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Volumn 89, Issue 19, 2015, Pages 9765-9780

Distribution and redistribution of HIV-1 nucleocapsid protein in immature, mature, and integrase-inhibited virions: A role for integrase in maturation

Author keywords

[No Author keywords available]

Indexed keywords

ALLOSTERIC INTEGRASE INHIBITOR; GAG PROTEIN; INTEGRASE; INTEGRASE INHIBITOR; NUCLEOCAPSID PROTEIN; UNCLASSIFIED DRUG; VIRAL RIBONUCLEOPROTEIN; VIRUS PROTEIN; VIRUS RNA;

EID: 84940994512     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01522-15     Document Type: Article
Times cited : (82)

References (74)
  • 3
    • 12544255655 scopus 로고    scopus 로고
    • Three-dimensional structure of HIV-1 virus-like particles by electron cryotomography
    • Benjamin J, Ganser-Pornillos BK, Tivol WF, Sundquist WI, Jensen GJ. 2005. Three-dimensional structure of HIV-1 virus-like particles by electron cryotomography. J Mol Biol 346:577-588. http://dx.doi.org/10.1016/j.jmb.2004.11.064.
    • (2005) J Mol Biol , vol.346 , pp. 577-588
    • Benjamin, J.1    Ganser-Pornillos, B.K.2    Tivol, W.F.3    Sundquist, W.I.4    Jensen, G.J.5
  • 4
    • 33644806492 scopus 로고    scopus 로고
    • The mechanism of HIV-1 core assembly: insights from threedimensional reconstructions of authentic virions
    • Briggs JA, Grünewald K, Glass B, Forster F, Kräusslich HG, Fuller SD. 2006. The mechanism of HIV-1 core assembly: insights from threedimensional reconstructions of authentic virions. Structure 14:15-20. http://dx.doi.org/10.1016/j.str.2005.09.010.
    • (2006) Structure , vol.14 , pp. 15-20
    • Briggs, J.A.1    Grünewald, K.2    Glass, B.3    Forster, F.4    Kräusslich, H.G.5    Fuller, S.D.6
  • 5
    • 84920767638 scopus 로고    scopus 로고
    • Electron cryotomography studies of maturing HIV-1 particles reveal the assembly pathway of the viral core
    • Woodward CL, Cheng SN, Jensen GJ. 2015. Electron cryotomography studies of maturing HIV-1 particles reveal the assembly pathway of the viral core. J Virol 89:1267-1277. http://dx.doi.org/10.1128/JVI.02997-14.
    • (2015) J Virol , vol.89 , pp. 1267-1277
    • Woodward, C.L.1    Cheng, S.N.2    Jensen, G.J.3
  • 7
    • 0031804609 scopus 로고    scopus 로고
    • Inhibitors of HIV-1 protease: a major success of structure-assisted drug design
    • Wlodawer A, Vondrasek J. 1998. Inhibitors of HIV-1 protease: a major success of structure-assisted drug design. Annu Rev Biophys Biomol Struct 27:249-284. http://dx.doi.org/10.1146/annurev.biophys.27.1.249.
    • (1998) Annu Rev Biophys Biomol Struct , vol.27 , pp. 249-284
    • Wlodawer, A.1    Vondrasek, J.2
  • 9
    • 0346688636 scopus 로고    scopus 로고
    • Small-molecule inhibition of human immunodeficiency virus type 1 replication by specific targeting of the final step of virion maturation
    • Zhou J, Yuan X, Dismuke D, Forshey BM, Lundquist C, Lee KH, Aiken C, Chen CH. 2004. Small-molecule inhibition of human immunodeficiency virus type 1 replication by specific targeting of the final step of virion maturation. J Virol 78:922-929. http://dx.doi.org/10.1128/JVI.78.2.922-929.2004.
