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Volumn 55, Issue 6, 2003, Pages 733-747

Virus nuclear import

Author keywords

Herpesvirus; HIV; Influenza; Nuclear targeting; Nuclear transport; Viral infection

Indexed keywords

BIOLOGICAL MEMBRANES; CELLS; GENES; PORE SIZE;

EID: 0038699054     PISSN: 0169409X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0169-409X(03)00051-6     Document Type: Review
Times cited : (48)

References (128)
  • 1
    • 0032551236 scopus 로고    scopus 로고
    • Nuclear import and export of viruses and virus genomes
    • Whittaker G.R., Helenius A. Nuclear import and export of viruses and virus genomes. Virology. 246:1998;1-23.
    • (1998) Virology , vol.246 , pp. 1-23
    • Whittaker, G.R.1    Helenius, A.2
  • 2
    • 0035907248 scopus 로고    scopus 로고
    • The nuclear pore complex as a transport machine
    • Rout M.P., Aitchison J.D. The nuclear pore complex as a transport machine. J. Biol. Chem. 276:2001;16593-16596.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16593-16596
    • Rout, M.P.1    Aitchison, J.D.2
  • 3
    • 0034717044 scopus 로고    scopus 로고
    • Gatekeepers of the nucleus
    • Wente S.R. Gatekeepers of the nucleus. Science. 288:2000;1374-1377.
    • (2000) Science , vol.288 , pp. 1374-1377
    • Wente, S.R.1
  • 4
    • 0023840074 scopus 로고
    • Translocation of RNA-coated gold particles through the nuclear pores at oocytes
    • Dworetzky S.I., Feldherr C.M. Translocation of RNA-coated gold particles through the nuclear pores at oocytes. J. Cell Biol. 106:1988;575-584.
    • (1988) J. Cell Biol. , vol.106 , pp. 575-584
    • Dworetzky, S.I.1    Feldherr, C.M.2
  • 5
    • 0024094917 scopus 로고
    • The effects of variations in the number and sequence of targeting signals on nuclear uptake
    • Dworetzky S.I., Lanford R.E., Feldherr C.M. The effects of variations in the number and sequence of targeting signals on nuclear uptake. J. Cell Biol. 107:1988;1279-1287.
    • (1988) J. Cell Biol. , vol.107 , pp. 1279-1287
    • Dworetzky, S.I.1    Lanford, R.E.2    Feldherr, C.M.3
  • 6
    • 0036175701 scopus 로고    scopus 로고
    • Nuclear pore complex is able to transport macromolecules with diameters of about 39 nm
    • Pante N., Kann M. Nuclear pore complex is able to transport macromolecules with diameters of about 39 nm. Mol. Biol. Cell. 13:2002;425-434.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 425-434
    • Pante, N.1    Kann, M.2
  • 7
    • 0033279841 scopus 로고    scopus 로고
    • Transport between the cell nucleus and the cytoplasm
    • Gorlich D., Kutay U. Transport between the cell nucleus and the cytoplasm. Annu. Rev. Cell Dev. Biol. 15:1999;607-660.
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 607-660
    • Gorlich, D.1    Kutay, U.2
  • 8
    • 0033598989 scopus 로고    scopus 로고
    • Transport of proteins and RNAs in and out of the nucleus
    • Nakielny S., Dreyfuss G. Transport of proteins and RNAs in and out of the nucleus. Cell. 99:1999;677-690.
    • (1999) Cell , vol.99 , pp. 677-690
    • Nakielny, S.1    Dreyfuss, G.2
  • 9
    • 0035203632 scopus 로고    scopus 로고
    • Transport into and out of the nucleus
    • Macara I.G. Transport into and out of the nucleus. Microbiol. Mol. Biol. Rev. 65:2001;570-594.
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 570-594
    • Macara, I.G.1
  • 10
    • 0031052263 scopus 로고    scopus 로고
    • Isolation of a common receptor for Coxsackie B viruses and adenoviruses 2 and 5
    • Bergelson J.M., et al. Isolation of a common receptor for Coxsackie B viruses and adenoviruses 2 and 5. Science. 275:1997;1320-1323.
    • (1997) Science , vol.275 , pp. 1320-1323
    • Bergelson, J.M.1
  • 11
    • 0027166647 scopus 로고
    • Integrins alpha v beta 3 and alpha v beta 5 promote adenovirus internalization but not virus attachment
    • Wickham T.J., Mathias P., Cheresh D.A., Nemerow G.R. Integrins alpha v beta 3 and alpha v beta 5 promote adenovirus internalization but not virus attachment. Cell. 73:1993;309-319.
    • (1993) Cell , vol.73 , pp. 309-319
    • Wickham, T.J.1    Mathias, P.2    Cheresh, D.A.3    Nemerow, G.R.4
  • 12
    • 0014748494 scopus 로고
    • Early events in the interaction of adenoviruses with HeLa cells. I. Penetration of type 5 and intracellular release of the DNA genome
    • Chardonnnet Y., Dales S. Early events in the interaction of adenoviruses with HeLa cells. I. Penetration of type 5 and intracellular release of the DNA genome. Virology. 40:1970;462-477.
    • (1970) Virology , vol.40 , pp. 462-477
    • Chardonnnet, Y.1    Dales, S.2
  • 14
    • 0002159224 scopus 로고
    • Adenovirus entry into cells: Some new observations on an old problem
    • A.L. Notkins, & M.B.A. Oldstone. New York: Springer Verlag
    • Pastan I., Seth P., FitzGerald D., Willingham M. Adenovirus entry into cells: some new observations on an old problem. Notkins A.L., Oldstone M.B.A. Concepts in Viral Pathogenesis II. 1986;Springer Verlag, New York.
    • (1986) Concepts in Viral Pathogenesis II
    • Pastan, I.1    Seth, P.2    FitzGerald, D.3    Willingham, M.4
  • 15
    • 0028169584 scopus 로고
    • Integrin alpha v beta 5 selectively promotes adenovirus mediated cell membrane permeabilization
    • Wickham T.J., Filardo E.J., Cheresh D.A., Nemerow G.R. Integrin alpha v beta 5 selectively promotes adenovirus mediated cell membrane permeabilization. J. Cell Biol. 127:1994;257-264.
    • (1994) J. Cell Biol. , vol.127 , pp. 257-264
    • Wickham, T.J.1    Filardo, E.J.2    Cheresh, D.A.3    Nemerow, G.R.4
  • 16
    • 0027496645 scopus 로고
    • Stepwise dismantling of adenovirus 2 during entry into cells
    • Greber U.F., Willetts M., Webster P., Helenius A. Stepwise dismantling of adenovirus 2 during entry into cells. Cell. 75:1993;477-486.
    • (1993) Cell , vol.75 , pp. 477-486
    • Greber, U.F.1    Willetts, M.2    Webster, P.3    Helenius, A.4
  • 17
    • 0028883978 scopus 로고
    • The adenovirus protease is required for virus entry into host cells
    • Cotten M., Weber J.M. The adenovirus protease is required for virus entry into host cells. Virology. 213:1995;494-502.
