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Volumn 210, Issue 4, 2015, Pages 629-646

Live-cell observation of cytosolic HIV-1 assembly onset reveals RNA-interacting Gag oligomers

Author keywords

[No Author keywords available]

Indexed keywords

GAG PROTEIN; MONOMER; OLIGOMER; RNA;

EID: 84964697416     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201504006     Document Type: Article
Times cited : (77)

References (84)
  • 1
    • 0022495870 scopus 로고
    • Production of acquired immunodeficiency syndrome-associated retrovirus in human and nonhuman cells transfected with an infectious molecular clone
    • Adachi, A., H.E. Gendelman, S. Koenig, T. Folks, R. Willey, A. Rabson, and M.A. Martin. 1986. Production of acquired immunodeficiency syndrome-associated retrovirus in human and nonhuman cells transfected with an infectious molecular clone. J. Virol. 59:284-291.
    • (1986) J. Virol , vol.59 , pp. 284-291
    • Adachi, A.1    Gendelman, H.E.2    Koenig, S.3    Folks, T.4    Willey, R.5    Rabson, A.6    Martin, M.A.7
  • 3
    • 84966663179 scopus 로고    scopus 로고
    • 6th edition. Becker & Hickl GmbH, Berlin
    • Becker, W. 2014. The bh TCSPC Handbook. 6th edition. Becker & Hickl GmbH, Berlin. 782 pp.
    • (2014) The bh TCSPC Handbook , pp. 782
    • Becker, W.1
  • 4
    • 0000310530 scopus 로고    scopus 로고
    • Time-resolved detection and identification of single analyte molecules in microcapillaries by time-correlated single-photon counting (TCSPC)
    • Becker, W., H. Hickl, C. Zander, K.H. Drexhage, M. Sauer, S. Siebert, and J. Wolfrum. 1999. Time-resolved detection and identification of single analyte molecules in microcapillaries by time-correlated single-photon counting (TCSPC). Rev. Sci. Instrum. 70:1835. http://dx.doi.org/10.1063/1.1149677
    • (1999) Rev. Sci. Instrum , vol.70 , pp. 1835
    • Becker, W.1    Hickl, H.2    Zander, C.3    Drexhage, K.H.4    Sauer, M.5    Siebert, S.6    Wolfrum, J.7
  • 5
    • 84875233720 scopus 로고    scopus 로고
    • HIV Gag polyprotein: processing and early viral particle assembly
    • Bell, N.M., and A.M. Lever. 2013. HIV Gag polyprotein: processing and early viral particle assembly. Trends Microbiol. 21:136-144. http://dx.doi.org/10.1016/j.tim.2012.11.006
    • (2013) Trends Microbiol , vol.21 , pp. 136-144
    • Bell, N.M.1    Lever, A.M.2
  • 6
    • 80051713783 scopus 로고    scopus 로고
    • The molecular architecture of HIV
    • Briggs, J.A.G., and H.G. Kräusslich. 2011. The molecular architecture of HIV. J. Mol. Biol. 410:491-500. http://dx.doi.org/10.1016/j.jmb.2011.04.021
    • (2011) J. Mol. Biol , vol.410 , pp. 491-500
    • Briggs, J.A.G.1    Kräusslich, H.G.2
  • 8
    • 80051718223 scopus 로고    scopus 로고
    • Molecular determinants that regulate plasma membrane association of HIV-1 Gag
    • Chukkapalli, V., and A. Ono. 2011. Molecular determinants that regulate plasma membrane association of HIV-1 Gag. J. Mol. Biol. 410:512-524. http://dx.doi.org/10.1016/j.jmb.2011.04.015
    • (2011) J. Mol. Biol , vol.410 , pp. 512-524
    • Chukkapalli, V.1    Ono, A.2
  • 9
    • 76549119994 scopus 로고    scopus 로고
    • Opposing mechanisms involving RNA and lipids regulate HIV-1 Gag membrane binding through the highly basic region of the matrix domain
    • Chukkapalli, V., S.J. Oh, and A. Ono. 2010. Opposing mechanisms involving RNA and lipids regulate HIV-1 Gag membrane binding through the highly basic region of the matrix domain. Proc. Natl. Acad. Sci. USA. 107:1600-1605. http://dx.doi.org/10.1073/pnas.0908661107
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 1600-1605
    • Chukkapalli, V.1    Oh, S.J.2    Ono, A.3
  • 10
    • 0034011267 scopus 로고    scopus 로고
    • Basic residues in human immunodeficiency virus type 1 nucleocapsid promote virion assembly via interaction with RNA
    • Cimarelli, A., S. Sandin, S. Höglund, and J. Luban. 2000. Basic residues in human immunodeficiency virus type 1 nucleocapsid promote virion assembly via interaction with RNA. J. Virol. 74:3046-3057. http://dx.doi.org/10.1128/JVI.74.7.3046-3057.2000
    • (2000) J. Virol , vol.74 , pp. 3046-3057
    • Cimarelli, A.1    Sandin, S.2    Höglund, S.3    Luban, J.4
  • 12
    • 79251596756 scopus 로고    scopus 로고
    • HIV-1 Gag extension: conformational changes require simultaneous interaction with membrane and nucleic acid
    • Datta, S.A., F. Heinrich, S. Raghunandan, S. Krueger, J.E. Curtis, A. Rein, and H. Nanda. 2011. HIV-1 Gag extension: conformational changes require simultaneous interaction with membrane and nucleic acid. J. Mol. Biol. 406:205-214. http://dx.doi.org/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    Nanda, H.7
  • 13
    • 0346373724 scopus 로고    scopus 로고
    • A novel fluorescence resonance energy transfer assay demonstrates that the human immunodeficiency virus type 1 Pr55Gag I domain mediates Gag-Gag interactions
    • Derdowski, A., L. Ding, and P. Spearman. 2004. A novel fluorescence resonance energy transfer assay demonstrates that the human immunodeficiency virus type 1 Pr55Gag I domain mediates Gag-Gag interactions. J. Virol. 78:1230-1242. http://dx.doi.org/10.1128/JVI.78.3.1230-1242.2004