    • (2004) J Virol , vol.78 , pp. 922-929
    • Zhou, J.1    Yuan, X.2    Dismuke, D.3    Forshey, B.M.4    Lundquist, C.5    Lee, K.H.6    Aiken, C.7    Chen, C.H.8
  • 10
    • 0032617446 scopus 로고    scopus 로고
    • In vivo analysis of retroviral integrase structure and function
    • Engelman A. 1999. In vivo analysis of retroviral integrase structure and function. Adv Virus Res 52:411-426. http://dx.doi.org/10.1016/S0065-3527(08)60309-7.
    • (1999) Adv Virus Res , vol.52 , pp. 411-426
    • Engelman, A.1
  • 17
    • 84905390193 scopus 로고    scopus 로고
    • Allosteric inhibition of human immunodeficiency virus integrase: late block during viral replication and abnormal multimerization involving specific protein domains
    • Gupta K, Brady T, Dyer BM, Malani N, Hwang Y, Male F, Nolte RT, Wang L, Velthuisen E, Jeffrey J, Van Duyne GD, Bushman FD. 2014. Allosteric inhibition of human immunodeficiency virus integrase: late block during viral replication and abnormal multimerization involving specific protein domains. J Biol Chem 289:20477-20488. http://dx.doi.org/10.1074/jbc. M114.551119.
    • (2014) J Biol Chem , vol.289 , pp. 20477-20488
    • Gupta, K.1    Brady, T.2    Dyer, B.M.3    Malani, N.4    Hwang, Y.5    Male, F.6    Nolte, R.T.7    Wang, L.8    Velthuisen, E.9    Jeffrey, J.10    Van Duyne, G.D.11    Bushman, F.D.12
  • 20
    • 84921369549 scopus 로고    scopus 로고
    • Molecular mechanisms of retroviral integration site selection
    • Kvaratskhelia M, Sharma A, Larue RC, Serrao E, Engelman A. 2014. Molecular mechanisms of retroviral integration site selection. Nucleic Acids Res 42:10209-10225. http://dx.doi.org/10.1093/nar/gku769.
    • (2014) Nucleic Acids Res , vol.42 , pp. 10209-10225
    • Kvaratskhelia, M.1    Sharma, A.2    Larue, R.C.3    Serrao, E.4    Engelman, A.5
  • 22
    • 84907224797 scopus 로고    scopus 로고
    • TALEN knockout of the PSIP1 gene in human cells: analyses of HIV-1 replication and allosteric integrase inhibitor mechanism
    • Fadel HJ, Morrison JH, Saenz DT, Fuchs JR, Kvaratskhelia M, Ekker SC, Poeschla EM. 2014. TALEN knockout of the PSIP1 gene in human cells: analyses of HIV-1 replication and allosteric integrase inhibitor mechanism. J Virol 88:9704-9717. http://dx.doi.org/10.1128/JVI.01397-14.
    • (2014) J Virol , vol.88 , pp. 9704-9717
    • Fadel, H.J.1    Morrison, J.H.2    Saenz, D.T.3    Fuchs, J.R.4    Kvaratskhelia, M.5    Ekker, S.C.6    Poeschla, E.M.7
  • 25
    • 78951488338 scopus 로고    scopus 로고
    • HIV-1 maturation inhibitor bevirimat stabilizes the immature Gag lattice
    • Keller PW, Adamson CS, Heymann JB, Freed EO, Steven AC. 2011. HIV-1 maturation inhibitor bevirimat stabilizes the immature Gag lattice. J Virol 85:1420-1428. http://dx.doi.org/10.1128/JVI.01926-10.
    • (2011) J Virol , vol.85 , pp. 1420-1428
    • Keller, P.W.1    Adamson, C.S.2    Heymann, J.B.3    Freed, E.O.4    Steven, A.C.5
  • 26
    • 84888036006 scopus 로고    scopus 로고
    • A two-pronged structural analysis of retroviral maturation indicates that core formation proceeds by a disassembly-reassembly pathway rather than a displacive transition
    • Keller PW, Huang RK, England MR, Waki K, Cheng N, Heymann JB, Craven RC, Freed EO, Steven AC. 2013. A two-pronged structural analysis of retroviral maturation indicates that core formation proceeds by a disassembly-reassembly pathway rather than a displacive transition. J Virol 87:13655-13664. http://dx.doi.org/10.1128/JVI.01408-13.