    • (1995) Virology , vol.213 , pp. 494-502
    • Cotten, M.1    Weber, J.M.2
  • 18
    • 0029983628 scopus 로고    scopus 로고
    • The role of the adenovirus protease on virus entry into cells
    • Greber U.F., Webster P., Weber J., Helenius A. The role of the adenovirus protease on virus entry into cells. EMBO J. 15:1996;1766-1777.
    • (1996) EMBO J. , vol.15 , pp. 1766-1777
    • Greber, U.F.1    Webster, P.2    Weber, J.3    Helenius, A.4
  • 19
    • 0035154757 scopus 로고    scopus 로고
    • Adenovirus serotype 7 retention in a late endosomal compartment prior to cytosol escape is modulated by fiber protein
    • Miyazawa N., Crystal R.G., Leopold P.L. Adenovirus serotype 7 retention in a late endosomal compartment prior to cytosol escape is modulated by fiber protein. J. Virol. 75:2001;1387-1400.
    • (2001) J. Virol. , vol.75 , pp. 1387-1400
    • Miyazawa, N.1    Crystal, R.G.2    Leopold, P.L.3
  • 20
    • 0033593811 scopus 로고    scopus 로고
    • Microtubule-dependent plus- and minus end-directed motilities are competing processes for nuclear targeting of adenovirus
    • Suomalainen M., Nakano M.Y., Keller S., Boucke K., Stidwell R.P., Greber U.J. Microtubule-dependent plus- and minus end-directed motilities are competing processes for nuclear targeting of adenovirus. Cell Biol. 144:1999;657-672.
    • (1999) Cell Biol. , vol.144 , pp. 657-672
    • Suomalainen, M.1    Nakano, M.Y.2    Keller, S.3    Boucke, K.4    Stidwell, R.P.5    Greber, U.J.6
  • 21
    • 0035868714 scopus 로고    scopus 로고
    • Adenovirus-activated PKA and p38/MAPK pathways boost microtubule-mediated nuclear targeting of virus
    • Suomalainen M., Nakano M.Y., Boucke K., Keller S., Greber U.F. Adenovirus-activated PKA and p38/MAPK pathways boost microtubule-mediated nuclear targeting of virus. EMBO J. 20:2001;1310-1319.
    • (2001) EMBO J. , vol.20 , pp. 1310-1319
    • Suomalainen, M.1    Nakano, M.Y.2    Boucke, K.3    Keller, S.4    Greber, U.F.5
  • 22
    • 0035125270 scopus 로고    scopus 로고
    • Microtubule-independent motility and nuclear targeting of adenoviruses with fluorescently labeled genomes M
    • Glotzer J.B., Michou A.I., Baker A., et al. Microtubule-independent motility and nuclear targeting of adenoviruses with fluorescently labeled genomes M. J. Virol. 75:2001;2421-2434.
    • (2001) J. Virol. , vol.75 , pp. 2421-2434
    • Glotzer, J.B.1    Michou, A.I.2    Baker, A.3
  • 23
    • 0014605507 scopus 로고
    • Structure and development of viruses as observed in the electron microscope. V. Entry and uncoating of adenovirus
    • Morgan C., Rosenkranz H.S., Mednis B.J. Structure and development of viruses as observed in the electron microscope. V. Entry and uncoating of adenovirus. Virology. 4:1969;777-796.
    • (1969) Virology , vol.4 , pp. 777-796
    • Morgan, C.1    Rosenkranz, H.S.2    Mednis, B.J.3
  • 25
    • 0039174260 scopus 로고    scopus 로고
    • Nuclear import of adenovirus DNA in vitro involves the nuclear protein import pathway and hsc70
    • Saphire A.C.S., Guan T., Schirmer E.C., Nemerow G.R., Gerace L. Nuclear import of adenovirus DNA in vitro involves the nuclear protein import pathway and hsc70. J. Biol. Chem. 275:2000;4298-4304.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4298-4304
    • Saphire, A.C.S.1    Guan, T.2    Schirmer, E.C.3    Nemerow, G.R.4    Gerace, L.5
  • 26
    • 0033198897 scopus 로고    scopus 로고
    • Specific binding of the adenovirus capsid to the nuclear envelope
    • Wisnivesky J.P., Leopold P.L., Crystal R.G. Specific binding of the adenovirus capsid to the nuclear envelope. Hum. Gene Ther. 10:1999;2187-2195.
    • (1999) Hum. Gene Ther. , vol.10 , pp. 2187-2195
    • Wisnivesky, J.P.1    Leopold, P.L.2    Crystal, R.G.3
  • 27
    • 0035195085 scopus 로고    scopus 로고
    • Import of adenovirus DNA involves the nuclear pore complex receptor CAN/Nup214 and histone H1
    • Trotman L.C., Mosberger N., Fornerod M., Stidwill R.P., Greber U.F. Import of adenovirus DNA involves the nuclear pore complex receptor CAN/Nup214 and histone H1. Nat. Cell Biol. 3:2001;1092-1100.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 1092-1100
    • Trotman, L.C.1    Mosberger, N.2    Fornerod, M.3    Stidwill, R.P.4    Greber, U.F.5
  • 28
    • 0033761804 scopus 로고    scopus 로고
    • Adeno-associated virus vectors for gene therapy: More pros than cons?
    • Monahan P.E., Samulski R.J. Adeno-associated virus vectors for gene therapy: more pros than cons? Mol. Med. Today. 6:2000;433-440.
    • (2000) Mol. Med. Today , vol.6 , pp. 433-440
    • Monahan, P.E.1    Samulski, R.J.2
  • 29
    • 0033937284 scopus 로고    scopus 로고
    • Cellular uptake and infection by canine parvovirus involves rapid dynamin-regulated clathrin-mediated endocytosis, followed by slower intracellular trafficking
    • Parker J.S., Parrish C.R. Cellular uptake and infection by canine parvovirus involves rapid dynamin-regulated clathrin-mediated endocytosis, followed by slower intracellular trafficking. J. Virol. 74:2000;1919-1930.
    • (2000) J. Virol. , vol.74 , pp. 1919-1930
    • Parker, J.S.1    Parrish, C.R.2
  • 30
    • 0026524911 scopus 로고
    • Infectious entry pathway for canine parvovirus
    • Basak S., Turner H. Infectious entry pathway for canine parvovirus. Virology. 186:1992;368-376.
    • (1992) Virology , vol.186 , pp. 368-376
    • Basak, S.1    Turner, H.2
  • 31
    • 0033998692 scopus 로고    scopus 로고
    • Infectious entry pathway of adeno-associated virus and adeno-associated virus vectors
    • Bartlett J.S., Wilcher R., Samulski R.J. Infectious entry pathway of adeno-associated virus and adeno-associated virus vectors. J. Virol. 74:2000;2777-2785.
