메뉴 건너뛰기




Volumn 4, Issue 3, 1998, Pages 138-143

HIV-1 nuclear import: Matrix protein is back on center stage, this time together with Vpr

Author keywords

[No Author keywords available]

Indexed keywords

MATRIX PROTEIN;

EID: 0031902773     PISSN: 10761551     EISSN: None     Source Type: Journal    
DOI: 10.1007/bf03401911     Document Type: Review
Times cited : (27)

References (51)
  • 1
    • 0028055281 scopus 로고
    • Passage through mitosis is required for oncoretroviruses but not for the human immunodeficiency virus
    • Lewis PF, Emerman M. (1994) Passage through mitosis is required for oncoretroviruses but not for the human immunodeficiency virus. J. Virol. 68: 510-516.
    • (1994) J. Virol. , vol.68 , pp. 510-516
    • Lewis, P.F.1    Emerman, M.2
  • 2
    • 0027158091 scopus 로고
    • Integration of murine leukemia virus DNA depends on mitosis
    • Roe T, Reynolds TC, Yu G, Brown PO. (1993) Integration of murine leukemia virus DNA depends on mitosis. EMBO J. 12: 2099-2108.
    • (1993) EMBO J. , vol.12 , pp. 2099-2108
    • Roe, T.1    Reynolds, T.C.2    Yu, G.3    Brown, P.O.4
  • 3
    • 0028239060 scopus 로고
    • The Vpr protein of human immunodeficiency virus type 1 influences nuclear localization of viral nucleic acids in nondividing host cells
    • Heinzinger NK, Bukrinsky MI, Haggerty SA, et al. (1994) The Vpr protein of human immunodeficiency virus type 1 influences nuclear localization of viral nucleic acids in nondividing host cells. Proc. Natl. Acad. Sci. USA 91: 7311-7315.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7311-7315
    • Heinzinger, N.K.1    Bukrinsky, M.I.2    Haggerty, S.A.3
  • 4
    • 0028234528 scopus 로고
    • The nuclear localization signal of the matrix protein of human immunodeficiency virus type 1 allows the establishment of infection in macrophages and quiescent T lymphocytes
    • von Schwedler U, Kornbluth RS, Trono D. (1994) The nuclear localization signal of the matrix protein of human immunodeficiency virus type 1 allows the establishment of infection in macrophages and quiescent T lymphocytes. Proc. Natl. Acad. Sci. USA 91: 6992-6996.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6992-6996
    • Von Schwedler, U.1    Kornbluth, R.S.2    Trono, D.3
  • 5
    • 0028283854 scopus 로고
    • HIV-1 infection of non-dividing cells
    • Emerman M, Bukrinsky M, Stevenson M. (1994) HIV-1 infection of non-dividing cells. Nature 369: 107-108.
    • (1994) Nature , vol.369 , pp. 107-108
    • Emerman, M.1    Bukrinsky, M.2    Stevenson, M.3
  • 6
    • 0026770379 scopus 로고
    • Active nuclear import of human immunodeficiency virus type 1 preintegration complexes
    • Bukrinsky MI, Sharova N, Dempsey MP, et al. (1992) Active nuclear import of human immunodeficiency virus type 1 preintegration complexes. Proc. Natl. Acad. Sci. USA 89: 6580-6584.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6580-6584
    • Bukrinsky, M.I.1    Sharova, N.2    Dempsey, M.P.3
  • 7
    • 0025949412 scopus 로고
    • Nuclear targeting sequences-a consensus?
    • Dingwall C, Laskey RA. (1991) Nuclear targeting sequences-a consensus? Trends Biochem. Sci. 16: 478-481.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 478-481
    • Dingwall, C.1    Laskey, R.A.2
  • 8
    • 0026042170 scopus 로고
    • Cytosolic proteins that specifically bind nuclear location signals are receptors for nuclear import
    • Adam SA, Gerace L. (1991) Cytosolic proteins that specifically bind nuclear location signals are receptors for nuclear import. Cell 66: 837-847.
