B.K.1    Li, S.2    Klishko, V.Y.3    Finch, J.T.4    Sundquist, W.I.5
  • 27
    • 0024110320 scopus 로고
    • Point mutants of Moloney murine leukemia virus that fail to package viral RNA: evidence for specific RNA recognition by a "zinc finger-like" protein sequence
    • doi: 10.1073/pnas.85.22.8420
    • Gorelick, R. J., Henderson, L. E., Hanser, J. P., and Rein, A. (1988). Point mutants of Moloney murine leukemia virus that fail to package viral RNA: evidence for specific RNA recognition by a "zinc finger-like" protein sequence. Proc. Natl. Acad. Sci. U.S.A. 85, 8420-8424. doi: 10.1073/pnas.85.22.8420
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 8420-8424
    • Gorelick, R.J.1    Henderson, L.E.2    Hanser, J.P.3    Rein, A.4
  • 28
    • 42949175719 scopus 로고    scopus 로고
    • Real-time visualization of HIV-1 GAG trafficking in infected macrophages
    • doi: 10.1371/journal.ppat.1000015
    • Gousset, K., Ablan, S. D., Coren, L. V., Ono, A., Soheilian, F., Nagashima, K.,et al. (2008). Real-time visualization of HIV-1 GAG trafficking in infected macrophages. PLoS Pathog. 4:e1000015. doi: 10.1371/journal.ppat.1000015
    • (2008) PLoS Pathog , vol.4
    • Gousset, K.1    Ablan, S.D.2    Coren, L.V.3    Ono, A.4    Soheilian, F.5    Nagashima, K.6
  • 29
    • 72849142782 scopus 로고    scopus 로고
    • Targeting of murine leukemia virus gag to the plasma membrane is mediated by PI(4,5)P2/PS and a polybasic region in the matrix
    • doi: 10.1128/JVI.01134-09
    • Hamard-Peron, E., Juillard, F., Saad, J. S., Roy, C., Roingeard, P., Summers, M. F.,et al. (2010). Targeting of murine leukemia virus gag to the plasma membrane is mediated by PI(4,5)P2/PS and a polybasic region in the matrix. J. Virol. 84, 503-515. doi: 10.1128/JVI.01134-09
    • (2010) J. Virol. , vol.84 , pp. 503-515
    • Hamard-Peron, E.1    Juillard, F.2    Saad, J.S.3    Roy, C.4    Roingeard, P.5    Summers, M.F.6
  • 30
    • 0026515142 scopus 로고
    • Gag proteins of the highly replicative MN strain of human immunodeficiency virus type 1: posttranslational modifications, proteolytic processings, and complete amino acid sequences
    • Henderson, L. E., Bowers, M. A., Sowder, R. C. II, Serabyn, S. A., Johnson, D. G., Bess, J. W.,et al. (1992). Gag proteins of the highly replicative MN strain of human immunodeficiency virus type 1: posttranslational modifications, proteolytic processings, and complete amino acid sequences. J. Virol. 66, 1856-1865.