    • (2000) J. Virol. , vol.74 , pp. 2777-2785
    • Bartlett, J.S.1    Wilcher, R.2    Samulski, R.J.3
  • 32
    • 0034000922 scopus 로고    scopus 로고
    • Cytoplasmic trafficking of the canine parvovirus capsid and its role in infection and nuclear transport
    • Vihinen-Ranta M., Yuan W., Parrish C.R. Cytoplasmic trafficking of the canine parvovirus capsid and its role in infection and nuclear transport. J. Virol. 74:2000;4853-4859.
    • (2000) J. Virol. , vol.74 , pp. 4853-4859
    • Vihinen-Ranta, M.1    Yuan, W.2    Parrish, C.R.3
  • 33
    • 0035431876 scopus 로고    scopus 로고
    • A viral phospholipase A2 is required for parvovirus infectivity
    • Zadori Z., et al. A viral phospholipase A2 is required for parvovirus infectivity. Dev. Cell. 1:2001;291-302.
    • (2001) Dev. Cell , vol.1 , pp. 291-302
    • Zadori, Z.1
  • 34
    • 0033080393 scopus 로고    scopus 로고
    • Controlled conformational transitions in the MVM virion expose the VP1 N-terminus and viral genome without particle disassembly
    • Cotmore S.F., D'Abramo A.M. Jr., Ticknor C.M., Tattersall P. Controlled conformational transitions in the MVM virion expose the VP1 N-terminus and viral genome without particle disassembly. Virology. 254:1999;169-181.
    • (1999) Virology , vol.254 , pp. 169-181
    • Cotmore, S.F.1    D'Abramo A.M., Jr.2    Ticknor, C.M.3    Tattersall, P.4
  • 35
    • 0027194071 scopus 로고
    • Structure, sequence, and function correlations among parvoviruses
    • Chapman M.S., Rossmann M.G. Structure, sequence, and function correlations among parvoviruses. Virology. 194:1993;491-508.
    • (1993) Virology , vol.194 , pp. 491-508
    • Chapman, M.S.1    Rossmann, M.G.2
  • 37
    • 0032505630 scopus 로고    scopus 로고
    • Assaying for structural variation in the parvovirus capsid and its role in infection
    • Weichert W.S., Parker J.S., Wahid A.T.M., Chang S.F., Meier E., Parrish C.R. Assaying for structural variation in the parvovirus capsid and its role in infection. Virology. 250:1998;106-117.
    • (1998) Virology , vol.250 , pp. 106-117
    • Weichert, W.S.1    Parker, J.S.2    Wahid, A.T.M.3    Chang, S.F.4    Meier, E.5    Parrish, C.R.6
  • 38
    • 0031464535 scopus 로고    scopus 로고
    • Characterization of a nuclear localization signal of canine parvovirus capsid proteins
    • Vihinen-Ranta M., Kakkola L., Kalela A., Vilja P., Vuento M. Characterization of a nuclear localization signal of canine parvovirus capsid proteins. Eur. J. Biochem. 250:1997;389-394.
    • (1997) Eur. J. Biochem. , vol.250 , pp. 389-394
    • Vihinen-Ranta, M.1    Kakkola, L.2    Kalela, A.3    Vilja, P.4    Vuento, M.5
  • 39
    • 0036149891 scopus 로고    scopus 로고
    • The VP1 N-terminal sequence of canine parvovirus affects nuclear transport of capsids and efficient cell infection
    • Vihinen-Ranta M., Wang D., Weichert W.S., Parrish C.R. The VP1 N-terminal sequence of canine parvovirus affects nuclear transport of capsids and efficient cell infection. J. Virol. 76:2002;1884-1891.
    • (2002) J. Virol. , vol.76 , pp. 1884-1891
    • Vihinen-Ranta, M.1    Wang, D.2    Weichert, W.S.3    Parrish, C.R.4
  • 40
    • 0031693694 scopus 로고    scopus 로고
    • Differences in the intracellular localization and fate of herpes simplex virus tegument proteins early in the infection of Vero cells
    • Morrison E.E., Stevenson A.J., Wang Y.-F., Meredith D.M. Differences in the intracellular localization and fate of herpes simplex virus tegument proteins early in the infection of Vero cells. J. Gen. Virol. 79:1998;2517-2528.
    • (1998) J. Gen. Virol. , vol.79 , pp. 2517-2528
    • Morrison, E.E.1    Stevenson, A.J.2    Wang, Y.-F.3    Meredith, D.M.4
  • 41
    • 0031816798 scopus 로고    scopus 로고
    • Phosphorylation of structural components promotes dissociation of the herpes simplex virus type 1 tegument
    • Morrison E.E., Wang Y.F., Meredith D.M. Phosphorylation of structural components promotes dissociation of the herpes simplex virus type 1 tegument. J. Virol. 72:1998;7108-7114.
    • (1998) J. Virol. , vol.72 , pp. 7108-7114
    • Morrison, E.E.1    Wang, Y.F.2    Meredith, D.M.3
  • 42
    • 0033986874 scopus 로고    scopus 로고
    • Analysis of HCF, the cellular cofactor of VP16, in herpes simplex virus-infected cells
    • LaBoissiere S., O'Hare P. Analysis of HCF, the cellular cofactor of VP16, in herpes simplex virus-infected cells. J. Virol. 74:2000;99-109.
    • (2000) J. Virol. , vol.74 , pp. 99-109
    • LaBoissiere, S.1    O'Hare, P.2
  • 43
    • 0001682893 scopus 로고
    • The virion transactivator of herpes simplex virus
    • O'Hare P. The virion transactivator of herpes simplex virus. Sem. Virol. 4:1993;145-155.
    • (1993) Sem. Virol. , vol.4 , pp. 145-155
    • O'Hare, P.1
  • 44
    • 0345471494 scopus 로고    scopus 로고
    • Visualization of tegument-capsid interactions and DNA in intact herpes simplex virus type 1 virions
    • Zhou Z.H., Chen D.H., Jakana J., Rixon F.J., Chu W. Visualization of tegument-capsid interactions and DNA in intact herpes simplex virus type 1 virions. J. Virol. 73:1999;3210-3218.
    • (1999) J. Virol. , vol.73 , pp. 3210-3218
    • Zhou, Z.H.1    Chen, D.H.2    Jakana, J.3    Rixon, F.J.4    Chu, W.5
  • 45
    • 0034091334 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 entry into host cells: Reconstitution of capsid binding and uncoating at the nuclear pore complex in vitro
    • Ojala P.M., Sodeik B., Ebersold M.W., Kutay U., Helenius A. Herpes simplex virus type 1 entry into host cells: reconstitution of capsid binding and uncoating at the nuclear pore complex in vitro. Mol. Cell. Biol. 20:2000;4922-4931.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 4922-4931
    • Ojala, P.M.1    Sodeik, B.2    Ebersold, M.W.3    Kutay, U.4    Helenius, A.5
  • 46
    • 0003156753 scopus 로고
    • The replication of herpesviruses
    • H. Fraaenkel-Conrat, Wagner R.R. New York: Plenum Press
    • Roizman B., Furlong D. The replication of herpesviruses. Fraaenkel-Conrat H., Wagner R.R. Comprehensive Virology. Vol. 3:1974;Plenum Press, New York.