    • (1991) Cell , vol.66 , pp. 837-847
    • Adam, S.A.1    Gerace, L.2
  • 9
    • 0029278621 scopus 로고
    • Two different subunits of importin cooperate to recognize nuclear localization signals and bind them to the nuclear envelope
    • Gorlich D, Kostka S, Kraft R, et al. (1995) Two different subunits of importin cooperate to recognize nuclear localization signals and bind them to the nuclear envelope. Curr. Biol. 5: 383-392.
    • (1995) Curr. Biol. , vol.5 , pp. 383-392
    • Gorlich, D.1    Kostka, S.2    Kraft, R.3
  • 10
    • 0029132794 scopus 로고
    • The nuclear pore-targeting complex binds to nuclear pores after association with a karyophile
    • Imamoto N, Shimamoto T, Kose S, et al. (1995) The nuclear pore-targeting complex binds to nuclear pores after association with a karyophile. FEBS Lett. 368: 415-419.
    • (1995) FEBS Lett. , vol.368 , pp. 415-419
    • Imamoto, N.1    Shimamoto, T.2    Kose, S.3
  • 11
    • 0029025345 scopus 로고
    • Identification of a yeast karyopherin heterodimer that targets import substrate to mammalian nuclear pore complexes
    • Enenkel C, Blobel G, Rexach M. (1995) Identification of a yeast karyopherin heterodimer that targets import substrate to mammalian nuclear pore complexes. J. Biol. Chem. 270: 16499-16502.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16499-16502
    • Enenkel, C.1    Blobel, G.2    Rexach, M.3
  • 12
    • 0040182590 scopus 로고    scopus 로고
    • Nuclear protein import
    • Gorlich D. (1997) Nuclear protein import. Curr. Opin. Cell Biol. 9: 412-419.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 412-419
    • Gorlich, D.1
  • 13
    • 0027376308 scopus 로고
    • The GTP-binding protein Ran/TC4 is required for protein import into the nucleus
    • Moore MS, Blobel G. (1993) The GTP-binding protein Ran/TC4 is required for protein import into the nucleus. Nature 365: 661-663.
    • (1993) Nature , vol.365 , pp. 661-663
    • Moore, M.S.1    Blobel, G.2
  • 14
    • 0027714921 scopus 로고
    • Inhibition of nuclear protein import by nonhydrolyzable analogues of GTP and identification of the small GTPase Ran/TC4 as an essential transport factor
    • Melchior F, Paschal B, Evans J, Gerace L. (1993) Inhibition of nuclear protein import by nonhydrolyzable analogues of GTP and identification of the small GTPase Ran/TC4 as an essential transport factor. J. Cell Biol. 123: 1649-1659.
    • (1993) J. Cell Biol. , vol.123 , pp. 1649-1659
    • Melchior, F.1    Paschal, B.2    Evans, J.3    Gerace, L.4
  • 15
    • 0030272377 scopus 로고    scopus 로고
    • Importin provides a link between nuclear protein import and U snRNA export
    • Gorlich D, Kraft R, Kostka S, et al. (1996) Importin provides a link between nuclear protein import and U snRNA export. Cell 87: 21-32.
    • (1996) Cell , vol.87 , pp. 21-32
    • Gorlich, D.1    Kraft, R.2    Kostka, S.3
  • 16
    • 0029853631 scopus 로고    scopus 로고
    • Identification of different roles for RanGDP and RanGTP in nuclear protein import
    • Gorlich D, Pante N, Kutay U, Aebi U, Bischoff FR. (1996) Identification of different roles for RanGDP and RanGTP in nuclear protein import. EMBO J. 15: 5584-5594.