    • (2013) J Virol , vol.87 , pp. 13655-13664
    • Keller, P.W.1    Huang, R.K.2    England, M.R.3    Waki, K.4    Cheng, N.5    Heymann, J.B.6    Craven, R.C.7    Freed, E.O.8    Steven, A.C.9
  • 27
    • 84870664162 scopus 로고    scopus 로고
    • Role of the SP2 domain and its proteolytic cleavage in HIV-1 structural maturation and infectivity
    • de Marco A, Heuser AM, Glass B, Kräusslich HG, Muller B, Briggs JA. 2012. Role of the SP2 domain and its proteolytic cleavage in HIV-1 structural maturation and infectivity. J Virol 86:13708-13716. http://dx.doi.org/10.1128/JVI.01704-12.
    • (2012) J Virol , vol.86 , pp. 13708-13716
    • de Marco, A.1    Heuser, A.M.2    Glass, B.3    Kräusslich, H.G.4    Muller, B.5    Briggs, J.A.6
  • 29
    • 0032846188 scopus 로고    scopus 로고
    • Structure-based mutagenesis of the human immunodeficiency virus type 1 DNA attachment site: effects on integration and cDNA synthesis
    • Brown HE, Chen H, Engelman A. 1999. Structure-based mutagenesis of the human immunodeficiency virus type 1 DNA attachment site: effects on integration and cDNA synthesis. J Virol 73:9011-9020.
    • (1999) J Virol , vol.73 , pp. 9011-9020
    • Brown, H.E.1    Chen, H.2    Engelman, A.3
  • 30
    • 0036838711 scopus 로고    scopus 로고
    • Nuclear localization of human immunodeficiency virus type 1 preintegration complexes (PICs): V165A and R166A are pleiotropic integrase mutants primarily defective for integration, not PIC nuclear import
    • Limon A, Devroe E, Lu R, Ghory HZ, Silver PA, Engelman A. 2002. Nuclear localization of human immunodeficiency virus type 1 preintegration complexes (PICs): V165A and R166A are pleiotropic integrase mutants primarily defective for integration, not PIC nuclear import. J Virol 76:10598-10607. http://dx.doi.org/10.1128/JVI.76.21.10598-10607.2002.
    • (2002) J Virol , vol.76 , pp. 10598-10607
    • Limon, A.1    Devroe, E.2    Lu, R.3    Ghory, H.Z.4    Silver, P.A.5    Engelman, A.6
  • 31
    • 8644226108 scopus 로고    scopus 로고
    • Class II integrase mutants with changes in putative nuclear localization signals are primarily blocked at a postnuclear entry step of human immunodeficiency virus type 1 replication
    • Lu R, Limon A, Devroe E, Silver PA, Cherepanov P, Engelman A. 2004. Class II integrase mutants with changes in putative nuclear localization signals are primarily blocked at a postnuclear entry step of human immunodeficiency virus type 1 replication. J Virol 78:12735-12746. http://dx.doi.org/10.1128/JVI.78.23.12735-12746.2004.
    • (2004) J Virol , vol.78 , pp. 12735-12746
    • Lu, R.1    Limon, A.2    Devroe, E.3    Silver, P.A.4    Cherepanov, P.5    Engelman, A.6
  • 32
    • 60049091300 scopus 로고    scopus 로고
    • Assembly properties of human immunodeficiency virus type 1 Gag-leucine zipper chimeras: implications for retrovirus assembly
    • Crist RM, Datta SA, Stephen AG, Soheilian F, Mirro J, Fisher RJ, Nagashima K, Rein A. 2009. Assembly properties of human immunodeficiency virus type 1 Gag-leucine zipper chimeras: implications for retrovirus assembly. J Virol 83:2216-2225. http://dx.doi.org/10.1128/JVI.02031-08.