    • (1974) Comprehensive Virology , vol.3
    • Roizman, B.1    Furlong, D.2
  • 47
    • 0020701819 scopus 로고
    • Molecular genetics of herpes simplex virus. VIII. Further characterization of a temperature-sensitive mutant defective in release of viral DNA and in other stages of the viral reproductive cycle
    • Batterson W., Furlong D., Roizman B. Molecular genetics of herpes simplex virus. VIII. Further characterization of a temperature-sensitive mutant defective in release of viral DNA and in other stages of the viral reproductive cycle. J. Virol. 45:1983;397-407.
    • (1983) J. Virol. , vol.45 , pp. 397-407
    • Batterson, W.1    Furlong, D.2    Roizman, B.3
  • 48
    • 0032247683 scopus 로고    scopus 로고
    • Infection and spread of alphaherpesviruses in the nervous system
    • Enquist L.W., Husak P.J., Banfield B.W., Smith G.A. Infection and spread of alphaherpesviruses in the nervous system. Adv. Virus Res. 51:1998;237-347.
    • (1998) Adv. Virus Res. , vol.51 , pp. 237-347
    • Enquist, L.W.1    Husak, P.J.2    Banfield, B.W.3    Smith, G.A.4
  • 49
    • 0022531958 scopus 로고
    • Neuritic transport of herpes simplex virus in rat sensory neurons in vitro. Effects of substances interacting with microtubular function and axonal flow [nocodazole, taxol and erythro-9-3-(2-hydroxynonyl)adenine]
    • Kristensson K., Lycke E., Roytta M., Svennerholm B., Vahlne A. Neuritic transport of herpes simplex virus in rat sensory neurons in vitro. Effects of substances interacting with microtubular function and axonal flow [nocodazole, taxol and erythro-9-3-(2-hydroxynonyl)adenine]. J. Gen. Virol. 67:1986;2023-2028.
    • (1986) J. Gen. Virol. , vol.67 , pp. 2023-2028
    • Kristensson, K.1    Lycke, E.2    Roytta, M.3    Svennerholm, B.4    Vahlne, A.5
  • 50
    • 0030896925 scopus 로고    scopus 로고
    • Microtubule-mediated transport of incoming herpes simplex virus 1 capsids to the nucleus
    • Sodeik B., Ebersold M.W., Helenius A. Microtubule-mediated transport of incoming herpes simplex virus 1 capsids to the nucleus. J. Cell Biol. 136:1997;1007-1021.
    • (1997) J. Cell Biol. , vol.136 , pp. 1007-1021
    • Sodeik, B.1    Ebersold, M.W.2    Helenius, A.3
  • 51
    • 0033937283 scopus 로고    scopus 로고
    • Anterograde transport of herpes simplex virus type 1 in cultured, dissociated human and rat dorsal root ganglion neurons
    • Miranda-Saksena M., Armati P., Boadle R.A., Holland D.J., Cunningham A.L. Anterograde transport of herpes simplex virus type 1 in cultured, dissociated human and rat dorsal root ganglion neurons. J. Virol. 74:2000;1827-1839.
    • (2000) J. Virol. , vol.74 , pp. 1827-1839
    • Miranda-Saksena, M.1    Armati, P.2    Boadle, R.A.3    Holland, D.J.4    Cunningham, A.L.5
  • 52
    • 0035853091 scopus 로고    scopus 로고
    • Herpesviruses use bidirectional fast-axonal transport to spread in sensory neurons
    • Smith G.A., Gross S.P., Enquist L.W. Herpesviruses use bidirectional fast-axonal transport to spread in sensory neurons. Proc. Natl. Acad. Sci. USA. 98:2001;3466-3470.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3466-3470
    • Smith, G.A.1    Gross, S.P.2    Enquist, L.W.3
  • 53
    • 0028969951 scopus 로고
    • Recent studies on replication of hepatitis B virus
    • Kann M., Lu X., Gerlich W.H. Recent studies on replication of hepatitis B virus. J. Hepatol. 22:1995;9-13.
    • (1995) J. Hepatol. , vol.22 , pp. 9-13
    • Kann, M.1    Lu, X.2    Gerlich, W.H.3
  • 54
  • 55
    • 0031017060 scopus 로고    scopus 로고
    • In vitro model for the nuclear transport of the hepadnavirus genome
    • Kann M., Bischof A., Gerlich W.H. In vitro model for the nuclear transport of the hepadnavirus genome. J. Virol. 71:1997;1310-1316.
    • (1997) J. Virol. , vol.71 , pp. 1310-1316
    • Kann, M.1    Bischof, A.2    Gerlich, W.H.3
  • 56
    • 0033526096 scopus 로고    scopus 로고
    • Phosphorylation-dependent binding of hepatitis B virus core particles to the nuclear pore complex
    • Kann M., Sodeik B., Vlachoul A., Gerlich W.H., Helenius A. Phosphorylation-dependent binding of hepatitis B virus core particles to the nuclear pore complex. J. Cell Biol. 145:1999;45-55.
    • (1999) J. Cell Biol. , vol.145 , pp. 45-55
    • Kann, M.1    Sodeik, B.2    Vlachoul, A.3    Gerlich, W.H.4    Helenius, A.5
  • 57
    • 0031785929 scopus 로고    scopus 로고
    • How do animal DNA viruses get to the nucleus?
    • Kasamatsu H., Nakashini A. How do animal DNA viruses get to the nucleus? Annu. Rev. Microbiol. 52:1998;627-686.
    • (1998) Annu. Rev. Microbiol. , vol.52 , pp. 627-686
    • Kasamatsu, H.1    Nakashini, A.2
  • 58
    • 0035963944 scopus 로고    scopus 로고
    • Caveolae in the uptake and targeting of infectious agents and secreted toxins
    • Norkin L.C. Caveolae in the uptake and targeting of infectious agents and secreted toxins. Adv. Drug Deliv. Rev. 49:2001;301-315.
    • (2001) Adv. Drug Deliv. Rev. , vol.49 , pp. 301-315
    • Norkin, L.C.1
  • 59
    • 0035017308 scopus 로고    scopus 로고
    • Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER
    • Pelkmans L.J.K., Helenius A. Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER. Nat. Cell Biol. 3:2001;473-483.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 473-483
    • Pelkmans, L.J.K.1    Helenius, A.2
  • 60
    • 0024844490 scopus 로고
    • Endocytosis of simian virus 40 into the endoplasmic reticulum
    • Kartenbeck J., Stukenbrok H., Helenius A. Endocytosis of simian virus 40 into the endoplasmic reticulum. J. Cell Biol. 109:1989;2721-2729.