    • (1996) EMBO J. , vol.15 , pp. 5584-5594
    • Gorlich, D.1    Pante, N.2    Kutay, U.3    Aebi, U.4    Bischoff, F.R.5
  • 17
    • 0028834428 scopus 로고
    • Protein import into nuclei: Association and dissociation reactions involving transport substrate, transport factors, and nucleoporins
    • Rexach M, Blobel G. (1995) Protein import into nuclei: Association and dissociation reactions involving transport substrate, transport factors, and nucleoporins. Cell 83: 683-692.
    • (1995) Cell , vol.83 , pp. 683-692
    • Rexach, M.1    Blobel, G.2
  • 18
    • 0029847386 scopus 로고    scopus 로고
    • RanBP1 stabilizes the interaction of Ran with p97 nuclear protein import
    • Chi NC, Adam EJ, Visser GD, Adam SA. (1996) RanBP1 stabilizes the interaction of Ran with p97 nuclear protein import. J. Cell Biol. 135: 559-569.
    • (1996) J. Cell Biol. , vol.135 , pp. 559-569
    • Chi, N.C.1    Adam, E.J.2    Visser, G.D.3    Adam, S.A.4
  • 19
    • 0028170744 scopus 로고
    • Purification of a Ran-interacting protein that is required for protein import into the nucleus
    • Moore MS, Blobel G. (1994) Purification of a Ran-interacting protein that is required for protein import into the nucleus. Proc. Natl. Acad. Sci. USA 91: 10212-10216.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10212-10216
    • Moore, M.S.1    Blobel, G.2
  • 20
    • 0029027836 scopus 로고
    • Identification of NTF2, a cytosolic factor for nuclear import that interacts with nuclear pore complex protein p62
    • Paschal BM, Gerace L. (1995) Identification of NTF2, a cytosolic factor for nuclear import that interacts with nuclear pore complex protein p62. J. Cell Biol. 129: 925-937.
    • (1995) J. Cell Biol. , vol.129 , pp. 925-937
    • Paschal, B.M.1    Gerace, L.2
  • 21
    • 0030570091 scopus 로고    scopus 로고
    • Role of the nuclear transport factor p10 in nuclear import
    • Nehrbass U, Blobel G. (1996) Role of the nuclear transport factor p10 in nuclear import. Science 272: 120-122.
    • (1996) Science , vol.272 , pp. 120-122
    • Nehrbass, U.1    Blobel, G.2
  • 22
    • 0031040797 scopus 로고    scopus 로고
    • Differential expression and sequence-specific interaction of karyopherin alpha with nuclear localization sequences
    • Nadler SG, Tritschler D, Haffar OK, Blake J, Bruce AG, Cleaveland JS. (1997) Differential expression and sequence-specific interaction of karyopherin alpha with nuclear localization sequences. J. Biol. Chem. 272: 4310-4315.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4310-4315
    • Nadler, S.G.1    Tritschler, D.2    Haffar, O.K.3    Blake, J.4    Bruce, A.G.5    Cleaveland, J.S.6
  • 23
    • 0029960517 scopus 로고    scopus 로고
    • In vivo nuclear transport kinetics in Saccharomyces cerevisiae: A role for heat shock protein 70 during targeting and translocalion
    • Shulga N, Roberts P, Gu Z, et al. (1996) In vivo nuclear transport kinetics in Saccharomyces cerevisiae: A role for heat shock protein 70 during targeting and translocalion. J. Cell Biol. 135: 329-339.
    • (1996) J. Cell Biol. , vol.135 , pp. 329-339
    • Shulga, N.1    Roberts, P.2    Gu, Z.3
  • 24
    • 0025833813 scopus 로고
    • Human major HSP70 protein complements the localization and functional defects of cytoplasmic mutant SV40 T antigen in Swiss 3T3 mouse fibroblast cells
    • Jeoung DI, Chen S, Windsor J, Pollack RE. (1991) Human major HSP70 protein complements the localization and functional defects of cytoplasmic mutant SV40 T antigen in Swiss 3T3 mouse fibroblast cells. Genes Dev. 5: 2235-2244.