    • (2004) J. Virol , vol.78 , pp. 1230-1242
    • Derdowski, A.1    Ding, L.2    Spearman, P.3
  • 14
    • 23244441649 scopus 로고    scopus 로고
    • Measuring fast dynamics in solutions and cells with a laser scanning microscope
    • Digman, M.A., C.M. Brown, P. Sengupta, P.W. Wiseman, A.R. Horwitz, and E. Gratton. 2005. Measuring fast dynamics in solutions and cells with a laser scanning microscope. Biophys. J. 89:1317-1327. http://dx.doi.org/10.1529/biophysj.105.062836
    • (2005) Biophys. J , vol.89 , pp. 1317-1327
    • Digman, M.A.1    Brown, C.M.2    Sengupta, P.3    Wiseman, P.W.4    Horwitz, A.R.5    Gratton, E.6
  • 15
    • 44049105523 scopus 로고    scopus 로고
    • Mapping the number of molecules and brightness in the laser scanning microscope
    • Digman, M.A., R. Dalal, A.F. Horwitz, and E. Gratton. 2008. Mapping the number of molecules and brightness in the laser scanning microscope. Biophys. J. 94:2320-2332. http://dx.doi.org/10.1529/biophysj.107.114645
    • (2008) Biophys. J , vol.94 , pp. 2320-2332
    • Digman, M.A.1    Dalal, R.2    Horwitz, A.F.3    Gratton, E.4
  • 16
    • 58849141678 scopus 로고    scopus 로고
    • Detecting protein complexes in living cells from laser scanning confocal image sequences by the cross correlation raster image spectroscopy method
    • Digman, M.A., P.W. Wiseman, A.R. Horwitz, and E. Gratton. 2009. Detecting protein complexes in living cells from laser scanning confocal image sequences by the cross correlation raster image spectroscopy method. Biophys. J. 96:707-716. http://dx.doi.org/10.1016/j.bpj.2008.09.051
    • (2009) Biophys. J , vol.96 , pp. 707-716
    • Digman, M.A.1    Wiseman, P.W.2    Horwitz, A.R.3    Gratton, E.4
  • 17
    • 84880675693 scopus 로고    scopus 로고
    • Fast spatiotemporal correlation spectroscopy to determine protein lateral diffusion laws in live cell membranes
    • Di Rienzo, C., E. Gratton, F. Beltram, and F. Cardarelli. 2013. Fast spatiotemporal correlation spectroscopy to determine protein lateral diffusion laws in live cell membranes. Proc. Natl. Acad. Sci. USA. 110:12307-12312. http://dx.doi.org/10.1073/pnas.1222097110
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 12307-12312
    • Di Rienzo, C.1    Gratton, E.2    Beltram, F.3    Cardarelli, F.4
  • 18
    • 84924157256 scopus 로고    scopus 로고
    • Role of the nucleocapsid domain in HIV-1 Gag oligomerization and trafficking to the plasma membrane: a fluorescence lifetime imaging microscopy investigation
    • El Meshri, S.E., D. Dujardin, J. Godet, L. Richert, C. Boudier, J.L. Darlix, P. Didier, Y. Mély, and H. de Rocquigny. 2015. Role of the nucleocapsid domain in HIV-1 Gag oligomerization and trafficking to the plasma membrane: a fluorescence lifetime imaging microscopy investigation. J. Mol. Biol. 427(Pt. B):1480-1494. http://dx.doi.org/10.1016/j.jmb.2015.01.015
    • (2015) J. Mol. Biol , vol.427 , Issue.PART. B , pp. 1480-1494
    • El Meshri, S.E.1    Dujardin, D.2    Godet, J.3    Richert, L.4    Boudier, C.5    Darlix, J.L.6    Didier, P.7    Mély, Y.8    de Rocquigny, H.9
  • 19
    • 79953896583 scopus 로고    scopus 로고
    • Characterization of cytoplasmic Gag-gag interactions by dual-color z-scan fluorescence fluctuation spectroscopy
    • Fogarty, K.H., Y. Chen, I.F. Grigsby, P.J. Macdonald, E.M. Smith, J.L. Johnson, J.M. Rawson, L.M. Mansky, and J.D. Mueller. 2011a. Characterization of cytoplasmic Gag-gag interactions by dual-color z-scan fluorescence fluctuation spectroscopy. Biophys. J. 100:1587-1595. http://dx.doi.org/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    Rawson, J.M.7    Mansky, L.M.8    Mueller, J.D.9
  • 20
    • 79959660777 scopus 로고    scopus 로고
    • New insights into HTLV-1 particle structure, assembly, and Gag-Gag interactions in living cells
    • Fogarty, K.H., W. Zhang, I.F. Grigsby, J.L. Johnson, Y. Chen, J.D. Mueller, and L.M. Mansky. 2011b. New insights into HTLV-1 particle structure, assembly, and Gag-Gag interactions in living cells. Viruses. 3:770-793. http://dx.doi.org/10.3390/v3060770
    • (2011) Viruses , vol.3 , pp. 770-793
    • Fogarty, K.H.1    Zhang, W.2    Grigsby, I.F.3    Johnson, J.L.4    Chen, Y.5    Mueller, J.D.6    Mansky, L.M.7
  • 21
    • 84895925747 scopus 로고    scopus 로고
    • Interrelationship between cytoplasmic retroviral Gag concentration and Gag-membrane association
    • Fogarty, K.H., S. Berk, I.F. Grigsby, Y. Chen, L.M. Mansky, and J.D. Mueller. 2014. Interrelationship between cytoplasmic retroviral Gag concentration and Gag-membrane association. J. Mol. Biol. 426:1611-1624. http://dx.doi.org/10.1016/j.jmb.2013.11.025
    • (2014) 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
  • 22
    • 0028234481 scopus 로고
    • Single amino acid changes in the human immunodeficiency virus type 1 matrix protein block virus particle production
    • Freed, E.O., J.M. Orenstein, A.J. Buckler-White, and M.A. Martin. 1994. Single amino acid changes in the human immunodeficiency virus type 1 matrix protein block virus particle production. J. Virol. 68:5311-5320.