    • (1992) J. Virol. , vol.66 , pp. 1856-1865
    • Henderson, L.E.1    Bowers, M.A.2    Sowder R.C.II Serabyn, S.A.3    Johnson, D.G.4    Bess, J.W.5
  • 31
    • 50349090965 scopus 로고    scopus 로고
    • Intracellular transport and kinesin superfamily proteins, KIFs: structure, function, and dynamics
    • doi: 10.1152/physrev.00023.2007
    • Hirokawa, N., and Noda, Y. (2008). Intracellular transport and kinesin superfamily proteins, KIFs: structure, function, and dynamics. Physiol. Rev. 88, 1089-1118. doi: 10.1152/physrev.00023.2007
    • (2008) Physiol. Rev. , vol.88 , pp. 1089-1118
    • Hirokawa, N.1    Noda, Y.2
  • 32
    • 67650439272 scopus 로고    scopus 로고
    • Quantitative fluorescence resonance energy transfer microscopy analysis of the human immunodeficiency virus type 1 Gag-Gag interaction: relative contributions of the CA and NC domains and membrane binding
    • doi: 10.1128/JVI.02545-08
    • Hogue, I. B., Hoppe, A., and Ono, A. (2009). Quantitative fluorescence resonance energy transfer microscopy analysis of the human immunodeficiency virus type 1 Gag-Gag interaction: relative contributions of the CA and NC domains and membrane binding. J. Virol. 83, 7322-7336. doi: 10.1128/JVI.02545-08
    • (2009) J. Virol. , vol.83 , pp. 7322-7336
    • Hogue, I.B.1    Hoppe, A.2    Ono, A.3
  • 33
    • 79952850453 scopus 로고    scopus 로고
    • Gag localization and virus-like particle release mediated by the matrix domain of human T-lymphotropic virus type 1 Gag are less dependent on phosphatidylinositol-(4,5)-bisphosphate than those mediated by the matrix domain of HIV-1 Gag
    • doi: 10.1128/JVI.02383-10
    • Inlora, J., Chukkapalli, V., Derse, D., and Ono, A. (2011). Gag localization and virus-like particle release mediated by the matrix domain of human T-lymphotropic virus type 1 Gag are less dependent on phosphatidylinositol-(4,5)-bisphosphate than those mediated by the matrix domain of HIV-1 Gag. J. Virol. 85, 3802-3810. doi: 10.1128/JVI.02383-10
    • (2011) J. Virol. , vol.85 , pp. 3802-3810
    • Inlora, J.1    Chukkapalli, V.2    Derse, D.3    Ono, A.4
  • 34
    • 33845493481 scopus 로고    scopus 로고
    • Plasma membrane is the site of productive HIV-1 particle assembly
    • doi: 10.1371/journal.pbio.0040435
    • Jouvenet, N., Neil, S. J., Bess, C., Johnson, M. C., Virgen, C. A., Simon, S. M.,et al. (2006). Plasma membrane is the site of productive HIV-1 particle assembly. PLoS Biol. 4:e435. doi: 10.1371/journal.pbio.0040435
    • (2006) PLoS Biol , vol.4
    • Jouvenet, N.1    Neil, S.J.2    Bess, C.3    Johnson, M.C.4    Virgen, C.A.5    Simon, S.M.6
  • 35
    • 73149122533 scopus 로고    scopus 로고
    • Imaging the interaction of HIV-1 genomes and Gag during assembly of individual viral particles
    • doi: 10.1073/pnas.0907364106
    • Jouvenet, N., Simon, S. M., and Bieniasz, P. D. (2009). Imaging the interaction of HIV-1 genomes and Gag during assembly of individual viral particles. Proc. Natl. Acad. Sci. U.S.A. 106, 19114-19119. doi: 10.1073/pnas.0907364106
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 19114-19119
    • Jouvenet, N.1    Simon, S.M.2    Bieniasz, P.D.3
  • 36
    • 0036196932 scopus 로고    scopus 로고
    • Role of RNA in facilitating Gag/Gag-Pol interaction
    • doi: 10.1128/JVI.76.8.4131-4137.2002
    • Khorchid, A., Halwani, R., Wainberg, M. A., and Kleiman, L. (2002). Role of RNA in facilitating Gag/Gag-Pol interaction. J. Virol. 76, 4131-4137. doi: 10.1128/JVI.76.8.4131-4137.2002
    • (2002) J. Virol. , vol.76 , pp. 4131-4137
    • Khorchid, A.1    Halwani, R.2    Wainberg, M.A.3    Kleiman, L.4
  • 37
    • 52949130695 scopus 로고    scopus 로고
    • Global analysis of host-pathogen interactions that regulate early-stage HIV-1 replication
    • doi: 10.1016/j.cell.2008.07.032
    • Konig, R., Zhou, Y., Elleder, D., Diamond, T. L., Bonamy, G. M., Irelan, J. T.,et al. (2008). Global analysis of host-pathogen interactions that regulate early-stage HIV-1 replication. Cell 135, 49-60. doi: 10.1016/j.cell.2008.07.032
    • (2008) Cell , vol.135 , pp. 49-60
    • Konig, R.1    Zhou, Y.2    Elleder, D.3    Diamond, T.L.4    Bonamy, G.M.5    Irelan, J.T.6
  • 38
    • 0029013585 scopus 로고
    • The spacer peptide between human immunodeficiency virus capsid and nucleocapsid proteins is essential for ordered assembly and viral infectivity
    • Krausslich, H. G., Facke, M., Heuser, A. M., Konvalinka, J., and Zentgraf, H. (1995). The spacer peptide between human immunodeficiency virus capsid and nucleocapsid proteins is essential for ordered assembly and viral infectivity. J. Virol. 69, 3407-3419.