    • (1991) Genes Dev. , vol.5 , pp. 2235-2244
    • Jeoung, D.I.1    Chen, S.2    Windsor, J.3    Pollack, R.E.4
  • 25
    • 0026643651 scopus 로고
    • The transport of proteins into the nucleus requires the 70-kilodalton heat shock protein or its cytosolic cognate
    • Shi Y, Thomas JO. (1992) The transport of proteins into the nucleus requires the 70-kilodalton heat shock protein or its cytosolic cognate. Mol. Cell Biol. 12: 2186-2192.
    • (1992) Mol. Cell Biol. , vol.12 , pp. 2186-2192
    • Shi, Y.1    Thomas, J.O.2
  • 26
    • 0027315529 scopus 로고
    • 70-kDa heat-shock cognate protein colocalizes with karyophilic proteins into the nucleus during their transport in vitro
    • Okuno Y, Imamoto N, Yoneda Y. (1993) 70-kDa heat-shock cognate protein colocalizes with karyophilic proteins into the nucleus during their transport in vitro. Exp. Cell Res. 206: 134-142.
    • (1993) Exp. Cell Res. , vol.206 , pp. 134-142
    • Okuno, Y.1    Imamoto, N.2    Yoneda, Y.3
  • 27
    • 0027376309 scopus 로고
    • A nuclear localization signal within HIV-1 matrix protein that governs infection of non-dividing cells
    • Bukrinsky MI, Haggerty S, Dempsey MP, et al. (1993) A nuclear localization signal within HIV-1 matrix protein that governs infection of non-dividing cells. Nature 365: 666-669.
    • (1993) Nature , vol.365 , pp. 666-669
    • Bukrinsky, M.I.1    Haggerty, S.2    Dempsey, M.P.3
  • 28
    • 0029062117 scopus 로고
    • Role of the basic domain of human immunodeficiency virus type 1 matrix in macrophage infection
    • Freed EO, Englund G, Martin MA. (1995) Role of the basic domain of human immunodeficiency virus type 1 matrix in macrophage infection. J. Virol. 69: 3949-3954.
    • (1995) J. Virol. , vol.69 , pp. 3949-3954
    • Freed, E.O.1    Englund, G.2    Martin, M.A.3
  • 29
    • 0030747461 scopus 로고    scopus 로고
    • HIV-1 infection of non-dividing cells: Evidence that the amino-terminal basic region of the viral matrix protein is important for Gag processing but not for post-entry nuclear import
    • Fouchier RA, Meyer BE, Simon JH, Fischer U, Malim MH. (1997) HIV-1 infection of non-dividing cells: Evidence that the amino-terminal basic region of the viral matrix protein is important for Gag processing but not for post-entry nuclear import. EMBO J. 16: 4531-4539.
    • (1997) EMBO J. , vol.16 , pp. 4531-4539
    • Fouchier, R.A.1    Meyer, B.E.2    Simon, J.H.3    Fischer, U.4    Malim, M.H.5
  • 30
    • 0030988835 scopus 로고    scopus 로고
    • Infant-maternal HIV-specific immunoglobulin G1 antibody ratios as an indicator of vertical transmission
    • Madurai S, Moodley D, Coovadia HM, Gopaul W, Smith AN, York DF. (1997) Infant-maternal HIV-specific immunoglobulin G1 antibody ratios as an indicator of vertical transmission. AIDS 11: 1191-1193.
    • (1997) AIDS , vol.11 , pp. 1191-1193
    • Madurai, S.1    Moodley, D.2    Coovadia, H.M.3    Gopaul, W.4    Smith, A.N.5    York, D.F.6
  • 31
    • 0031060369 scopus 로고    scopus 로고
    • Subcellular localization of avian sarcoma virus and human immunodeficiency virus type 1 integrases
    • Kukolj G, Jones KS, Skalka AM. (1997) Subcellular localization of avian sarcoma virus and human immunodeficiency virus type 1 integrases. J. Virol. 71: 843-847.