    • (1989) J. Cell Biol. , vol.109 , pp. 2721-2729
    • Kartenbeck, J.1    Stukenbrok, H.2    Helenius, A.3
  • 61
    • 0033540271 scopus 로고    scopus 로고
    • Extracellular simian virus 40 transmits a signal that promotes virus enclosure within caveolae
    • Chen Y., Norkin L.C. Extracellular simian virus 40 transmits a signal that promotes virus enclosure within caveolae. Exp. Cell Res. 246:1999;83-90.
    • (1999) Exp. Cell Res. , vol.246 , pp. 83-90
    • Chen, Y.1    Norkin, L.C.2
  • 63
    • 0031936604 scopus 로고    scopus 로고
    • Intercapsomeric disulfide bonds in papillomavirus assembly and disassembly
    • Li M., Beard P., Estes P.A., Lyon M.K., Garcea R.L. Intercapsomeric disulfide bonds in papillomavirus assembly and disassembly. J. Virol. 72:1998;2160-2167.
    • (1998) J. Virol. , vol.72 , pp. 2160-2167
    • Li, M.1    Beard, P.2    Estes, P.A.3    Lyon, M.K.4    Garcea, R.L.5
  • 64
  • 65
    • 0025915718 scopus 로고
    • Import of simian virus 40 virions through nuclear pore complexes
    • Clever J., Yamada M., Kasamatsu H. Import of simian virus 40 virions through nuclear pore complexes. Proc. Natl. Acad. Sci. USA. 88:1991;7333-7337.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7333-7337
    • Clever, J.1    Yamada, M.2    Kasamatsu, H.3
  • 66
    • 0027439610 scopus 로고
    • Role of nuclear pore complex in simian virus 40 nuclear targeting
    • Yamada M., Kasamatsu H. Role of nuclear pore complex in simian virus 40 nuclear targeting. J. Virol. 67:1993;119-130.
    • (1993) J. Virol. , vol.67 , pp. 119-130
    • Yamada, M.1    Kasamatsu, H.2
  • 67
    • 0023877646 scopus 로고
    • Early events in polyomavirus infection: Fusion of monopinocytotic vesicles containing virions with mouse kidney cell nuclei
    • Griffith G.R., Marriot S.J., Rintoul D.A., Consilgi R.A. Early events in polyomavirus infection: fusion of monopinocytotic vesicles containing virions with mouse kidney cell nuclei. Virus Res. 10:1988;41-51.
    • (1988) Virus Res. , vol.10 , pp. 41-51
    • Griffith, G.R.1    Marriot, S.J.2    Rintoul, D.A.3    Consilgi, R.A.4
  • 68
    • 0033822438 scopus 로고    scopus 로고
    • Use of electron microscopic and immunogold labeling techniques to determine polyomavirus recombinant VP1 capsid-like particles entry into mouse 3T6 cell nucleus
    • An K., Paulsen A.Q., Tilley M.B., Consigli R.A. Use of electron microscopic and immunogold labeling techniques to determine polyomavirus recombinant VP1 capsid-like particles entry into mouse 3T6 cell nucleus. J. Virol. Methods. 90:2000;91-97.
    • (2000) J. Virol. Methods , vol.90 , pp. 91-97
    • An, K.1    Paulsen, A.Q.2    Tilley, M.B.3    Consigli, R.A.4
  • 69
    • 0033567847 scopus 로고    scopus 로고
    • Nuclear import of HPV11 L1 capsid protein is mediated by karyopherin alpha2beta1 heterodimers
    • Merle E., Rose R.C., LeRoux L., Moroianu J. Nuclear import of HPV11 L1 capsid protein is mediated by karyopherin alpha2beta1 heterodimers. J. Cell Biochem. 74:1999;628-637.
    • (1999) J. Cell Biochem. , vol.74 , pp. 628-637
    • Merle, E.1    Rose, R.C.2    LeRoux, L.3    Moroianu, J.4
  • 70
    • 0033794984 scopus 로고    scopus 로고
    • Nuclear import and DNA binding of human papillomavirus type 45 L1 capsid protein
    • Nelson L.M., Rose R.C., LeRoux L., Lane C., Bruya K., Moroianu J. Nuclear import and DNA binding of human papillomavirus type 45 L1 capsid protein. J. Cell Biochem. 79:2000;225-238.
    • (2000) J. Cell Biochem. , vol.79 , pp. 225-238
    • Nelson, L.M.1    Rose, R.C.2    LeRoux, L.3    Lane, C.4    Bruya, K.5    Moroianu, J.6
  • 71
    • 0035836374 scopus 로고    scopus 로고
    • Association of bovine papillomavirus type 1 with microtubules
    • Liu W.J., Qi Y.M., Zhao K.N., Liu Y.H., Liu X.S., Frazer I.H. Association of bovine papillomavirus type 1 with microtubules. Virology. 282:2001;237-244.
    • (2001) Virology , vol.282 , pp. 237-244
    • Liu, W.J.1    Qi, Y.M.2    Zhao, K.N.3    Liu, Y.H.4    Liu, X.S.5    Frazer, I.H.6
  • 72
    • 0028055281 scopus 로고
    • Passage through mitosis is required for oncoretroviruses but not for the human immunodeficiency virus
    • Lewis P.F., Emerman M. Passage through mitosis is required for oncoretroviruses but not for the human immunodeficiency virus. J. Virol. 68:1994;510-516.
    • (1994) J. Virol. , vol.68 , pp. 510-516
    • Lewis, P.F.1    Emerman, M.2
  • 73
    • 0033012398 scopus 로고    scopus 로고
    • Chemokine receptors as HIV-1 coreceptors: Roles in viral entry, tropism, and disease
    • Berger E.A., Murphy P.M., Farber J.M. Chemokine receptors as HIV-1 coreceptors: roles in viral entry, tropism, and disease. Annu. Rev. Immunol. 17:1999;657-700.
    • (1999) Annu. Rev. Immunol. , vol.17 , pp. 657-700
    • Berger, E.A.1    Murphy, P.M.2    Farber, J.M.3
  • 74
    • 0030050591 scopus 로고    scopus 로고
    • Portals of entry: Uncovering HIV nuclear transport pathways
    • Stevenson M. Portals of entry: uncovering HIV nuclear transport pathways. Trends Cell Biol. 6:1996;9-15.
    • (1996) Trends Cell Biol. , vol.6 , pp. 9-15
    • Stevenson, M.1
  • 75
    • 0030972160 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 preintegration complexes: Studies of organization and composition
    • Miller M.D., Farnet C.M., Bushman F.D. Human immunodeficiency virus type 1 preintegration complexes: studies of organization and composition. J. Virol. 71:1997;5382-5390.