    • (2009) J Virol , vol.83 , pp. 2216-2225
    • Crist, R.M.1    Datta, S.A.2    Stephen, A.G.3    Soheilian, F.4    Mirro, J.5    Fisher, R.J.6    Nagashima, K.7    Rein, A.8
  • 33
    • 0030960338 scopus 로고    scopus 로고
    • Inactivation of the human immunodeficiency virus type 1 inhibitory elements allows Rev-independent expression of Gag and Gag/protease and particle formation
    • Schneider R, Campbell M, Nasioulas G, Felber BK, Pavlakis GN. 1997. Inactivation of the human immunodeficiency virus type 1 inhibitory elements allows Rev-independent expression of Gag and Gag/protease and particle formation. J Virol 71:4892-4903.
    • (1997) J Virol , vol.71 , pp. 4892-4903
    • Schneider, R.1    Campbell, M.2    Nasioulas, G.3    Felber, B.K.4    Pavlakis, G.N.5
  • 34
    • 0033046030 scopus 로고    scopus 로고
    • Efficacy and safety analyses of a recombinant human immunodeficiency virus type 1 derived vector system
    • Chang LJ, Urlacher V, Iwakuma T, Cui Y, Zucali J. 1999. Efficacy and safety analyses of a recombinant human immunodeficiency virus type 1 derived vector system. Gene Ther 6:715-728. http://dx.doi.org/10.1038/sj.gt.3300895.
    • (1999) Gene Ther , vol.6 , pp. 715-728
    • Chang, L.J.1    Urlacher, V.2    Iwakuma, T.3    Cui, Y.4    Zucali, J.5
  • 35
    • 0034863355 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 replication in the absence of integrase-mediated DNA recombination: definition of permissive and nonpermissive T-cell lines
    • Nakajima N, Lu R, Engelman A. 2001. Human immunodeficiency virus type 1 replication in the absence of integrase-mediated DNA recombination: definition of permissive and nonpermissive T-cell lines. J Virol 75: 7944-7955. http://dx.doi.org/10.1128/JVI.75.17.7944-7955.2001.
    • (2001) J Virol , vol.75 , pp. 7944-7955
    • Nakajima, N.1    Lu, R.2    Engelman, A.3
  • 36
    • 0030851908 scopus 로고    scopus 로고
    • Functional RT and IN incorporated into HIV-1 particles independently of the Gag/Pol precursor protein
    • Wu X, Liu H, Xiao H, Conway JA, Hunter E, Kappes JC. 1997. Functional RT and IN incorporated into HIV-1 particles independently of the Gag/Pol precursor protein. EMBO J 16:5113-5122. http://dx.doi.org/10.1093/emboj/16.16.5113.
    • (1997) EMBO J , vol.16 , pp. 5113-5122
    • Wu, X.1    Liu, H.2    Xiao, H.3    Conway, J.A.4    Hunter, E.5    Kappes, J.C.6
  • 37
    • 84871220094 scopus 로고    scopus 로고
    • HRP2 determines the efficiency and specificity of HIV-1 integration in LEDGF/p75 knockout cells but does not contribute to the antiviral activity of a potent LEDGF/p75-binding site integrase inhibitor
    • Wang H, Jurado KA, Wu X, Shun MC, Li X, Ferris AL, Smith SJ, Patel PA, Fuchs JR, Cherepanov P, Kvaratskhelia M, Hughes SH, Engelman A. 2012. HRP2 determines the efficiency and specificity of HIV-1 integration in LEDGF/p75 knockout cells but does not contribute to the antiviral activity of a potent LEDGF/p75-binding site integrase inhibitor. Nucleic Acids Res 40:11518-11530. http://dx.doi.org/10.1093/nar/gks913.
    • (2012) Nucleic Acids Res , vol.40 , pp. 11518-11530
    • Wang, H.1    Jurado, K.A.2    Wu, X.3    Shun, M.C.4    Li, X.5    Ferris, A.L.6    Smith, S.J.7    Patel, P.A.8    Fuchs, J.R.9    Cherepanov, P.10    Kvaratskhelia, M.11    Hughes, S.H.12    Engelman, A.13
  • 38
    • 34447513231 scopus 로고    scopus 로고
    • LEDGF/p75 functions downstream from preintegration complex formation to effect genespecific HIV-1 integration
    • Shun MC, Raghavendra NK, VandegraaffN, Daigle JE, Hughes S, Kellam P, Cherepanov P, Engelman A. 2007. LEDGF/p75 functions downstream from preintegration complex formation to effect genespecific HIV-1 integration. Genes Dev 21:1767-1778. http://dx.doi.org/10.1101/gad.1565107.