    • (1997) J. Virol. , vol.71 , pp. 843-847
    • Kukolj, G.1    Jones, K.S.2    Skalka, A.M.3
  • 32
    • 18844468523 scopus 로고    scopus 로고
    • Viral protein R (Vpr) regulates nuclear import of the HIV-1 preintegration complex
    • Popov S, Rexach M, Zybarth G, et al. (1998) Viral protein R (Vpr) regulates nuclear import of the HIV-1 preintegration complex. EMBO J. 17: 909-917.
    • (1998) EMBO J. , vol.17 , pp. 909-917
    • Popov, S.1    Rexach, M.2    Zybarth, G.3
  • 33
    • 0025350783 scopus 로고
    • Integration is not necessary for expression of human immunodeficiency virus type 1 protein products
    • Stevenson M, Haggerty S, Lamonica CA, Meier CM, Welch SK, Wasiak AJ. (1990) Integration is not necessary for expression of human immunodeficiency virus type 1 protein products. J. Virol. 64: 2421-2425.
    • (1990) J. Virol. , vol.64 , pp. 2421-2425
    • Stevenson, M.1    Haggerty, S.2    Lamonica, C.A.3    Meier, C.M.4    Welch, S.K.5    Wasiak, A.J.6
  • 34
    • 0025342694 scopus 로고
    • HIV-1 entry into quiescent primary lymphocytes: Molecular analysis reveals a labile, latent viral structure
    • Zack JA, Arrigo SJ, Weitsman SR, Go AS, Haislip A, Chen IS. (1990) HIV-1 entry into quiescent primary lymphocytes: molecular analysis reveals a labile, latent viral structure. Cell 61: 213-222.
    • (1990) Cell , vol.61 , pp. 213-222
    • Zack, J.A.1    Arrigo, S.J.2    Weitsman, S.R.3    Go, A.S.4    Haislip, A.5    Chen, I.S.6
  • 35
    • 0027162620 scopus 로고
    • Human immunodeficiency virus type 1 DNA synthesis, integration, and efficient viral replication in growth-arrested T cells
    • Li G, Simm M, Potash MJ, Volsky DJ. (1993) Human immunodeficiency virus type 1 DNA synthesis, integration, and efficient viral replication in growth-arrested T cells. J. Virol. 67: 3969-3977.
    • (1993) J. Virol. , vol.67 , pp. 3969-3977
    • Li, G.1    Simm, M.2    Potash, M.J.3    Volsky, D.J.4
  • 36
    • 0031971090 scopus 로고    scopus 로고
    • CNI-H0294, a nuclear importation inhibitor of the human immunodeficiency virus type-1 genome, abrogates virus replication in infected activated peripheral blood mononuclear cells
    • In press
    • Haffar OK, Smithgall MD, Popov S, et al. (1998) CNI-H0294, a nuclear importation inhibitor of the human immunodeficiency virus type-1 genome, abrogates virus replication in infected activated peripheral blood mononuclear cells. Antimicrob. Agents Chemother. (In press)
    • (1998) Antimicrob. Agents Chemother.
    • Haffar, O.K.1    Smithgall, M.D.2    Popov, S.3
  • 37
    • 16044371466 scopus 로고    scopus 로고
    • Critical role of reverse transcriptase in the inhibitory mechanism of CNI-H0294 on HIV-1 nuclear translocation
    • Popov S, Dubrovsky L, Lee MA, et al. (1996) Critical role of reverse transcriptase in the inhibitory mechanism of CNI-H0294 on HIV-1 nuclear translocation. Proc. Natl. Acad. Sci. USA 93: 11859-11864.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 11859-11864
    • Popov, S.1    Dubrovsky, L.2    Lee, M.A.3
  • 38
    • 0030065395 scopus 로고    scopus 로고
    • Role of the karyopherin pathway in human immunodeficiency virus type 1 nuclear import
    • Gallay P, Stitt V, Mundy C, Oettinger M, Trono D. (1996) Role of the karyopherin pathway in human immunodeficiency virus type 1 nuclear import. J. Virol. 70: 1027-1032.