    • (1997) J. Virol. , vol.71 , pp. 5382-5390
    • Miller, M.D.1    Farnet, C.M.2    Bushman, F.D.3
  • 76
  • 77
    • 0035875067 scopus 로고    scopus 로고
    • Journey to the center of the cell
    • Cullen B.R. Journey to the center of the cell. Cell. 105:2001;697-700.
    • (2001) Cell , vol.105 , pp. 697-700
    • Cullen, B.R.1
  • 78
    • 0036163845 scopus 로고    scopus 로고
    • Slipping through the door: HIV entry into the nucleus
    • Sherman M.P., Greene W.C. Slipping through the door: HIV entry into the nucleus. Microbes Infect. 4:2002;67-73.
    • (2002) Microbes Infect. , vol.4 , pp. 67-73
    • Sherman, M.P.1    Greene, W.C.2
  • 79
    • 0027376309 scopus 로고
    • A nuclear localization signal within HIV-1 matrix protein that governs infection of non-dividing cells
    • Bukrinsky M., et al. A nuclear localization signal within HIV-1 matrix protein that governs infection of non-dividing cells. Nature. 365:1993;666-669.
    • (1993) Nature , vol.365 , pp. 666-669
    • Bukrinsky, M.1
  • 80
    • 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. Role of the karyopherin pathway in human immunodeficiency virus type 1 nuclear import. J. Virol. 70:1996;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
  • 81
    • 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 R.A.M., Meyer B.E., Simon J.H.M., Fischer U., Malim M.H. 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. 15:1997;4531-4539.
    • (1997) EMBO J. , vol.15 , pp. 4531-4539
    • Fouchier, R.A.M.1    Meyer, B.E.2    Simon, J.H.M.3    Fischer, U.4    Malim, M.H.5
  • 82
    • 0034595514 scopus 로고    scopus 로고
    • Two nuclear localization signals in the HIV-1 matrix protein regulate nuclear import of the HIV-1 pre-integration complex
    • Haffar O.K., Popov S., Dubrovsky L., Agostini I., Tang H., Pushkarsky T., Nadler S.G., Bukrinsky M. Two nuclear localization signals in the HIV-1 matrix protein regulate nuclear import of the HIV-1 pre-integration complex. J. Mol. Biol. 299:2000;359-368.
    • (2000) J. Mol. Biol. , vol.299 , pp. 359-368
    • Haffar, O.K.1    Popov, S.2    Dubrovsky, L.3    Agostini, I.4    Tang, H.5    Pushkarsky, T.6    Nadler, S.G.7    Bukrinsky, M.8
  • 84
    • 0034329417 scopus 로고    scopus 로고
    • Cellular distribution and karyophilic properties of matrix, integrase, and Vpr proteins from the human and simian immunodeficiency viruses
    • Depienne C., Roques P., Creminon C., Fritsch L., Casseron R., Dormont D., Dargemont C., Benichou S. Cellular distribution and karyophilic properties of matrix, integrase, and Vpr proteins from the human and simian immunodeficiency viruses. Exp. Cell Res. 260:2000;387-395.
    • (2000) Exp. Cell Res. , vol.260 , pp. 387-395
    • Depienne, C.1    Roques, P.2    Creminon, C.3    Fritsch, L.4    Casseron, R.5    Dormont, D.6    Dargemont, C.7    Benichou, S.8
  • 85
    • 0028821383 scopus 로고
    • HIV-1 infection of nondividing cells: C-terminal tyrosine phosphorylation of the viral matrix protein is a key regulator
    • Gallay P., Swingler S., Aiken C., Trono D. HIV-1 infection of nondividing cells: C-terminal tyrosine phosphorylation of the viral matrix protein is a key regulator. Cell. 80:1995;379-388.
    • (1995) Cell , vol.80 , pp. 379-388
    • Gallay, P.1    Swingler, S.2    Aiken, C.3    Trono, D.4
  • 86
    • 0028839344 scopus 로고
    • HIV nuclear import is governed by the phosphotyrosine-mediated binding of matrix to the core domain of integrase
    • Gallay P., Swingler S., Song J., Bushman F., Trono D. HIV nuclear import is governed by the phosphotyrosine-mediated binding of matrix to the core domain of integrase. Cell. 83:1995;569-576.
    • (1995) Cell , vol.83 , pp. 569-576
    • Gallay, P.1    Swingler, S.2    Song, J.3    Bushman, F.4    Trono, D.5
  • 87
    • 0030791698 scopus 로고    scopus 로고
    • Human immunodeficiency virus matrix tyrosine phosphorylation: Characterization of the kinase and its substrate requirements
    • Camaur D., Gallay P., Swingler S., Trono D. Human immunodeficiency virus matrix tyrosine phosphorylation: characterization of the kinase and its substrate requirements. J. Virol. 71:1997;6834-6841.
    • (1997) J. Virol. , vol.71 , pp. 6834-6841
    • Camaur, D.1    Gallay, P.2    Swingler, S.3    Trono, D.4
  • 90
    • 0028239060 scopus 로고
    • The Vpr protein of human immunodeficiency virus type 1 influences nuclear localization of viral nucleic acids in nondividing host cells
    • Heinzinger N.K., et al. 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. 91:1994;7311-7315.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7311-7315
    • Heinzinger, N.K.1
  • 91
    • 0032538829 scopus 로고    scopus 로고
    • Characterization of HIV-1 vpr nuclear import: Analysis of signals and pathways
    • Jenkins Y., McEntee M., Weis K., Greene W.C. Characterization of HIV-1 vpr nuclear import: analysis of signals and pathways. J. Cell Biol. 143:1998;875-885.
    • (1998) J. Cell Biol. , vol.143 , pp. 875-885
    • Jenkins, Y.1    McEntee, M.2    Weis, K.3    Greene, W.C.4
  • 92
    • 18844468523 scopus 로고    scopus 로고
    • Viral protein R regulates nuclear import of the HIV-1 pre-integration complex
    • Popov S., et al. Viral protein R regulates nuclear import of the HIV-1 pre-integration complex. EMBO J. 17:1998;909-917.
    • (1998) EMBO J. , vol.17 , pp. 909-917
    • Popov, S.1
  • 93
    • 0031975959 scopus 로고    scopus 로고
    • HIV-1 Vpr interacts with the nuclear transport pathway to promote macrophage infection
    • Vodicka M.A., Koepp D.M., Silver P.A., Emerman M. HIV-1 Vpr interacts with the nuclear transport pathway to promote macrophage infection. Genes Dev. 12:1998;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
  • 94
    • 0032557445 scopus 로고    scopus 로고
    • Viral protein R regulates docking of the HIV-1 preintegration complex to the nuclear pore complex
    • Popov S., Rexach M., Ratner L., Blobel G., Bukrinsky M. Viral protein R regulates docking of the HIV-1 preintegration complex to the nuclear pore complex. J. Biol. Chem. 273:1998;13347-13352.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13347-13352
    • Popov, S.1    Rexach, M.2    Ratner, L.3    Blobel, G.4    Bukrinsky, M.5
  • 96
  • 97
    • 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. HIV-1 infection of nondividing cells through the recognition of integrase by the importin/karyopherin pathway. Proc. Natl. Acad. Sci. USA. 94:1997;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
  • 98
    • 0033526522 scopus 로고    scopus 로고
    • Nuclear localization of human immunodeficiency virus type 1 integrase expressed as a fusion protein with green fluorescent protein
    • Pluymers W., Cherepanov S.D., De Celrq E., Debyser Z. Nuclear localization of human immunodeficiency virus type 1 integrase expressed as a fusion protein with green fluorescent protein. Virology. 258:1999;327-332.