    • (2007) Genes Dev , vol.21 , pp. 1767-1778
    • Shun, M.C.1    Raghavendra, N.K.2    Vandegraaff, N.3    Daigle, J.E.4    Hughes, S.5    Kellam, P.6    Cherepanov, P.7    Engelman, A.8
  • 39
    • 84857981961 scopus 로고    scopus 로고
    • Structural changes in influenza virus at low pH characterized by cryoelectron tomography
    • Fontana J, Cardone G, Heymann JB, Winkler DC, Steven AC. 2012. Structural changes in influenza virus at low pH characterized by cryoelectron tomography. J Virol 86:2919-2929. http://dx.doi.org/10.1128/JVI.06698-11.
    • (2012) J Virol , vol.86 , pp. 2919-2929
    • Fontana, J.1    Cardone, G.2    Heymann, J.B.3    Winkler, D.C.4    Steven, A.C.5
  • 40
    • 25644458666 scopus 로고    scopus 로고
    • Automated electron microscope tomography using robust prediction of specimen movements
    • Mastronarde DN. 2005. Automated electron microscope tomography using robust prediction of specimen movements. J Struct Biol 152:36-51. http://dx.doi.org/10.1016/j.jsb.2005.07.007.
    • (2005) J Struct Biol , vol.152 , pp. 36-51
    • Mastronarde, D.N.1
  • 41
    • 40649123787 scopus 로고    scopus 로고
    • Computational resources for cryo-electron tomography in Bsoft
    • Heymann JB, Cardone G, Winkler DC, Steven AC. 2008. Computational resources for cryo-electron tomography in Bsoft. J Struct Biol 161: 232-242. http://dx.doi.org/10.1016/j.jsb.2007.08.002.
    • (2008) J Struct Biol , vol.161 , pp. 232-242
    • Heymann, J.B.1    Cardone, G.2    Winkler, D.C.3    Steven, A.C.4
  • 42
    • 0035783287 scopus 로고    scopus 로고
    • Noise reduction in electron tomographic reconstructions using nonlinear anisotropic diffusion
    • Frangakis AS, Hegerl R. 2001. Noise reduction in electron tomographic reconstructions using nonlinear anisotropic diffusion. J Struct Biol 135: 239-250. http://dx.doi.org/10.1006/jsbi.2001.4406.
    • (2001) J Struct Biol , vol.135 , pp. 239-250
    • Frangakis, A.S.1    Hegerl, R.2
  • 45
    • 0032776165 scopus 로고    scopus 로고
    • Coupled integration of human immunodeficiency virus type 1cDNAends by purified integrase in vitro: stimulation by the viral nucleocapsid protein
    • Carteau S, Gorelick RJ, Bushman FD. 1999. Coupled integration of human immunodeficiency virus type 1cDNAends by purified integrase in vitro: stimulation by the viral nucleocapsid protein. J Virol 73:6670-6679.
    • (1999) J Virol , vol.73 , pp. 6670-6679
    • Carteau, S.1    Gorelick, R.J.2    Bushman, F.D.3
  • 46
    • 0028915128 scopus 로고
    • Multiple effects of mutations in human immunodeficiency virus type 1 integrase on viral replication
    • Engelman A, Englund G, Orenstein JM, Martin MA, Craigie R. 1995. Multiple effects of mutations in human immunodeficiency virus type 1 integrase on viral replication. J Virol 69:2729-2736.
