메뉴 건너뛰기




Volumn 34, Issue , 2015, Pages 113-121

Viruses and the nuclear envelope

Author keywords

[No Author keywords available]

Indexed keywords

DYNEIN ADENOSINE TRIPHOSPHATASE; HISTONE H1; IMPORTIN 7; KARYOPHERIN; KARYOPHERIN BETA; KINESIN 1; LAMIN A; LAMIN C; UNCLASSIFIED DRUG;

EID: 84932631293     PISSN: 09550674     EISSN: 18790410     Source Type: Journal    
DOI: 10.1016/j.ceb.2015.06.002     Document Type: Review
Times cited : (24)

References (114)
  • 2
    • 84865983670 scopus 로고    scopus 로고
    • Effect of viral infection on the nuclear envelope and nuclear pore complex
    • Cohen S., Etingov I., Pante N. Effect of viral infection on the nuclear envelope and nuclear pore complex. Int Rev Cell Mol Biol 2012, 299:117-159.
    • (2012) Int Rev Cell Mol Biol , vol.299 , pp. 117-159
    • Cohen, S.1    Etingov, I.2    Pante, N.3
  • 3
    • 84872478119 scopus 로고    scopus 로고
    • Virus strategies for passing the nuclear envelope barrier
    • Kobiler O., Drayman N., Butin-Israeli V., Oppenheim A. Virus strategies for passing the nuclear envelope barrier. Nucleus 2012, 3:526-539.
    • (2012) Nucleus , vol.3 , pp. 526-539
    • Kobiler, O.1    Drayman, N.2    Butin-Israeli, V.3    Oppenheim, A.4
  • 4
    • 67649422214 scopus 로고    scopus 로고
    • DNA-tumor virus entry-from plasma membrane to the nucleus
    • Greber U.F., Puntener D. DNA-tumor virus entry-from plasma membrane to the nucleus. Seminars Cell Dev Biol 2009, 20:631-642.
    • (2009) Seminars Cell Dev Biol , vol.20 , pp. 631-642
    • Greber, U.F.1    Puntener, D.2
  • 7
    • 0038187637 scopus 로고    scopus 로고
    • Nuclear import of viral DNA genomes
    • Greber U.F., Fassati A. Nuclear import of viral DNA genomes. Traffic 2003, 4:136-143.
    • (2003) Traffic , vol.4 , pp. 136-143
    • Greber, U.F.1    Fassati, A.2
  • 8
    • 80052336130 scopus 로고    scopus 로고
    • Transportin 3 promotes a nuclear maturation step required for efficient HIV-1 integration
    • Zhou L., Sokolskaja E., Jolly C., et al. Transportin 3 promotes a nuclear maturation step required for efficient HIV-1 integration. PLoS Pathogens 2011, 7:e1002194.
    • (2011) PLoS Pathogens , vol.7 , pp. e1002194
    • Zhou, L.1    Sokolskaja, E.2    Jolly, C.3
  • 9
    • 79958238205 scopus 로고    scopus 로고
    • HIV-1 remodels the nuclear pore complex
    • Monette A., Pante N., Mouland A.J. HIV-1 remodels the nuclear pore complex. J Cell Biol 2011, 193:619-631.
    • (2011) J Cell Biol , vol.193 , pp. 619-631
    • Monette, A.1    Pante, N.2    Mouland, A.J.3
  • 10
    • 70149101538 scopus 로고    scopus 로고
    • Nuclear entry of hepatitis B virus capsids involves disintegration to protein dimers followed by nuclear reassociation to capsids
    • Rabe B., Delaleau M., Bischof A., et al. Nuclear entry of hepatitis B virus capsids involves disintegration to protein dimers followed by nuclear reassociation to capsids. PLoS Pathogens 2009, 5:e1000563.
    • (2009) PLoS Pathogens , vol.5 , pp. e1000563
    • Rabe, B.1    Delaleau, M.2    Bischof, A.3
  • 11
    • 0033526096 scopus 로고    scopus 로고
    • Phosphorylation-dependent binding of hepatitis B virus core particles to the nuclear pore complex
    • Kann M., Sodeik B., Vlachou A., et al. Phosphorylation-dependent binding of hepatitis B virus core particles to the nuclear pore complex. J Cell Biol 1999, 145:45-55.
    • (1999) J Cell Biol , vol.145 , pp. 45-55
    • Kann, M.1    Sodeik, B.2    Vlachou, A.3
  • 12
    • 79960927856 scopus 로고    scopus 로고