    • (1999) Virology , vol.258 , pp. 327-332
    • Pluymers, W.1    Cherepanov, S.D.2    De Celrq, E.3    Debyser, Z.4
  • 99
    • 0033912323 scopus 로고    scopus 로고
    • The karyophilic properties of human immunodeficiency virus type 1 integrase are not required for nuclear import of proviral DNA
    • Petit C., Schwartz O., Mammano F. The karyophilic properties of human immunodeficiency virus type 1 integrase are not required for nuclear import of proviral DNA. J. Virol. 74:2000;7119-7126.
    • (2000) J. Virol. , vol.74 , pp. 7119-7126
    • Petit, C.1    Schwartz, O.2    Mammano, F.3
  • 103
    • 0028024644 scopus 로고
    • Nuclear import of microinjected influenza virus ribonucleoproteins
    • Kemler I., Whittaker G., Helenius A. Nuclear import of microinjected influenza virus ribonucleoproteins. Virology. 202:1994;1028-1033.
    • (1994) Virology , vol.202 , pp. 1028-1033
    • Kemler, I.1    Whittaker, G.2    Helenius, A.3
  • 104
    • 0026070664 scopus 로고
    • Transport of incoming influenza virus nucleocapsids into the nucleus
    • Martin K., Helenius A. Transport of incoming influenza virus nucleocapsids into the nucleus. J. Virol. 65:1991;232-244.
    • (1991) J. Virol. , vol.65 , pp. 232-244
    • Martin, K.1    Helenius, A.2
  • 105
    • 0019814443 scopus 로고
    • Infectious entry pathway of influenza virus in a canine kidney cell line
    • Matlin K.S., Reggio H., Helenius A., Simons K. Infectious entry pathway of influenza virus in a canine kidney cell line. J. Cell Biol. 91:1981;601-613.
    • (1981) J. Cell Biol. , vol.91 , pp. 601-613
    • Matlin, K.S.1    Reggio, H.2    Helenius, A.3    Simons, K.4
  • 107
    • 0029861558 scopus 로고    scopus 로고
    • Effect of M1 protein and low pH on nuclear transport of influenza virus ribonucleoproteins
    • Bui M., Whittaker G., Helenius A. Effect of M1 protein and low pH on nuclear transport of influenza virus ribonucleoproteins. J. Virol. 70:1996;8391-8401.
    • (1996) J. Virol. , vol.70 , pp. 8391-8401
    • Bui, M.1    Whittaker, G.2    Helenius, A.3
  • 108
    • 0026006258 scopus 로고
    • Nuclear transport of influenza virus ribonucleoproteins: The viral matrix protein (M1) promotes export and inhibits import
    • Martin K., Helenius A. Nuclear transport of influenza virus ribonucleoproteins: the viral matrix protein (M1) promotes export and inhibits import. Cell. 67:1991;117-130.
    • (1991) Cell , vol.67 , pp. 117-130
    • Martin, K.1    Helenius, A.2
  • 109
    • 0029130751 scopus 로고
    • Nuclear import of influenza virus RNA can be mediated by viral nucleoprotein and transport factors required for protein import
    • O'Neill R.E., Jaskunas R., Blobel G., Palese P., Moroianu J. Nuclear import of influenza virus RNA can be mediated by viral nucleoprotein and transport factors required for protein import. J. Biol. Chem. 270:1995;22701-22704.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22701-22704
    • O'Neill, R.E.1    Jaskunas, R.2    Blobel, G.3    Palese, P.4    Moroianu, J.5
  • 110
    • 0031058042 scopus 로고    scopus 로고
    • The NPI-1/NPI-3 (karyopherin alpha) binding site on the influenza a virus nucleoprotein NP is a nonconventional nuclear localization signal
    • Wang P., Palese P., O'Neill R.E. The NPI-1/NPI-3 (karyopherin alpha) binding site on the influenza a virus nucleoprotein NP is a nonconventional nuclear localization signal. J. Virol. 71:1997;1850-1856.
    • (1997) J. Virol. , vol.71 , pp. 1850-1856
    • Wang, P.1    Palese, P.2    O'Neill, R.E.3
  • 111
    • 0030731422 scopus 로고    scopus 로고
    • Nuclear import and export of influenza virus nucleoprotein
    • Neumann G., Castrucci M.R., Kawaoka Y. Nuclear import and export of influenza virus nucleoprotein. J. Virol. 71:1997;9690-9700.
    • (1997) J. Virol. , vol.71 , pp. 9690-9700
    • Neumann, G.1    Castrucci, M.R.2    Kawaoka, Y.3
  • 112
    • 0031950575 scopus 로고    scopus 로고
    • The N-terminal extension of the influenza B virus nucleoprotein is not required for nuclear accumulation or the expression and replication of a model RNA
    • Stevens M.P., Barclay W.S. The N-terminal extension of the influenza B virus nucleoprotein is not required for nuclear accumulation or the expression and replication of a model RNA. J. Virol. 72:1998;5307-5312.
    • (1998) J. Virol. , vol.72 , pp. 5307-5312
    • Stevens, M.P.1    Barclay, W.S.2
  • 113
    • 0032505542 scopus 로고    scopus 로고
    • A classical bipartite nuclear localization signal on Thogoto and influenza A virus nucleoprotein
    • Weber F., Kochs G., Gruber S., Haller O. A classical bipartite nuclear localization signal on Thogoto and influenza A virus nucleoprotein. Virology. 250:1998;8-18.
    • (1998) Virology , vol.250 , pp. 8-18
    • Weber, F.1    Kochs, G.2    Gruber, S.3    Haller, O.4
  • 114
    • 0032981158 scopus 로고    scopus 로고
    • Modulation of nuclear localization of the influenza virus nucleoprotein through interaction with actin filaments
    • Digard P., Elton D., Bishop K., Medcalf E., Pope A. Modulation of nuclear localization of the influenza virus nucleoprotein through interaction with actin filaments. J. Virol. 73:1999;2222-2231.
    • (1999) J. Virol. , vol.73 , pp. 2222-2231
    • Digard, P.1    Elton, D.2    Bishop, K.3    Medcalf, E.4    Pope, A.5
  • 115
    • 0343049028 scopus 로고    scopus 로고
    • Several protein regions contribute to determine the nuclear and cytoplasmic localization of the influenza A virus nucleoprotein
    • Bullido R., Gómez-Puertas P., Albo C., Portela A. Several protein regions contribute to determine the nuclear and cytoplasmic localization of the influenza A virus nucleoprotein. J. Gen. Virol. 81:2000;135-142.