    • (1995) J. Virol. , vol.69 , pp. 3407-3419
    • Krausslich, H.G.1    Facke, M.2    Heuser, A.M.3    Konvalinka, J.4    Zentgraf, H.5
  • 39
    • 79251506313 scopus 로고    scopus 로고
    • Analysis of the initiating events in HIV-1 particle assembly and genome packaging
    • doi: 10.1371/journal.ppat.1001200
    • Kutluay, S. B., and Bieniasz, P. D. (2010). Analysis of the initiating events in HIV-1 particle assembly and genome packaging. PLoS Pathog. 6:e1001200. doi: 10.1371/journal.ppat.1001200
    • (2010) PLoS Pathog , vol.6
    • Kutluay, S.B.1    Bieniasz, P.D.2
  • 40
    • 36349029236 scopus 로고    scopus 로고
    • Myristoylation is required for human immunodeficiency virus type 1 Gag-Gag multimerization in mammalian cells
    • doi: 10.1128/JVI.01280-07
    • Li, H., Dou, J., Ding, L., and Spearman, P. (2007). Myristoylation is required for human immunodeficiency virus type 1 Gag-Gag multimerization in mammalian cells. J. Virol. 81, 12899-12910. doi: 10.1128/JVI.01280-07
    • (2007) J. Virol. , vol.81 , pp. 12899-12910
    • Li, H.1    Dou, J.2    Ding, L.3    Spearman, P.4
  • 41
    • 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., and Resh, M. D. (2001). Multimerization of human immunodeficiency virus type 1 Gag promotes its localization to barges, raft-like membrane microdomains. J. Virol. 75, 7913-7924. doi: 10.1128/JVI.75.17.7913-7924.2001
    • (2001) J. Virol. , vol.75 , pp. 7913-7924
    • Lindwasser, O.W.1    Resh, M.D.2
  • 42
    • 70350172934 scopus 로고    scopus 로고
    • Lipid rafts as functional heterogeneity in cell membranes
    • doi: 10.1042/BST0370955
    • Lingwood, D., Kaiser, H. J., Levental, I., and Simons, K. (2009). Lipid rafts as functional heterogeneity in cell membranes. Biochem. Soc. Trans. 37, 955-960. doi: 10.1042/BST0370955
    • (2009) Biochem. Soc. Trans. , vol.37 , pp. 955-960
    • Lingwood, D.1    Kaiser, H.J.2    Levental, I.3    Simons, K.4
  • 43
    • 7644240076 scopus 로고    scopus 로고
    • Role of murine leukemia virus nucleocapsid protein in virus assembly
    • doi: 10.1128/JVI.78.22.12378-12385.2004
    • Muriaux, D., Costes, S., Nagashima, K., Mirro, J., Cho, E., Lockett, S.,et al. (2004). Role of murine leukemia virus nucleocapsid protein in virus assembly. J. Virol. 78, 12378-12385. doi: 10.1128/JVI.78.22.12378-12385.2004
    • (2004) J. Virol. , vol.78 , pp. 12378-12385
    • Muriaux, D.1    Costes, S.2    Nagashima, K.3    Mirro, J.4    Cho, E.5    Lockett, S.6
  • 44
    • 26444444082 scopus 로고    scopus 로고
    • Retroviral matrix domains share electrostatic homology: models for membrane binding function throughout the viral life cycle
    • doi: 10.1016/j.str.2005.07.010
    • Murray, P. S., Li, Z., Wang, J., Tang, C. L., Honig, B., and Murray, D. (2005). Retroviral matrix domains share electrostatic homology: models for membrane binding function throughout the viral life cycle. Structure 13, 1521-1531. doi: 10.1016/j.str.2005.07.010