    • (1994) J. Virol , vol.68 , pp. 5311-5320
    • Freed, E.O.1    Orenstein, J.M.2    Buckler-White, A.J.3    Martin, M.A.4
  • 25
    • 34548768339 scopus 로고    scopus 로고
    • Intracellular HIV-1 Gag localization is impaired by mutations in the nucleocapsid zinc fingers
    • Grigorov, B., D. Décimo, F. Smagulova, C. Péchoux, M. Mougel, D. Muriaux, and J.L. Darlix. 2007. Intracellular HIV-1 Gag localization is impaired by mutations in the nucleocapsid zinc fingers. Retrovirology. 4:54. http://dx.doi.org/10.1186/1742-4690-4-54
    • (2007) Retrovirology , vol.4 , pp. 54
    • Grigorov, B.1    Décimo, D.2    Smagulova, F.3    Péchoux, C.4    Mougel, M.5    Muriaux, D.6    Darlix, J.L.7
  • 26
    • 0032506222 scopus 로고    scopus 로고
    • Dynamics of fluorescence fluctuations in green fluorescent protein observed by fluorescence correlation spectroscopy
    • Haupts, U., S. Maiti, P. Schwille, and W.W. Webb. 1998. Dynamics of fluorescence fluctuations in green fluorescent protein observed by fluorescence correlation spectroscopy. Proc. Natl. Acad. Sci. USA. 95:13573-13578. http://dx.doi.org/10.1073/pnas.95.23.13573
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 13573-13578
    • Haupts, U.1    Maiti, S.2    Schwille, P.3    Webb, W.W.4
  • 27
    • 2242492943 scopus 로고
    • An automatic focus/hold system for optical microscopes
    • Hellen, E.H., and D. Axelrod. 1990. An automatic focus/hold system for optical microscopes. Rev. Sci. Instrum. 61:3722-3725. http://dx.doi.org/10.1063/1.1141542
    • (1990) Rev. Sci. Instrum , vol.61 , pp. 3722-3725
    • Hellen, E.H.1    Axelrod, D.2
  • 28
  • 29
    • 84882950477 scopus 로고    scopus 로고
    • Pulsed interleaved excitation fluctuation imaging
    • Hendrix, J., W. Schrimpf, M. Höller, and D.C. Lamb. 2013. Pulsed interleaved excitation fluctuation imaging. Biophys. J. 105:848-861. http://dx.doi.org/10.1016/j.bpj.2013.05.059
    • (2013) Biophys. J , vol.105 , pp. 848-861
    • Hendrix, J.1    Schrimpf, W.2    Höller, M.3    Lamb, D.C.4
  • 30
    • 0042322244 scopus 로고    scopus 로고
    • The photon counting histogram in fluorescence fluctuation spectroscopy with non-ideal photodetectors
    • Hillesheim, L.N., and J.D. Müller. 2003. The photon counting histogram in fluorescence fluctuation spectroscopy with non-ideal photodetectors. Biophys. J. 85:1948-1958. http://dx.doi.org/10.1016/S0006-3495(03) 74622-0
    • (2003) Biophys. J , vol.85 , pp. 1948-1958
    • Hillesheim, L.N.1    Müller, J.D.2
  • 31
    • 84858025964 scopus 로고    scopus 로고
    • Fluorescence Correlation Spectroscopy: Principles and Developments
    • J. Brnjas-Kraljevic, and G. Pifat-Mrzljak, editors. Springer, Dordrecht, Netherlands
    • Ivanchenko, S., and D.C. Lamb. 2011. Fluorescence Correlation Spectroscopy: Principles and Developments. In Supramolecular Structure and Function. Vol. 10. J. Brnjas-Kraljevic, and G. Pifat-Mrzljak, editors. Springer, Dordrecht, Netherlands. 1-30.