    • (1995) J Virol , vol.69 , pp. 2729-2736
    • Engelman, A.1    Englund, G.2    Orenstein, J.M.3    Martin, M.A.4    Craigie, R.5
  • 47
    • 84878252974 scopus 로고    scopus 로고
    • A homology model of HIV-1 integrase and analysis of mutations designed to test the model
    • Johnson BC, Métifiot M, Ferris A, Pommier Y, Hughes SH. 2013. A homology model of HIV-1 integrase and analysis of mutations designed to test the model. J Mol Biol 425:2133-2146. http://dx.doi.org/10.1016/j.jmb.2013.03.027.
    • (2013) J Mol Biol , vol.425 , pp. 2133-2146
    • Johnson, B.C.1    Métifiot, M.2    Ferris, A.3    Pommier, Y.4    Hughes, S.H.5
  • 52
    • 84862907893 scopus 로고    scopus 로고
    • Bubblegrams reveal the inner body of bacteriophage phiKZ
    • Wu W, Thomas JA, Cheng N, Black LW, Steven AC. 2012. Bubblegrams reveal the inner body of bacteriophage phiKZ. Science 335:182. http://dx.doi.org/10.1126/science.1214120.
    • (2012) Science , vol.335 , pp. 182
    • Wu, W.1    Thomas, J.A.2    Cheng, N.3    Black, L.W.4    Steven, A.C.5
  • 53
    • 84894484537 scopus 로고    scopus 로고
    • Exploiting radiation damage to map proteins in nucleoprotein complexes: the internal structure of bacteriophage T7
    • Cheng N, Wu W, Watts NR, Steven AC. 2014. Exploiting radiation damage to map proteins in nucleoprotein complexes: the internal structure of bacteriophage T7. J Struct Biol 185:250-256. http://dx.doi.org/10.1016/j.jsb.2013.12.004.
    • (2014) J Struct Biol , vol.185 , pp. 250-256
    • Cheng, N.1    Wu, W.2    Watts, N.R.3    Steven, A.C.4
  • 54
    • 0027853061 scopus 로고
    • The effects of radiation damage on the structure of frozen hydrated HSV-1 capsids
    • Conway JF, Trus BL, Booy FP, Newcomb WW, Brown JC, Steven AC. 1993. The effects of radiation damage on the structure of frozen hydrated HSV-1 capsids. J Struct Biol 111:222-233. http://dx.doi.org/10.1006/jsbi.1993.1052.
    • (1993) J Struct Biol , vol.111 , pp. 222-233
    • Conway, J.F.1    Trus, B.L.2    Booy, F.P.3    Newcomb, W.W.4    Brown, J.C.5    Steven, A.C.6
  • 55
    • 0029123968 scopus 로고
    • Cryo-electron energy loss spectroscopy: observations on vitrified hydrated specimens and radiation damage
    • Leapman RD, Sun S. 1995. Cryo-electron energy loss spectroscopy: observations on vitrified hydrated specimens and radiation damage. Ultramicroscopy 59:71-79. http://dx.doi.org/10.1016/0304-3991(95)00019-W.
    • (1995) Ultramicroscopy , vol.59 , pp. 71-79
    • Leapman, R.D.1    Sun, S.2
  • 56
    • 75749092651 scopus 로고    scopus 로고
    • Origin and temperature dependence of radiation damage in biological samples at cryogenic temperatures
    • Meents A, Gutmann S, Wagner A, Schulze-Briese C. 2010. Origin and temperature dependence of radiation damage in biological samples at cryogenic temperatures. Proc Natl Acad Sci U S A 107:1094-1099. http://dx.doi.org/10.1073/pnas.0905481107.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 1094-1099
    • Meents, A.1    Gutmann, S.2    Wagner, A.3    Schulze-Briese, C.4
  • 59
    • 0029815034 scopus 로고    scopus 로고
    • Lack of integrase can markedly affect human immunodeficiency virus type 1 particle production in the presence of an active viral protease
    • Bukovsky A, Gottlinger H. 1996. Lack of integrase can markedly affect human immunodeficiency virus type 1 particle production in the presence of an active viral protease. J Virol 70:6820-6825.