    • (1996) J. Virol. , vol.70 , pp. 1027-1032
    • Gallay, P.1    Stitt, V.2    Mundy, C.3    Oettinger, M.4    Trono, D.5
  • 39
    • 0030987672 scopus 로고    scopus 로고
    • HIV-1 infection of nondividing cells through the recognition of integrase by the importin/karyopherin pathway
    • Gallay P, Hope T, Chin D, Trono D. (1997) HIV-1 infection of nondividing cells through the recognition of integrase by the importin/karyopherin pathway. Proc. Natl. Acad. Sci. USA 94: 9825-9830.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9825-9830
    • Gallay, P.1    Hope, T.2    Chin, D.3    Trono, D.4
  • 40
    • 0028803669 scopus 로고
    • Assembly of the preprotein receptor MOM72/MAS70 into the protein import complex of the outer membrane of mitochondria
    • Schlossmann J, Neupert W. (1995) Assembly of the preprotein receptor MOM72/MAS70 into the protein import complex of the outer membrane of mitochondria. J. Biol. Chem. 270: 27116-27121.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27116-27121
    • Schlossmann, J.1    Neupert, W.2
  • 41
    • 0024094917 scopus 로고
    • The effects of variations in the number and sequence of targeting signals on nuclear uptake
    • Dworetzky SI, Lanford RE, Feldherr CM. (1988) The effects of variations in the number and sequence of targeting signals on nuclear uptake. J. Cell Biol. 107: 1279-1287.
    • (1988) J. Cell Biol. , vol.107 , pp. 1279-1287
    • Dworetzky, S.I.1    Lanford, R.E.2    Feldherr, C.M.3
  • 42
    • 1842411367 scopus 로고    scopus 로고
    • Highly efficient and sustained gene transfer in adult neurons with a lentivirus vector
    • Blomer U, Naldini L, Kafri T, Trono D, Verma IM, Gage FH. (1997) Highly efficient and sustained gene transfer in adult neurons with a lentivirus vector. J. Virol. 71: 6641-6649.
    • (1997) J. Virol. , vol.71 , pp. 6641-6649
    • Blomer, U.1    Naldini, L.2    Kafri, T.3    Trono, D.4    Verma, I.M.5    Gage, F.H.6
  • 43
    • 0031975959 scopus 로고    scopus 로고
    • HIV-1 Vpr interacts with the nuclear transport pathway to promote macrophage infection
    • Vodicka MA, Koepp DM, Silver PA, Emerman M. (1998) HIV-1 Vpr interacts with the nuclear transport pathway to promote macrophage infection. Genes Dev. 12: 175-185.
    • (1998) Genes Dev. , vol.12 , pp. 175-185
    • Vodicka, M.A.1    Koepp, D.M.2    Silver, P.A.3    Emerman, M.4
  • 44
    • 0028824894 scopus 로고
    • Mutational analysis of cell cycle arrest, nuclear localization and virion packaging of human immunodeficiency virus type 1 Vpr
    • Di Marzio P, Choe S, Ebright M, Knoblauch R, Landau NR. (1995) Mutational analysis of cell cycle arrest, nuclear localization and virion packaging of human immunodeficiency virus type 1 Vpr. J. Virol. 69: 7909-7916.