    • (2011) Supramolecular Structure and Function , vol.10 , pp. 1-30
    • Ivanchenko, S.1    Lamb, D.C.2
  • 33
    • 78951492319 scopus 로고    scopus 로고
    • Matrix domain modulates HIV-1 Gag's nucleic acid chaperone activity via inositol phosphate binding
    • Jones, C.P., S.A. Datta, A. Rein, I. Rouzina, and K. Musier-Forsyth. 2011. Matrix domain modulates HIV-1 Gag's nucleic acid chaperone activity via inositol phosphate binding. J. Virol. 85:1594-1603. http://dx.doi.org/10.1128/JVI.01809-10
    • (2011) J. Virol , vol.85 , pp. 1594-1603
    • Jones, C.P.1    Datta, S.A.2    Rein, A.3    Rouzina, I.4    Musier-Forsyth, K.5
  • 34
    • 47049130164 scopus 로고    scopus 로고
    • Imaging the biogenesis of individual HIV-1 virions in live cells
    • Jouvenet, N., P.D. Bieniasz, and S.M. Simon. 2008. Imaging the biogenesis of individual HIV-1 virions in live cells. Nature. 454:236-240. http://dx.doi.org/10.1038/nature06998
    • (2008) Nature , vol.454 , pp. 236-240
    • Jouvenet, N.1    Bieniasz, P.D.2    Simon, S.M.3
  • 35
    • 73149122533 scopus 로고    scopus 로고
    • Imaging the interaction of HIV-1 genomes and Gag during assembly of individual viral particles
    • Jouvenet, N., S.M. Simon, and P.D. Bieniasz. 2009. Imaging the interaction of HIV-1 genomes and Gag during assembly of individual viral particles. Proc. Natl. Acad. Sci. USA. 106:19114-19119. http://dx.doi.org/10.1073/pnas.0907364106
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 19114-19119
    • Jouvenet, N.1    Simon, S.M.2    Bieniasz, P.D.3
  • 36
    • 84888318547 scopus 로고    scopus 로고
    • Absolute diffusion coefficients: Compilation of reference data for FCS calibration
    • Kapusta, P. 2010. Absolute diffusion coefficients: Compilation of reference data for FCS calibration. Picoquant Application Note. http://www.researchgate. net/publication/269278844_Absolute_Diffusion_Coefficients_ Compilation_of_Reference:Data_for_FCS_Calibration
    • (2010) Picoquant Application Note
    • Kapusta, P.1
  • 37
    • 25844507533 scopus 로고    scopus 로고
    • Determining protease activity in vivo by fluorescence cross-correlation analysis
    • Kohl, T., E. Haustein, and P. Schwille. 2005. Determining protease activity in vivo by fluorescence cross-correlation analysis. Biophys. J. 89:2770-2782. http://dx.doi.org/10.1529/biophysj.105.061127
    • (2005) Biophys. J , vol.89 , pp. 2770-2782
    • Kohl, T.1    Haustein, E.2    Schwille, P.3
  • 38
    • 79251506313 scopus 로고    scopus 로고
    • Analysis of the initiating events in HIV-1 particle assembly and genome packaging
    • Kutluay, S.B., and P.D. Bieniasz. 2010. Analysis of the initiating events in HIV-1 particle assembly and genome packaging. PLoS Pathog. 6:e1001200. http://dx.doi.org/10.1371/journal.ppat.1001200
    • (2010) PLoS Pathog , vol.6
    • Kutluay, S.B.1    Bieniasz, P.D.2
  • 39
    • 84911879495 scopus 로고    scopus 로고
    • Global changes in the RNA binding specificity of HIV-1 gag regulate virion genesis
    • Kutluay, S.B., T. Zang, D. Blanco-Melo, C. Powell, D. Jannain, M. Errando, and P.D. Bieniasz. 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
  • 40
    • 84897959539 scopus 로고    scopus 로고
    • Life of psi: how full-length HIV-1 RNAs become packaged genomes in the viral particles
    • Kuzembayeva, M., K. Dilley, L. Sardo, and W.S. Hu. 2014. Life of psi: how full-length HIV-1 RNAs become packaged genomes in the viral particles. Virology. 454-455:362-370. http://dx.doi.org/10.1016/j.virol.2014.01.019
    • (2014) Virology , vol.454-455 , pp. 362-370
    • Kuzembayeva, M.1    Dilley, K.2    Sardo, L.3    Hu, W.S.4
  • 41
    • 0033880469 scopus 로고    scopus 로고
    • Sensitivity enhancement in fluorescence correlation spectroscopy of multiple species using time-gated detection
    • Lamb, D.C., A. Schenk, C. Röcker, C. Scalfi-Happ, and G.U. Nienhaus. 2000. Sensitivity enhancement in fluorescence correlation spectroscopy of multiple species using time-gated detection. Biophys. J. 79:1129-1138. http://dx.doi.org/10.1016/S0006-3495(00)76366-1
    • (2000) Biophys. J , vol.79 , pp. 1129-1138
    • Lamb, D.C.1    Schenk, A.2    Röcker, C.3    Scalfi-Happ, C.4    Nienhaus, G.U.5
  • 42
    • 27844545215 scopus 로고    scopus 로고
    • Enhancing the sensitivity of fluorescence correlation spectroscopy by using time-correlated single photon counting
    • Lamb, D.C., B.K. Müller, and C. Bräuchle. 2005. Enhancing the sensitivity of fluorescence correlation spectroscopy by using time-correlated single photon counting. Curr. Pharm. Biotechnol. 6:405-414. http://dx.doi.org/10.2174/138920105774370625
    • (2005) Curr. Pharm. Biotechnol , vol.6 , pp. 405-414
    • Lamb, D.C.1    Müller, B.K.2    Bräuchle, C.3
  • 43
    • 0141530039 scopus 로고    scopus 로고
    • Direct measurement of Gag-Gag interaction during retrovirus assembly with FRET and fluorescence correlation spectroscopy
    • Larson, D.R., Y.M. Ma, V.M. Vogt, and W.W. Webb. 2003. Direct measurement of Gag-Gag interaction during retrovirus assembly with FRET and fluorescence correlation spectroscopy. J. Cell Biol. 162:1233-1244. http://dx.doi.org/10.1083/jcb.200303200
    • (2003) J. Cell Biol , vol.162 , pp. 1233-1244
    • Larson, D.R.1    Ma, Y.M.2    Vogt, V.M.3    Webb, W.W.4
  • 44
    • 84881194293 scopus 로고    scopus 로고
    • Visualization of retrovirus budding with correlated light and electron microscopy
    • Larson, D.R., M.C. Johnson, W.W. Webb, and V.M. Vogt. 2005. Visualization of retrovirus budding with correlated light and electron microscopy. Proc. Natl. Acad. Sci. USA. 102:15453-15458. http://dx.doi.org/10.1073/pnas.0504812102
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 15453-15458
    • Larson, D.R.1    Johnson, M.C.2    Webb, W.W.3    Vogt, V.M.4
  • 45
    • 0032579806 scopus 로고    scopus 로고
    • Identification and characterization of virus assembly intermediate complexes in HIV-1-infected CD4+ T cells
    • Lee, Y.M., and X.F. Yu. 1998. Identification and characterization of virus assembly intermediate complexes in HIV-1-infected CD4+ T cells. Virology. 243:78-93. http://dx.doi.org/10.1006/viro.1998.9064
    • (1998) Virology , vol.243 , pp. 78-93
    • Lee, Y.M.1    Yu, X.F.2
  • 46
    • 0032990415 scopus 로고    scopus 로고
    • Formation of virus assembly intermediate complexes in the cytoplasm by wild-type and assembly-defective mutant human immunodeficiency virus type 1 and their association with membranes
    • Lee, Y.M., B. Liu, and X.F. Yu. 1999. Formation of virus assembly intermediate complexes in the cytoplasm by wild-type and assembly-defective mutant human immunodeficiency virus type 1 and their association with membranes. J. Virol. 73:5654-5662.