    • (2000) J. Gen. Virol. , vol.81 , pp. 135-142
    • Bullido, R.1    Gómez-Puertas, P.2    Albo, C.3    Portela, A.4
  • 116
    • 0036469888 scopus 로고    scopus 로고
    • Importins fulfil a dual function as nuclear import receptors and cytoplasmic chaperones for exposed basic domains
    • Jakel S., Mingot J.M., Schwarzmaier P., Hartmann E., Gorlich D. Importins fulfil a dual function as nuclear import receptors and cytoplasmic chaperones for exposed basic domains. EMBO J. 21:2002;377-386.
    • (2002) EMBO J. , vol.21 , pp. 377-386
    • Jakel, S.1    Mingot, J.M.2    Schwarzmaier, P.3    Hartmann, E.4    Gorlich, D.5
  • 117
    • 0026497478 scopus 로고
    • Borna disease virus, a negative-strand RNA virus, transcribes in the nucleus of infected cells
    • Briese T., de la Torre J., Lewis A., Ludwig H., Lipkin W.I. Borna disease virus, a negative-strand RNA virus, transcribes in the nucleus of infected cells. Proc. Natl. Acad. Sci. USA. 89:1992;11486-11489.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11486-11489
    • Briese, T.1    De la Torre, J.2    Lewis, A.3    Ludwig, H.4    Lipkin, W.I.5
  • 118
    • 0030725201 scopus 로고    scopus 로고
    • Amantadine does not have antiviral activity against Borna disease virus
    • Cubitt B., de la Torre J.C. Amantadine does not have antiviral activity against Borna disease virus. Arch. Virol. 142:1997;2035-2042.
    • (1997) Arch. Virol. , vol.142 , pp. 2035-2042
    • Cubitt, B.1    De la Torre, J.C.2
  • 119
    • 0030726384 scopus 로고    scopus 로고
    • Borna disease virus is not sensitive to amantadine
    • Hallensleben W., Zocher M., Staehli P. Borna disease virus is not sensitive to amantadine. Arch. Virol. 142:1997;2043-2048.
    • (1997) Arch. Virol. , vol.142 , pp. 2043-2048
    • Hallensleben, W.1    Zocher, M.2    Staehli, P.3
  • 120
    • 0032918491 scopus 로고    scopus 로고
    • Characterization of the major nuclear localization signal of the Borna disease virus phosphoprotein
    • Schwemmle M., Jehle C., Shoemaker T., Lipkin W.I. Characterization of the major nuclear localization signal of the Borna disease virus phosphoprotein. J. Gen. Virol. 80:1999;97-100.
    • (1999) J. Gen. Virol. , vol.80 , pp. 97-100
    • Schwemmle, M.1    Jehle, C.2    Shoemaker, T.3    Lipkin, W.I.4
  • 121
    • 0037023770 scopus 로고    scopus 로고
    • Characterization of an unusual importin alpha binding motif in the borna disease virus p10 protein that directs nuclear import
    • Wolff T., Unterstab G., Heins G., Richt J.A., Kann M. Characterization of an unusual importin alpha binding motif in the borna disease virus p10 protein that directs nuclear import. J. Biol. Chem. 277:2002;12151-12157.
    • (2002) J. Biol. Chem. , vol.277 , pp. 12151-12157
    • Wolff, T.1    Unterstab, G.2    Heins, G.3    Richt, J.A.4    Kann, M.5
  • 122
    • 0027325777 scopus 로고
    • Mx-proteins: GTPases with antiviral activity
    • Staeheli P., Pavlovic J. Mx-proteins: GTPases with antiviral activity. Trends Cell Biol. 3:1993;268-272.
    • (1993) Trends Cell Biol. , vol.3 , pp. 268-272
    • Staeheli, P.1    Pavlovic, J.2
  • 123
    • 0033548268 scopus 로고    scopus 로고
    • GTP-bound human MxA protein interacts with the nucleocapsids of Thogoto virus (Orthomyxoviridae)
    • Kochs G., Haller O. GTP-bound human MxA protein interacts with the nucleocapsids of Thogoto virus (Orthomyxoviridae). J. Biol. Chem. 274:1999;4370-4376.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4370-4376
    • Kochs, G.1    Haller, O.2
  • 124
  • 125
    • 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
    • Haffar O.K., Smithgall M.D., Popov S., Ulrich P., Bruce A.G., Nadler S.G., Cerami A., Bukrinsky M.I. 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. 42:1998;1133-1138.
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 1133-1138
    • Haffar, O.K.1    Smithgall, M.D.2    Popov, S.3    Ulrich, P.4    Bruce, A.G.5    Nadler, S.G.6    Cerami, A.7    Bukrinsky, M.I.8
  • 126
    • 0033830427 scopus 로고    scopus 로고
    • Small molecule inhibitor of HIV-1 nuclear import suppresses HIV-1 replication in human lymphoid tissue ex vivo: A potential addition to current anti-HIV drug repertoire
    • Glushakova S., Dubrovsky L., Grivel J., Haffar O., Bukrinsky M. Small molecule inhibitor of HIV-1 nuclear import suppresses HIV-1 replication in human lymphoid tissue ex vivo: a potential addition to current anti-HIV drug repertoire. Antiviral Res. 47:2000;89-95.
    • (2000) Antiviral Res. , vol.47 , pp. 89-95
    • Glushakova, S.1    Dubrovsky, L.2    Grivel, J.3    Haffar, O.4    Bukrinsky, M.5
  • 127
    • 0032554629 scopus 로고    scopus 로고
    • Backbone cyclic peptide, which mimics the nuclear localization signal of human immunodeficiency virus type 1 matrix protein, inhibits nuclear import and virus production in nondividing cells
    • Friedler A., Zakai N., Karni O., Broder Y.C., Baraz L., Kotler M., Loyter A., Gilon C. Backbone cyclic peptide, which mimics the nuclear localization signal of human immunodeficiency virus type 1 matrix protein, inhibits nuclear import and virus production in nondividing cells. Biochemistry. 37:1999;5616-5622.
    • (1999) Biochemistry , vol.37 , pp. 5616-5622
    • Friedler, A.1    Zakai, N.2    Karni, O.3    Broder, Y.C.4    Baraz, L.5    Kotler, M.6    Loyter, A.7    Gilon, C.8
  • 128
    • 0036196670 scopus 로고    scopus 로고
    • Protein and RNA export from the nucleus
    • Lei E.P., Silver P.A. Protein and RNA export from the nucleus. Dev. Cell. 2:2002;261-272.
    • (2002) Dev. Cell , vol.2 , pp. 261-272
    • Lei, E.P.1    Silver, P.A.2


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