    • (1996) J Virol , vol.70 , pp. 6820-6825
    • Bukovsky, A.1    Gottlinger, H.2
  • 60
    • 0036094824 scopus 로고    scopus 로고
    • Formation of a human immunodeficiency virus type 1 core of optimal stability is crucial for viral replication
    • Forshey BM, von Schwedler U, Sundquist WI, Aiken C. 2002. Formation of a human immunodeficiency virus type 1 core of optimal stability is crucial for viral replication. J Virol 76:5667-5677. http://dx.doi.org/10.1128/JVI.76.11.5667-5677.2002.
    • (2002) J Virol , vol.76 , pp. 5667-5677
    • Forshey, B.M.1    von Schwedler, U.2    Sundquist, W.I.3    Aiken, C.4
  • 63
    • 33745103496 scopus 로고    scopus 로고
    • The retrovirus RNA trafficking granule: from birth to maturity
    • Cochrane AW, McNally MT, Mouland AJ. 2006. The retrovirus RNA trafficking granule: from birth to maturity. Retrovirology 3:18. http://dx.doi.org/10.1186/1742-4690-3-18.
    • (2006) Retrovirology , vol.3 , pp. 18
    • Cochrane, A.W.1    McNally, M.T.2    Mouland, A.J.3
  • 64
    • 0037378462 scopus 로고    scopus 로고
    • Disassembly of human immunodeficiency virus type 1 cores in vitro reveals association of Nef with the subviral ribonucleoprotein complex
    • Forshey BM, Aiken C. 2003. Disassembly of human immunodeficiency virus type 1 cores in vitro reveals association of Nef with the subviral ribonucleoprotein complex. J Virol 77:4409-4414. http://dx.doi.org/10.1128/JVI.77.7.4409-4414.2003.
    • (2003) J Virol , vol.77 , pp. 4409-4414
    • Forshey, B.M.1    Aiken, C.2
  • 65
    • 85027947880 scopus 로고    scopus 로고
    • A protein ballet around the viral genome orchestrated by HIV-1 reverse transcriptase leads to an architectural switch: from nucleocapsidcondensed RNA to Vpr-bridged DNA
    • Lyonnais S, Gorelick RJ, Heniche-Boukhalfa F, Bouaziz S, Parissi V, Mouscadet JF, Restle T, Gatell JM, Le Cam E, Mirambeau G. 2013. A protein ballet around the viral genome orchestrated by HIV-1 reverse transcriptase leads to an architectural switch: from nucleocapsidcondensed RNA to Vpr-bridged DNA. Virus Res 171:287-303. http://dx.doi.org/10.1016/j.virusres.2012.09.008.
    • (2013) Virus Res , vol.171 , pp. 287-303
    • Lyonnais, S.1    Gorelick, R.J.2    Heniche-Boukhalfa, F.3    Bouaziz, S.4    Parissi, V.5    Mouscadet, J.F.6    Restle, T.7    Gatell, J.M.8    Le Cam, E.9    Mirambeau, G.10
  • 66
    • 0034125738 scopus 로고    scopus 로고
    • Isolation of human immunodeficiency virus type 1 cores: retention of Vpr in the absence of p6(gag)
    • Accola MA, Ohagen A, Gottlinger HG. 2000. Isolation of human immunodeficiency virus type 1 cores: retention of Vpr in the absence of p6(gag). J Virol 74:6198-6202. http://dx.doi.org/10.1128/JVI.74.13.6198-6202.2000.
    • (2000) J Virol , vol.74 , pp. 6198-6202
    • Accola, M.A.1    Ohagen, A.2    Gottlinger, H.G.3
  • 67
    • 0037388765 scopus 로고    scopus 로고
    • Structural organization of authentic, mature HIV-1 virions and cores
    • Briggs JA, Wilk T, Welker R, Kräusslich HG, Fuller SD. 2003. Structural organization of authentic, mature HIV-1 virions and cores. EMBO J 22: 1707-1715. http://dx.doi.org/10.1093/emboj/cdg143.