    • (1999) J. Virol , vol.73 , pp. 5654-5662
    • Lee, Y.M.1    Liu, B.2    Yu, X.F.3
  • 47
    • 36349029236 scopus 로고    scopus 로고
    • Myristoylation is required for human immunodeficiency virus type 1 Gag-Gag multimerization in mammalian cells
    • Li, H., J. Dou, L. Ding, and P. Spearman. 2007. Myristoylation is required for human immunodeficiency virus type 1 Gag-Gag multimerization in mammalian cells. J. Virol. 81:12899-12910. http://dx.doi.org/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
  • 49
    • 19944384581 scopus 로고    scopus 로고
    • Single point mutations in the zinc finger motifs of the human immunodeficiency virus type 1 nucleocapsid alter RNA binding specificities of the gag protein and enhance packaging and infectivity
    • Mark-Danieli, M., N. Laham, M. Kenan-Eichler, A. Castiel, D. Melamed, M. Landau, N.M. Bouvier, M.J. Evans, and E. Bacharach. 2005. Single point mutations in the zinc finger motifs of the human immunodeficiency virus type 1 nucleocapsid alter RNA binding specificities of the gag protein and enhance packaging and infectivity. J. Virol. 79:7756-7767. http://dx.doi.org/10.1128/JVI.79.12.7756-7767.2005
    • (2005) J. Virol , vol.79 , pp. 7756-7767
    • Mark-Danieli, M.1    Laham, N.2    Kenan-Eichler, M.3    Castiel, A.4    Melamed, D.5    Landau, M.6    Bouvier, N.M.7    Evans, M.J.8    Bacharach, E.9
  • 50
    • 84872112730 scopus 로고    scopus 로고
    • Wrapping up the bad news: HIV assembly and release
    • Meng, B., and A.M. Lever. 2013. Wrapping up the bad news: HIV assembly and release. Retrovirology. 10:5. http://dx.doi.org/10.1186/1742-4690-10-5
    • (2013) Retrovirology , vol.10 , pp. 5
    • Meng, B.1    Lever, A.M.2
  • 51
    • 0026585458 scopus 로고
    • Analysis of HIV particle formation using transient expression of subviral constructs in mammalian cells
    • Mergener, K., M. Fäcke, R. Welker, V. Brinkmann, H.R. Gelderblom, and H.G. Kräusslich. 1992. Analysis of HIV particle formation using transient expression of subviral constructs in mammalian cells. Virology. 186:25-39. http://dx.doi.org/10.1016/0042-6822(92)90058-W
    • (1992) Virology , vol.186 , pp. 25-39
    • Mergener, K.1    Fäcke, M.2    Welker, R.3    Brinkmann, V.4    Gelderblom, H.R.5    Kräusslich, H.G.6
  • 52
    • 4544232723 scopus 로고    scopus 로고
    • Construction and characterization of a fluorescently labeled infectious human immunodeficiency virus type 1 derivative
    • Müller, B., J. Daecke, O.T. Fackler, M.T. Dittmar, H. Zentgraf, and H.G. Kräusslich. 2004. Construction and characterization of a fluorescently labeled infectious human immunodeficiency virus type 1 derivative. J. Virol. 78:10803-10813. http://dx.doi.org/10.1128/JVI.78.19.10803-10813.2004
    • (2004) J. Virol , vol.78 , pp. 10803-10813
    • Müller, B.1    Daecke, J.2    Fackler, O.T.3    Dittmar, M.T.4    Zentgraf, H.5    Kräusslich, H.G.6
  • 53
    • 27744519499 scopus 로고    scopus 로고
    • Pulsed interleaved excitation
    • Müller, B.K., E. Zaychikov, C. Bräuchle, and D.C. Lamb. 2005. Pulsed interleaved excitation. Biophys. J. 89:3508-3522. http://dx.doi.org/10.1529/biophysj.105.064766
    • (2005) Biophys. J , vol.89 , pp. 3508-3522
    • Müller, B.K.1    Zaychikov, E.2    Bräuchle, C.3    Lamb, D.C.4
  • 54
    • 78751670345 scopus 로고    scopus 로고
    • Properties and functions of the nucleocapsid protein in virus assembly
    • Muriaux, D., and J.L. Darlix. 2010. Properties and functions of the nucleocapsid protein in virus assembly. RNA Biol. 7:744-753. http://dx.doi.org/10.4161/rna.7.6.14065
    • (2010) RNA Biol , vol.7 , pp. 744-753
    • Muriaux, D.1    Darlix, J.L.2
  • 55
    • 0035942236 scopus 로고    scopus 로고
    • RNA is a structural element in retrovirus particles
    • Muriaux, D., J. Mirro, D. Harvin, and A. Rein. 2001. RNA is a structural element in retrovirus particles. Proc. Natl. Acad. Sci. USA. 98:5246-5251. http://dx.doi.org/10.1073/pnas.091000398