    • (2005) Structure , vol.13 , pp. 1521-1531
    • Murray, P.S.1    Li, Z.2    Wang, J.3    Tang, C.L.4    Honig, B.5    Murray, D.6
  • 45
    • 84874678574 scopus 로고    scopus 로고
    • Alterations in the MA and NC domains modulate phosphoinositide-dependent plasma membrane localization of the Rous sarcoma virus Gag protein
    • doi: 10.1128/JVI.03059-12
    • Nadaraia-Hoke, S., Bann, D. V., Lochmann, T. L., Gudleski-O'regan, N., and Parent, L. J. (2013). Alterations in the MA and NC domains modulate phosphoinositide-dependent plasma membrane localization of the Rous sarcoma virus Gag protein. J. Virol. 87, 3609-3615. doi: 10.1128/JVI.03059-12
    • (2013) J. Virol. , vol.87 , pp. 3609-3615
    • Nadaraia-Hoke, S.1    Bann, D.V.2    Lochmann, T.L.3    Gudleski-O'regan, N.4    Parent, L.J.5
  • 46
    • 34548021883 scopus 로고    scopus 로고
    • Retroviral proteins that interact with the host cell cytoskeleton
    • doi: 10.1016/j.coi.2007.07.003
    • Naghavi, M. H., and Goff, S. P. (2007). Retroviral proteins that interact with the host cell cytoskeleton. Curr. Opin. Immunol. 19, 402-407. doi: 10.1016/j.coi.2007.07.003
    • (2007) Curr. Opin. Immunol. , vol.19 , pp. 402-407
    • Naghavi, M.H.1    Goff, S.P.2
  • 47
    • 0037331514 scopus 로고    scopus 로고
    • Involvement of macrophage mannose receptor in the binding and transmission of HIV by macrophages
    • doi: 10.1002/immu.200310024
    • Nguyen, D. G., and Hildreth, J. E. (2003). Involvement of macrophage mannose receptor in the binding and transmission of HIV by macrophages. Eur. J. Immunol. 33, 483-493. doi: 10.1002/immu.200310024
    • (2003) Eur. J. Immunol. , vol.33 , pp. 483-493
    • Nguyen, D.G.1    Hildreth, J.E.2
  • 48
    • 64049094283 scopus 로고    scopus 로고
    • Requirement for microtubule integrity in the SOCS1-mediated intracellular dynamics of HIV-1 Gag
    • doi: 10.1016/j.febslet.2009.03.041
    • Nishi, M., Ryo, A., Tsurutani, N., Ohba, K., Sawasaki, T., Morishita, R.,et al. (2009). Requirement for microtubule integrity in the SOCS1-mediated intracellular dynamics of HIV-1 Gag. FEBS Lett. 583, 1243-1250. doi: 10.1016/j.febslet.2009.03.041
    • (2009) FEBS Lett. , vol.583 , pp. 1243-1250
    • Nishi, M.1    Ryo, A.2    Tsurutani, N.3    Ohba, K.4    Sawasaki, T.5    Morishita, R.6
  • 49
    • 0346937486 scopus 로고    scopus 로고
    • HIV-1 egress is gated through late endosomal membranes
    • doi: 10.1046/j.1600-0854.2003.00145.x
    • Nydegger, S., Foti, M., Derdowski, A., Spearman, P., and Thali, M. (2003). HIV-1 egress is gated through late endosomal membranes. Traffic 4, 902-910. doi: 10.1046/j.1600-0854.2003.00145.x
    • (2003) Traffic , vol.4 , pp. 902-910