    • (1995) J. Virol. , vol.69 , pp. 7909-7916
    • Di Marzio, P.1    Choe, S.2    Ebright, M.3    Knoblauch, R.4    Landau, N.R.5
  • 45
    • 0028318421 scopus 로고
    • Biochemical mechanism of HIV-1 Vpr function. Specific interaction with a cellular protein
    • Zhao LJ, Mukherjee S, Narayan O. (1994) Biochemical mechanism of HIV-1 Vpr function. Specific interaction with a cellular protein. J. Biol. Chem. 269: 15577-15582.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15577-15582
    • Zhao, L.J.1    Mukherjee, S.2    Narayan, O.3
  • 46
    • 0028600072 scopus 로고
    • Biochemical mechanism of HIV-1 Vpr function. Oligomerization mediated by the N-terminal domain
    • Zhao LJ, Wang L, Mukherjee S, Narayan O. (1994) Biochemical mechanism of HIV-1 Vpr function. Oligomerization mediated by the N-terminal domain. J. Biol. Chem. 269: 32131-32137.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32131-32137
    • Zhao, L.J.1    Wang, L.2    Mukherjee, S.3    Narayan, O.4
  • 47
    • 0028967421 scopus 로고
    • The glucocorticoid receptor type II complex is a target of the HIV-1 vpr gene product
    • Refaeli Y, Levy DN, Weiner DB. (1995) The glucocorticoid receptor type II complex is a target of the HIV-1 vpr gene product. Proc. Natl. Acad. Sci. USA 92: 3621-3625.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3621-3625
    • Refaeli, Y.1    Levy, D.N.2    Weiner, D.B.3
  • 48
    • 0030824787 scopus 로고    scopus 로고
    • Nuclear import, virion incorporation, and cell cycle arrest/differentiation are mediated by distinct functional domains of human immunodeficiency virus type 1 Vpr
    • Mahalingam S, Ayyavoo V, Patel M, Kieber-Emmons T, Weiner DB. (1997) Nuclear import, virion incorporation, and cell cycle arrest/differentiation are mediated by distinct functional domains of human immunodeficiency virus type 1 Vpr. J. Virol. 71: 6339-6347.
    • (1997) J. Virol. , vol.71 , pp. 6339-6347
    • Mahalingam, S.1    Ayyavoo, V.2    Patel, M.3    Kieber-Emmons, T.4    Weiner, D.B.5
  • 49
    • 0030819379 scopus 로고    scopus 로고
    • Multiply attenuated lentiviral vector achieves efficient gene delivery in vivo
    • Zufferey R, Nagy D, Mandel RJ, Naldini L, Trono D. (1997) Multiply attenuated lentiviral vector achieves efficient gene delivery in vivo. Nat. Biotechnol. 15: 871-875.
    • (1997) Nat. Biotechnol. , vol.15 , pp. 871-875
    • Zufferey, R.1    Nagy, D.2    Mandel, R.J.3    Naldini, L.4    Trono, D.5
  • 50
    • 0029966361 scopus 로고    scopus 로고
    • Crystal structures of the trimeric human immunodeficiency virus type 1 matrix protein: Implications for membrane association and assembly
    • Hill CP, Worthylake D, Bancroft DP, Christensen AM, Sundquist WI. (1996) Crystal structures of the trimeric human immunodeficiency virus type 1 matrix protein: Implications for membrane association and assembly. Proc. Natl. Acad. Sci. USA 93: 3099-3104.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3099-3104
    • Hill, C.P.1    Worthylake, D.2    Bancroft, D.P.3    Christensen, A.M.4    Sundquist, W.I.5
  • 51
    • 0032557445 scopus 로고    scopus 로고
    • Viral protein R regulates docking of the HIV-1 preintegration complex to the nuclear pore complex
    • In press
    • Popov S, Rexach M, Blobel G, Bukrinsky MI. (1998) Viral protein R regulates docking of the HIV-1 preintegration complex to the nuclear pore complex. J. Biol. Chem. (In press)
    • (1998) J. Biol. Chem.
    • Popov, S.1    Rexach, M.2    Blobel, G.3    Bukrinsky, M.I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.