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 5246-5251
    • Muriaux, D.1    Mirro, J.2    Harvin, D.3    Rein, A.4
  • 56
    • 0036138908 scopus 로고    scopus 로고
    • A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications
    • Nagai, T., K. Ibata, E.S. Park, M. Kubota, K. Mikoshiba, and A. Miyawaki. 2002. A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications. Nat. Biotechnol. 20:87-90. http://dx.doi.org/10.1038/nbt0102-87
    • (2002) Nat. Biotechnol , vol.20 , pp. 87-90
    • Nagai, T.1    Ibata, K.2    Park, E.S.3    Kubota, M.4    Mikoshiba, K.5    Miyawaki, A.6
  • 57
    • 0037225271 scopus 로고    scopus 로고
    • Time course of Gag protein assembly in HIV-1-infected cells: a study by immunoelectron microscopy
    • Nermut, M.V., W.H. Zhang, G. Francis, F. Ciampor, Y. Morikawa, and I.M. Jones. 2003. Time course of Gag protein assembly in HIV-1-infected cells: a study by immunoelectron microscopy. Virology. 305:219-227. http://dx.doi.org/10.1006/viro.2002.1692
    • (2003) Virology , vol.305 , pp. 219-227
    • Nermut, M.V.1    Zhang, W.H.2    Francis, G.3    Ciampor, F.4    Morikawa, Y.5    Jones, I.M.6
  • 59
    • 85027932076 scopus 로고    scopus 로고
    • Elements in HIV-1 Gag contributing to virus particle assembly
    • O'Carroll, I.P., F. Soheilian, A. Kamata, K. Nagashima, and A. Rein. 2013. Elements in HIV-1 Gag contributing to virus particle assembly. Virus Res. 171:341-345. http://dx.doi.org/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
  • 60
    • 6944255361 scopus 로고    scopus 로고
    • Phosphatidylinositol (4,5) bisphosphate regulates HIV-1 Gag targeting to the plasma membrane
    • Ono, A., S.D. Ablan, S.J. Lockett, K. Nagashima, and E.O. Freed. 2004. Phosphatidylinositol (4,5) bisphosphate regulates HIV-1 Gag targeting to the plasma membrane. Proc. Natl. Acad. Sci. USA. 101:14889-14894. http://dx.doi.org/10.1073/pnas.0405596101
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 14889-14894
    • Ono, A.1    Ablan, S.D.2    Lockett, S.J.3    Nagashima, K.4    Freed, E.O.5
  • 61
    • 77953567262 scopus 로고    scopus 로고
    • A two-step path to inclusion formation of huntingtin peptides revealed by number and brightness analysis
    • Ossato, G., M.A. Digman, C. Aiken, T. Lukacsovich, J.L. Marsh, and E. Gratton. 2010. A two-step path to inclusion formation of huntingtin peptides revealed by number and brightness analysis. Biophys. J. 98:3078-3085. http://dx.doi.org/10.1016/j.bpj.2010.02.058
    • (2010) Biophys. J , vol.98 , pp. 3078-3085
    • Ossato, G.1    Digman, M.A.2    Aiken, C.3    Lukacsovich, T.4    Marsh, J.L.5    Gratton, E.6
  • 62
    • 0038710633 scopus 로고    scopus 로고
    • Elimination of protease activity restores efficient virion production to a human immunodeficiency virus type 1 nucleocapsid deletion mutant
    • Ott, D.E., L.V. Coren, E.N. Chertova, T.D. Gagliardi, K. Nagashima, R.C. Sowder II, D.T. Poon, and R.J. Gorelick. 2003. Elimination of protease activity restores efficient virion production to a human immunodeficiency virus type 1 nucleocapsid deletion mutant. J. Virol. 77:5547-5556. http://dx.doi.org/10.1128/JVI.77.10.5547-5556.2003
    • (2003) J. Virol , vol.77 , pp. 5547-5556
    • Ott, D.E.1    Coren, L.V.2    Chertova, E.N.3    Gagliardi, T.D.4    Nagashima, K.5    Sowder, R.C.6    Poon, D.T.7    Gorelick, R.J.8
  • 63
    • 0028858759 scopus 로고
    • The central globular domain of the nucleocapsid protein of human immunodeficiency virus type 1 is critical for virion structure and infectivity
    • Ottmann, M., C. Gabus, and J.L. Darlix. 1995. The central globular domain of the nucleocapsid protein of human immunodeficiency virus type 1 is critical for virion structure and infectivity. J. Virol. 69:1778-1784.