    • Nydegger, S.1    Foti, M.2    Derdowski, A.3    Spearman, P.4    Thali, M.5
  • 50
    • 84869205288 scopus 로고    scopus 로고
    • Functional redundancy in HIV-1 viral particle assembly
    • doi: 10.1128/JVI.06287-11
    • O'Carroll, I. P., Crist, R. M., Mirro, J., Harvin, D., Soheilian, F., Kamata, A.,et al. (2012). Functional redundancy in HIV-1 viral particle assembly. J. Virol. 86, 12991-12996. doi: 10.1128/JVI.06287-11
    • (2012) J. Virol. , vol.86 , pp. 12991-12996
    • O'Carroll, I.P.1    Crist, R.M.2    Mirro, J.3    Harvin, D.4    Soheilian, F.5    Kamata, A.6
  • 51
    • 85027932076 scopus 로고    scopus 로고
    • Elements in HIV-1 Gag contributing to virus particle assembly
    • doi: 10.1016/j.virusres.2012.10.016
    • O'Carroll, I. P., Soheilian, F., Kamata, A., Nagashima, K., and Rein, A. (2013). Elements in HIV-1 Gag contributing to virus particle assembly. Virus Res. 171, 341-345. doi: 10.1016/j.virusres.2012.10.016
    • (2013) Virus Res. , vol.171 , pp. 341-345
    • O'Carroll, I.P.1    Soheilian, F.2    Kamata, A.3    Nagashima, K.4    Rein, A.5
  • 52
    • 70350113492 scopus 로고    scopus 로고
    • HIV-1 assembly at the plasma membrane: Gag trafficking and localization
    • doi: 10.2217/fvl.09.4
    • Ono, A. (2009). HIV-1 assembly at the plasma membrane: Gag trafficking and localization. Future Virol. 4, 241-257. doi: 10.2217/fvl.09.4
    • (2009) Future Virol. , vol.4 , pp. 241-257
    • Ono, A.1
  • 53
    • 6944255361 scopus 로고    scopus 로고
    • Phosphatidylinositol (4,5) bisphosphate regulates HIV-1 Gag targeting to the plasma membrane
    • doi: 10.1073/pnas.0405596101
    • Ono, A., Ablan, S. D., Lockett, S. J., Nagashima, K., and Freed, E. O. (2004). Phosphatidylinositol (4,5) bisphosphate regulates HIV-1 Gag targeting to the plasma membrane. Proc. Natl. Acad. Sci. U.S.A. 101, 14889-14894. doi: 10.1073/pnas.0405596101
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 14889-14894
    • Ono, A.1    Ablan, S.D.2    Lockett, S.J.3    Nagashima, K.4    Freed, E.O.5
  • 54
    • 0033999270 scopus 로고    scopus 로고
    • Role of the Gag matrix domain in targeting human immunodeficiency virus type 1 assembly
    • doi: 10.1128/JVI.74.6.2855-2866.2000
    • Ono, A., Orenstein, J. M., and Freed, E. O. (2000). Role of the Gag matrix domain in targeting human immunodeficiency virus type 1 assembly. J. Virol. 74, 2855-2866. doi: 10.1128/JVI.74.6.2855-2866.2000
    • (2000) J. Virol. , vol.74 , pp. 2855-2866
    • Ono, A.1    Orenstein, J.M.2    Freed, E.O.3
  • 55
    • 0022408015 scopus 로고
    • Myristylation of gag protein in human T-cell leukemia virus type-I and type-II
    • Ootsuyama, Y., Shimotohno, K., Miwa, M., Oroszlan, S., and Sugimura, T. (1985). Myristylation of gag protein in human T-cell leukemia virus type-I and type-II. Jpn. J. Cancer Res. 76, 1132-1135.