    • (2003) EMBO J , vol.22 , pp. 1707-1715
    • Briggs, J.A.1    Wilk, T.2    Welker, R.3    Kräusslich, H.G.4    Fuller, S.D.5
  • 68
    • 0033958427 scopus 로고    scopus 로고
    • Biochemical and structural analysis of isolated mature cores of human immunodeficiency virus type 1
    • Welker R, Hohenberg H, Tessmer U, Huckhagel C, Kräusslich HG. 2000. Biochemical and structural analysis of isolated mature cores of human immunodeficiency virus type 1. J Virol 74:1168-1177. http://dx.doi.org/10.1128/JVI.74.3.1168-1177.2000.
    • (2000) J Virol , vol.74 , pp. 1168-1177
    • Welker, R.1    Hohenberg, H.2    Tessmer, U.3    Huckhagel, C.4    Kräusslich, H.G.5
  • 69
    • 84911879495 scopus 로고    scopus 로고
    • Global changes in the RNA binding specificity of HIV-1 gag regulate virion genesis
    • Kutluay SB, Zang T, Blanco-Melo D, Powell C, Jannain D, Errando M, Bieniasz PD. 2014. Global changes in the RNA binding specificity of HIV-1 gag regulate virion genesis. Cell 159:1096-1109. http://dx.doi.org/10.1016/j.cell.2014.09.057.
    • (2014) Cell , vol.159 , pp. 1096-1109
    • Kutluay, S.B.1    Zang, T.2    Blanco-Melo, D.3    Powell, C.4    Jannain, D.5    Errando, M.6    Bieniasz, P.D.7
  • 70
    • 84870340629 scopus 로고    scopus 로고
    • The choreography of HIV-1 proteolytic processing and virion assembly
    • Lee S-K, Potempa M, Swanstrom R. 2012. The choreography of HIV-1 proteolytic processing and virion assembly. J Biol Chem 287:40867-40874. http://dx.doi.org/10.1074/jbc. R112.399444.
    • (2012) J Biol Chem , vol.287 , pp. 40867-40874
    • Lee, S.-K.1    Potempa, M.2    Swanstrom, R.3
  • 71
    • 0032930797 scopus 로고    scopus 로고
    • Assembly and analysis of conical models for the HIV-1 core
    • Ganser BK, Li S, Klishko VY, Finch JT, Sundquist WI. 1999. Assembly and analysis of conical models for the HIV-1 core. Science 283:80-83. http://dx.doi.org/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
  • 72
    • 39049108146 scopus 로고    scopus 로고
    • RSV capsid polymorphism correlates with polymerization efficiency and envelope glycoprotein content: implications that nucleation controls morphogenesis
    • Butan C, Winkler DC, Heymann JB, Craven RC, Steven AC. 2008. RSV capsid polymorphism correlates with polymerization efficiency and envelope glycoprotein content: implications that nucleation controls morphogenesis. J Mol Biol 376:1168-1181. http://dx.doi.org/10.1016/j.jmb.2007.12.003.
    • (2008) J Mol Biol , vol.376 , pp. 1168-1181
    • Butan, C.1    Winkler, D.C.2    Heymann, J.B.3    Craven, R.C.4    Steven, A.C.5
  • 73
    • 0029055551 scopus 로고
    • Isolation of high-affinity RNA ligands to HIV-1 integrase from a random pool
    • Allen P, Worland S, Gold L. 1995. Isolation of high-affinity RNA ligands to HIV-1 integrase from a random pool. Virology 209:327-336. http://dx.doi.org/10.1006/viro.1995.1264.
    • (1995) Virology , vol.209 , pp. 327-336
    • Allen, P.1    Worland, S.2    Gold, L.3
  • 74
    • 84901611889 scopus 로고    scopus 로고
    • HIV-1 B-subtype capsid protein: a characterization of amino acid's conservation and its significant association with integrase signatures
    • Dimonte S, Babakir-Mina M, Aquaro S. 2014. HIV-1 B-subtype capsid protein: a characterization of amino acid's conservation and its significant association with integrase signatures. Virus Genes 48:429-437. http://dx.doi.org/10.1007/s11262-014-1039-y.
    • (2014) Virus Genes , vol.48 , pp. 429-437
    • Dimonte, S.1    Babakir-Mina, M.2    Aquaro, S.3


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