    • (1995) J. Virol , vol.69 , pp. 1778-1784
    • Ottmann, M.1    Gabus, C.2    Darlix, J.L.3
  • 64
    • 33751229633 scopus 로고    scopus 로고
    • Microenvironment and effect of energy depletion in the nucleus analyzed by mobility of multiple oligomeric EGFPs
    • Pack, C., K. Saito, M. Tamura, and M. Kinjo. 2006. Microenvironment and effect of energy depletion in the nucleus analyzed by mobility of multiple oligomeric EGFPs. Biophys. J. 91:3921-3936. http://dx.doi.org/10.1529/biophysj.105.079467
    • (2006) Biophys. J , vol.91 , pp. 3921-3936
    • Pack, C.1    Saito, K.2    Tamura, M.3    Kinjo, M.4
  • 65
    • 0027217936 scopus 로고
    • Quantitation of membrane receptor distributions by image correlation spectroscopy: concept and application
    • Petersen, N.O., P.L. Höddelius, P.W. Wiseman, O. Seger, and K.E. Magnusson. 1993. Quantitation of membrane receptor distributions by image correlation spectroscopy: concept and application. Biophys. J. 65:1135-1146. http://dx.doi.org/10.1016/S0006-3495(93)81173-1
    • (1993) Biophys. J , vol.65 , pp. 1135-1146
    • Petersen, N.O.1    Höddelius, P.L.2    Wiseman, P.W.3    Seger, O.4    Magnusson, K.E.5
  • 66
    • 0029817879 scopus 로고    scopus 로고
    • Charged amino acid residues of human immunodeficiency virus type 1 nucleocapsid p7 protein involved in RNA packaging and infectivity
    • Poon, D.T., J. Wu, and A. Aldovini. 1996. Charged amino acid residues of human immunodeficiency virus type 1 nucleocapsid p7 protein involved in RNA packaging and infectivity. J. Virol. 70:6607-6616.
    • (1996) J. Virol , vol.70 , pp. 6607-6616
    • Poon, D.T.1    Wu, J.2    Aldovini, A.3
  • 68
    • 0035778150 scopus 로고    scopus 로고
    • Fluorescence Correlation Spectroscopy-Theory and Applications
    • Springer-Verlag, Berlin
    • Rigler, R., and E. Elson, editors. 2001. Fluorescence Correlation Spectroscopy-Theory and Applications. Springer Series in Chemical Physics. Vol. 65. Springer-Verlag, Berlin.
    • (2001) Springer Series in Chemical Physics , vol.65
    • Rigler, R.1    Elson, E.2
  • 69
    • 0025793277 scopus 로고
    • Versatile eukaryotic vectors for strong and constitutive transient and stable gene expression
    • Rittner, K., H. Stoeppler, M. Pawlita, and G. Sczakiel. 1991. Versatile eukaryotic vectors for strong and constitutive transient and stable gene expression. Methods Mol. Cell. Biol. 2:176-181.
    • (1991) Methods Mol. Cell. Biol , vol.2 , pp. 176-181
    • Rittner, K.1    Stoeppler, H.2    Pawlita, M.3    Sczakiel, G.4
  • 70
    • 0025744626 scopus 로고
    • Functional domains of HIV-1 gag-polyprotein expressed in baculovirus-infected cells
    • Royer, M., M. Cerutti, B. Gay, S.S. Hong, G. Devauchelle, and P. Boulanger. 1991. Functional domains of HIV-1 gag-polyprotein expressed in baculovirus-infected cells. Virology. 184:417-422. http://dx.doi.org/10.1016/0042-6822(91)90861-5
    • (1991) Virology , vol.184 , pp. 417-422
    • Royer, M.1    Cerutti, M.2    Gay, B.3    Hong, S.S.4    Devauchelle, G.5    Boulanger, P.6
  • 71
    • 34249939912 scopus 로고    scopus 로고
    • Selective and nonselective packaging of cellular RNAs in retrovirus particles
    • Rulli, S.J., Jr., C.S. Hibbert, J. Mirro, T. Pederson, S. Biswal, and A. Rein. 2007. Selective and nonselective packaging of cellular RNAs in retrovirus particles. J. Virol. 81:6623-6631. http://dx.doi.org/10.1128/JVI.02833-06
    • (2007) J. Virol , vol.81 , pp. 6623-6631
    • Rulli, S.J.1    Hibbert, C.S.2    Mirro, J.3    Pederson, T.4    Biswal, S.5    Rein, A.6
  • 72
    • 33746625935 scopus 로고    scopus 로고
    • Structural basis for targeting HIV-1 Gag proteins to the plasma membrane for virus assembly
    • Saad, J.S., J. Miller, J. Tai, A. Kim, R.H. Ghanam, and M.F. Summers. 2006. Structural basis for targeting HIV-1 Gag proteins to the plasma membrane for virus assembly. Proc. Natl. Acad. Sci. USA. 103:11364-11369. http://dx.doi.org/10.1073/pnas.0602818103
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 11364-11369
    • Saad, J.S.1    Miller, J.2    Tai, J.3    Kim, A.4    Ghanam, R.H.5    Summers, M.F.6
  • 74
    • 50049091709 scopus 로고    scopus 로고
    • Structure of the myristylated human immunodeficiency virus type 2 matrix protein and the role of phosphatidylinositol-(4,5)-bisphosphate in membrane targeting
    • Saad, J.S., S.D. Ablan, R.H. Ghanam, A. Kim, K. Andrews, K. Nagashima, F. Soheilian, E.O. Freed, and M.F. Summers. 2008. Structure of the myristylated human immunodeficiency virus type 2 matrix protein and the role of phosphatidylinositol-(4,5)-bisphosphate in membrane targeting. J. Mol. Biol. 382:434-447. http://dx.doi.org/10.1016/j.jmb.2008.07.027