    • (1985) Jpn. J. Cancer Res. , vol.76 , pp. 1132-1135
    • Ootsuyama, Y.1    Shimotohno, K.2    Miwa, M.3    Oroszlan, S.4    Sugimura, T.5
  • 56
    • 0021905870 scopus 로고
    • Primary structure and processing of gag and env gene products of human T-cell leukemia viruses HTLV-ICR and HTLV-IATK
    • doi: 10.1007/978-3-642-70113-9_14
    • Oroszlan, S., and Copeland, T. D. (1985). Primary structure and processing of gag and env gene products of human T-cell leukemia viruses HTLV-ICR and HTLV-IATK. Curr. Top. Microbiol. Immunol. 115, 221-233. doi: 10.1007/978-3-642-70113-9_14
    • (1985) Curr. Top. Microbiol. Immunol. , vol.115 , pp. 221-233
    • Oroszlan, S.1    Copeland, T.D.2
  • 57
    • 0041488655 scopus 로고    scopus 로고
    • Infectious HIV-1 assembles in late endosomes in primary macrophages
    • doi: 10.1083/jcb.200304008
    • Pelchen-Matthews, A., Kramer, B., and Marsh, M. (2003). Infectious HIV-1 assembles in late endosomes in primary macrophages. J. Cell Biol. 162, 443-455. doi: 10.1083/jcb.200304008
    • (2003) J. Cell Biol. , vol.162 , pp. 443-455
    • Pelchen-Matthews, A.1    Kramer, B.2    Marsh, M.3
  • 58
    • 4143061388 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 matrix inhibits and confers cooperativity on gag precursor-membrane interactions
    • doi: 10.1128/JVI.78.17.9560-9563.2004
    • Perez-Caballero, D., Hatziioannou, T., Martin-Serrano, J., and Bieniasz, P. D. (2004). Human immunodeficiency virus type 1 matrix inhibits and confers cooperativity on gag precursor-membrane interactions. J. Virol. 78, 9560-9563. doi: 10.1128/JVI.78.17.9560-9563.2004
    • (2004) J. Virol. , vol.78 , pp. 9560-9563
    • Perez-Caballero, D.1    Hatziioannou, T.2    Martin-Serrano, J.3    Bieniasz, P.D.4
  • 59
    • 0035003983 scopus 로고    scopus 로고
    • Sequence-specific interaction between HIV-1 matrix protein and viral genomic RNA revealed by in vitro genetic selection
    • doi: 10.1017/S1355838201002023
    • Purohit, P., Dupont, S., Stevenson, M., and Green, M. R. (2001). Sequence-specific interaction between HIV-1 matrix protein and viral genomic RNA revealed by in vitro genetic selection. RNA 7, 576-584. doi: 10.1017/S1355838201002023
    • (2001) RNA , vol.7 , pp. 576-584
    • Purohit, P.1    Dupont, S.2    Stevenson, M.3    Green, M.R.4
  • 60
    • 73649131251 scopus 로고    scopus 로고
    • C-terminal domain modulates the nucleic acid chaperone activity of human T-cell leukemia virus type 1 nucleocapsid protein via an electrostatic mechanism
    • doi: 10.1074/jbc.M109.051334
    • Qualley, D. F., Stewart-Maynard, K. M., Wang, F., Mitra, M., Gorelick, R. J., Rouzina, I.,et al. (2010). C-terminal domain modulates the nucleic acid chaperone activity of human T-cell leukemia virus type 1 nucleocapsid protein via an electrostatic mechanism. J. Biol. Chem. 285, 295-307. doi: 10.1074/jbc.M109.051334
    • (2010) J. Biol. Chem. , vol.285 , pp. 295-307
    • Qualley, D.F.1    Stewart-Maynard, K.M.2    Wang, F.3    Mitra, M.4    Gorelick, R.J.5    Rouzina, I.6
  • 61
    • 0036788110 scopus 로고    scopus 로고
    • Human macrophages accumulate HIV-1 particles in MHC II compartments
    • doi: 10.1034/j.1600-0854.2002.31004.x
    • Raposo, G., Moore, M., Innes, D., Leijendekker, R., Leigh-Brown, A., Benaroch, P.,et al. (2002). Human macrophages accumulate HIV-1 particles in MHC II compartments. Traffic 3, 718-729. doi: 10.1034/j.1600-0854.2002.31004.x
    • (2002) Traffic , vol.3 , pp. 718-729
    • Raposo, G.1    Moore, M.2    Innes, D.3    Leijendekker, R.4    Leigh-Brown, A.5    Benaroch, P.6
  • 62
    • 0034744302 scopus 로고    scopus 로고
    • The NH2-terminal domain of the human T-cell leukemia virus type 1 capsid protein is involved in particle formation
    • doi: 10.1128/JVI.75.11.5277-5287.2001
    • Rayne, F., Bouamr, F., Lalanne, J., and Mamoun, R. Z. (2001). The NH2-terminal domain of the human T-cell leukemia virus type 1 capsid protein is involved in particle formation. J. Virol. 75, 5277-5287. doi: 10.1128/JVI.75.11.5277-5287.2001
    • (2001) J. Virol. , vol.75 , pp. 5277-5287
    • Rayne, F.1    Bouamr, F.2    Lalanne, J.3    Mamoun, R.Z.4
  • 63
    • 79959914775 scopus 로고    scopus 로고
    • Diverse interactions of retroviral Gag proteins with RNAs
    • doi: 10.1016/j.tibs.2011.04.001
    • Rein, A., Datta, S. A., Jones, C. P., and Musier-Forsyth, K. (2011). Diverse interactions of retroviral Gag proteins with RNAs. Trends Biochem. Sci. 36, 373-380. doi: 10.1016/j.tibs.2011.04.001
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 373-380
    • Rein, A.1    Datta, S.A.2    Jones, C.P.3    Musier-Forsyth, K.4
  • 64
    • 0032875098 scopus 로고    scopus 로고
    • Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins
    • doi: 10.1016/S0167-4889(99)00075-0
    • Resh, M. D. (1999). Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins. Biochim. Biophys. Acta 1451, 1-16. doi: 10.1016/S0167-4889(99)00075-0
    • (1999) Biochim. Biophys. Acta , vol.1451 , pp. 1-16
    • Resh, M.D.1
  • 65
    • 0347087223 scopus 로고    scopus 로고
    • A myristoyl switch regulates membrane binding of HIV-1 Gag
    • doi: 10.1073/pnas.0308043101
    • Resh, M. D. (2004). A myristoyl switch regulates membrane binding of HIV-1 Gag. Proc. Natl. Acad. Sci. U.S.A. 101, 417-418. doi: 10.1073/pnas.0308043101
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 417-418
    • Resh, M.D.1
  • 66
    • 84872973963 scopus 로고    scopus 로고
    • Membrane domains and the "lipid raft" concept
    • doi: 10.2174/0929867311320010003
    • Sonnino, S., and Prinetti, A. (2013). Membrane domains and the "lipid raft" concept. Curr. Med. Chem. 20, 4-21. doi: 10.2174/0929867311320010003
    • (2013) Curr. Med. Chem. , vol.20 , pp. 4-21
    • Sonnino, S.1    Prinetti, A.2
  • 67
    • 34548182230 scopus 로고    scopus 로고
    • Basic residues in the Mason-Pfizer monkey virus gag matrix domain regulate intracellular trafficking and capsid-membrane interactions
    • doi: 10.1128/JVI.00657-07
    • Stansell, E., Apkarian, R., Haubova, S., Diehl, W. E., Tytler, E. M., and Hunter, E. (2007). Basic residues in the Mason-Pfizer monkey virus gag matrix domain regulate intracellular trafficking and capsid-membrane interactions. J. Virol. 81, 8977-8988. doi: 10.1128/JVI.00657-07
    • (2007) J. Virol. , vol.81 , pp. 8977-8988
    • Stansell, E.1    Apkarian, R.2    Haubova, S.3    Diehl, W.E.4    Tytler, E.M.5    Hunter, E.6
  • 68
    • 0347717579 scopus 로고    scopus 로고
    • Entropic switch regulates myristate exposure in the HIV-1 matrix protein
    • doi: 10.1073/pnas.0305665101
    • Tang, C., Loeliger, E., Luncsford, P., Kinde, I., Beckett, D., and Summers, M. F. (2004). Entropic switch regulates myristate exposure in the HIV-1 matrix protein. Proc. Natl. Acad. Sci. U.S.A. 101, 517-522. doi: 10.1073/pnas.0305665101
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 517-522
    • Tang, C.1    Loeliger, E.2    Luncsford, P.3    Kinde, I.4    Beckett, D.5    Summers, M.F.6
  • 69
    • 0037459061 scopus 로고    scopus 로고
    • The molecular motor toolbox for intracellular transport
    • doi: 10.1016/S0092-8674(03)00111-9
    • Vale, R. D. (2003). The molecular motor toolbox for intracellular transport. Cell 112, 467-480. doi: 10.1016/S0092-8674(03)00111-9
    • (2003) Cell , vol.112 , pp. 467-480
    • Vale, R.D.1
  • 70
    • 38549173564 scopus 로고    scopus 로고
    • Membrane lipids: where they are and how they behave
    • doi: 10.1038/nrm2330
    • van Meer, G., Voelker, D. R., and Feigenson, G. W. (2008). Membrane lipids: where they are and how they behave. Nat. Rev. Mol. Cell Biol. 9, 112-124. doi: 10.1038/nrm2330
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 112-124
    • van Meer, G.1    Voelker, D.R.2    Feigenson, G.W.3
  • 71
    • 0032795497 scopus 로고    scopus 로고
    • Mass determination of rous sarcoma virus virions by scanning transmission electron microscopy
    • Vogt, V. M., and Simon, M. N. (1999). Mass determination of rous sarcoma virus virions by scanning transmission electron microscopy. J. Virol. 73, 7050-7055.