    • (2008) J. Mol. Biol , vol.382 , pp. 434-447
    • Saad, J.S.1    Ablan, S.D.2    Ghanam, R.H.3    Kim, A.4    Andrews, K.5    Nagashima, K.6    Soheilian, F.7    Freed, E.O.8    Summers, M.F.9
  • 75
    • 5444240958 scopus 로고    scopus 로고
    • Direct detection of caspase-3 activation in single live cells by cross-correlation analysis
    • Saito, K., I. Wada, M. Tamura, and M. Kinjo. 2004. Direct detection of caspase-3 activation in single live cells by cross-correlation analysis. Biochem. Biophys. Res. Commun. 324:849-854. http://dx.doi.org/10.1016/j.bbrc.2004.09.126
    • (2004) Biochem. Biophys. Res. Commun , vol.324 , pp. 849-854
    • Saito, K.1    Wada, I.2    Tamura, M.3    Kinjo, M.4
  • 76
    • 84924189026 scopus 로고    scopus 로고
    • Structure of the immature HIV-1 capsid in intact virus particles at 8.8 Å resolution
    • Schur, F.K., W.J. Hagen, M. Rumlová, T. Ruml, B. Müller, H.G. Kräusslich, and J.A. Briggs. 2015. Structure of the immature HIV-1 capsid in intact virus particles at 8.8 Å resolution. Nature. 517:505-508. http://dx.doi.org/10.1038/nature13838
    • (2015) Nature , vol.517 , pp. 505-508
    • Schur, F.K.1    Hagen, W.J.2    Rumlová, M.3    Ruml, T.4    Müller, B.5    Kräusslich, H.G.6    Briggs, J.A.7
  • 77
    • 0031795289 scopus 로고    scopus 로고
    • Diffusion of transferrin receptor clusters
    • Srivastava, M., and N.O. Petersen. 1998. Diffusion of transferrin receptor clusters. Biophys. Chem. 75:201-211. http://dx.doi.org/10.1016/S0301-4622(98)00206-3
    • (1998) Biophys. Chem , vol.75 , pp. 201-211
    • Srivastava, M.1    Petersen, N.O.2
  • 79
    • 0032536896 scopus 로고    scopus 로고
    • Proteolytic refolding of the HIV-1 capsid protein amino-terminus facilitates viral core assembly
    • von Schwedler, U.K., T.L. Stemmler, V.Y. Klishko, S. Li, K.H. Albertine, D.R. Davis, and W.I. Sundquist. 1998. Proteolytic refolding of the HIV-1 capsid protein amino-terminus facilitates viral core assembly. EMBO J. 17:1555-1568. http://dx.doi.org/10.1093/emboj/17.6.1555
    • (1998) EMBO J , vol.17 , pp. 1555-1568
    • von Schwedler, U.K.1    Stemmler, T.L.2    Klishko, V.Y.3    Li, S.4    Albertine, K.H.5    Davis, D.R.6    Sundquist, W.I.7
  • 80
    • 84855600681 scopus 로고    scopus 로고
    • HIV type 1 Gag as a target for antiviral therapy
    • Waheed, A.A., and E.O. Freed. 2012. HIV type 1 Gag as a target for antiviral therapy. AIDS Res. Hum. Retroviruses. 28:54-75. http://dx.doi.org/10.1089/aid.2011.0230
    • (2012) AIDS Res. Hum. Retroviruses , vol.28 , pp. 54-75
    • Waheed, A.A.1    Freed, E.O.2
  • 81
    • 0036106455 scopus 로고    scopus 로고
    • Analysis of ligand binding by two-colour fluorescence cross-correlation spectroscopy
    • Weidemann, T., M. Wachsmuth, M. Tewes, K. Rippe, and J. Langowski. 2002. Analysis of ligand binding by two-colour fluorescence cross-correlation spectroscopy. Single Mol. 3:49-61. http://dx.doi.org/10.1002/1438-5171(200204)3:149::AID-SIMO493.0.CO;2-T
    • (2002) Single Mol , vol.3 , pp. 49-61
    • Weidemann, T.1    Wachsmuth, M.2    Tewes, M.3    Rippe, K.4    Langowski, J.5
  • 82
    • 0033770633 scopus 로고    scopus 로고
    • Twophoton image correlation spectroscopy and image cross-correlation spectroscopy
    • Wiseman, P.W., J.A. Squier, M.H. Ellisman, and K.R. Wilson. 2000. Twophoton image correlation spectroscopy and image cross-correlation spectroscopy. J. Microsc. 200:14-25. http://dx.doi.org/10.1046/j.1365-2818.2000.00736.x
    • (2000) J. Microsc , vol.200 , pp. 14-25
    • Wiseman, P.W.1    Squier, J.A.2    Ellisman, M.H.3    Wilson, K.R.4
  • 83
    • 10944269216 scopus 로고    scopus 로고
    • Spatial mapping of integrin interactions and dynamics during cell migration by image correlation microscopy
    • Wiseman, P.W., C.M. Brown, D.J. Webb, B. Hebert, N.L. Johnson, J.A. Squier, M.H. Ellisman, and A.F. Horwitz. 2004. Spatial mapping of integrin interactions and dynamics during cell migration by image correlation microscopy. J. Cell Sci. 117:5521-5534. http://dx.doi.org/10.1242/jcs.01416
    • (2004) J. Cell Sci , vol.117 , pp. 5521-5534
    • Wiseman, P.W.1    Brown, C.M.2    Webb, D.J.3    Hebert, B.4    Johnson, N.L.5    Squier, J.A.6    Ellisman, M.H.7    Horwitz, A.F.8
  • 84
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells
    • Zacharias, D.A., J.D. Violin, A.C. Newton, and R.Y. Tsien. 2002. Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells. Science. 296:913-916. http://dx.doi.org/10.1126/science.1068539
    • (2002) Science , vol.296 , pp. 913-916
    • Zacharias, D.A.1    Violin, J.D.2    Newton, A.C.3    Tsien, R.Y.4


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