    • (1999) J. Virol. , vol.73 , pp. 7050-7055
    • Vogt, V.M.1    Simon, M.N.2
  • 72
    • 0037404501 scopus 로고    scopus 로고
    • Functional surfaces of the human immunodeficiency virus type 1 capsid protein
    • doi: 10.1128/JVI.77.9.5439-5450.2003
    • von Schwedler, U. K., Stray, K. M., Garrus, J. E., and Sundquist, W. I. (2003). Functional surfaces of the human immunodeficiency virus type 1 capsid protein. J. Virol. 77, 5439-5450. doi: 10.1128/JVI.77.9.5439-5450.2003
    • (2003) J. Virol. , vol.77 , pp. 5439-5450
    • von Schwedler, U.K.1    Stray, K.M.2    Garrus, J.E.3    Sundquist, W.I.4
  • 73
    • 34248229690 scopus 로고    scopus 로고
    • More than one door-budding of enveloped viruses through cellular membranes
    • doi: 10.1016/j.febslet.2007.03.060
    • Welsch, S., Muller, B., and Krausslich, H. G. (2007). More than one door-budding of enveloped viruses through cellular membranes. FEBS Lett. 581, 2089-2097. doi: 10.1016/j.febslet.2007.03.060
    • (2007) FEBS Lett. , vol.581 , pp. 2089-2097
    • Welsch, S.1    Muller, B.2    Krausslich, H.G.3
  • 74
    • 0032560502 scopus 로고    scopus 로고
    • Supramolecular organization of immature and mature murine leukemia virus revealed by electron cryo-microscopy: implications for retroviral assembly mechanisms
    • doi: 10.1073/pnas.95.13.7299
    • Yeager, M., Wilson-Kubalek, E. M., Weiner, S. G., Brown, P. O., and Rein, A. (1998). Supramolecular organization of immature and mature murine leukemia virus revealed by electron cryo-microscopy: implications for retroviral assembly mechanisms. Proc. Natl. Acad. Sci. U.S.A. 95, 7299-7304. doi: 10.1073/pnas.95.13.7299
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 7299-7304
    • Yeager, M.1    Wilson-Kubalek, E.M.2    Weiner, S.G.3    Brown, P.O.4    Rein, A.5
  • 75
    • 55249088255 scopus 로고    scopus 로고
    • Genome-scale RNAi screen for host factors required for HIV replication
    • doi: 10.1016/j.chom.2008.10.004
    • Zhou, H., Xu, M., Huang, Q., Gates, A. T., Zhang, X. D., Castle, J. C.,et al. (2008). Genome-scale RNAi screen for host factors required for HIV replication. Cell Host Microbe 4, 495-504. doi: 10.1016/j.chom.2008.10.004
    • (2008) Cell Host Microbe , vol.4 , pp. 495-504
    • Zhou, H.1    Xu, M.2    Huang, Q.3    Gates, A.T.4    Zhang, X.D.5    Castle, J.C.6
  • 76
    • 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., and 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
  • 77
    • 0029861657 scopus 로고    scopus 로고
    • Differential membrane binding of the human immunodeficiency virus type 1 matrix protein
    • Zhou, W., and Resh, M. D. (1996). Differential membrane binding of the human immunodeficiency virus type 1 matrix protein. J. Virol. 70, 8540-8548.
    • (1996) J. Virol. , vol.70 , pp. 8540-8548
    • Zhou, W.1    Resh, M.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.