    • Strategies to inhibit viral protein nuclear import: HIV-1 as a target
    • Levin A., Loyter A., Bukrinsky M. Strategies to inhibit viral protein nuclear import: HIV-1 as a target. Biochim Biophys Acta 2011, 1813:1646-1653.
    • (2011) Biochim Biophys Acta , vol.1813 , pp. 1646-1653
    • Levin, A.1    Loyter, A.2    Bukrinsky, M.3
  • 13
    • 79960897397 scopus 로고    scopus 로고
    • How viruses access the nucleus
    • Cohen S., Au S., Pante N. How viruses access the nucleus. Biochim Biophys Acta 2011, 1813:1634-1645.
    • (2011) Biochim Biophys Acta , vol.1813 , pp. 1634-1645
    • Cohen, S.1    Au, S.2    Pante, N.3
  • 14
    • 73449134082 scopus 로고    scopus 로고
    • Three-dimensional visualization of gammaherpesvirus life cycle in host cells by electron tomography
    • Peng L., Ryazantsev S., Sun R., Zhou Z.H. Three-dimensional visualization of gammaherpesvirus life cycle in host cells by electron tomography. Structure 2010, 18:47-58.
    • (2010) Structure , vol.18 , pp. 47-58
    • Peng, L.1    Ryazantsev, S.2    Sun, R.3    Zhou, Z.H.4
  • 15
    • 13944272582 scopus 로고    scopus 로고
    • Entry of pseudorabies virus: an immunogold-labeling study
    • Granzow H., Klupp B.G., Mettenleiter T.C. Entry of pseudorabies virus: an immunogold-labeling study. J Virol 2005, 79:3200-3205.
    • (2005) J Virol , vol.79 , pp. 3200-3205
    • Granzow, H.1    Klupp, B.G.2    Mettenleiter, T.C.3
  • 16
    • 1842862375 scopus 로고    scopus 로고
    • The role of the cytoskeleton during viral infection
    • Dohner K., Sodeik B. The role of the cytoskeleton during viral infection. Curr Top Microbiol Immunol 2005, 285:67-108.
    • (2005) Curr Top Microbiol Immunol , vol.285 , pp. 67-108
    • Dohner, K.1    Sodeik, B.2
  • 17
    • 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., et al. 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 2000, 20:4922-4931.
    • (2000) Mol Cell Biol , vol.20 , pp. 4922-4931
    • Ojala, P.M.1    Sodeik, B.2    Ebersold, M.W.3
  • 18
    • 0030875903 scopus 로고    scopus 로고
    • The role of the nuclear pore complex in adenovirus DNA entry
    • Greber U.F., Suomalainen M., Stidwill R.P., et al. The role of the nuclear pore complex in adenovirus DNA entry. EMBO J 1997, 16:5998-6007.
    • (1997) EMBO J , vol.16 , pp. 5998-6007
    • Greber, U.F.1    Suomalainen, M.2    Stidwill, R.P.3
  • 19
    • 80052975075 scopus 로고    scopus 로고
    • Kinesin-1-mediated capsid disassembly and disruption of the nuclear pore complex promote virus infection
    • Strunze S., Engelke M.F., Wang I.H., et al. Kinesin-1-mediated capsid disassembly and disruption of the nuclear pore complex promote virus infection. Cell Host Microbe 2011, 10:210-223.
    • (2011) Cell Host Microbe , vol.10 , pp. 210-223
    • Strunze, S.1    Engelke, M.F.2    Wang, I.H.3
  • 20
    • 77958028568 scopus 로고    scopus 로고
    • The nuclear pore complex: a new dynamic in HIV-1 replication
    • Woodward C.L., Chow S.A. The nuclear pore complex: a new dynamic in HIV-1 replication. Nucleus 2010, 1:18-22.
    • (2010) Nucleus , vol.1 , pp. 18-22
    • Woodward, C.L.1    Chow, S.A.2
  • 21
    • 84897965284 scopus 로고    scopus 로고
    • HIV-1 uncoating: connection to nuclear entry and regulation by host proteins
    • Ambrose Z., Aiken C. HIV-1 uncoating: connection to nuclear entry and regulation by host proteins. Virology 2014, 454-455:371-379.
    • (2014) Virology , vol.454-455 , pp. 371-379
    • Ambrose, Z.1    Aiken, C.2
  • 22
    • 34250363900 scopus 로고    scopus 로고
    • Nuclear import of influenza A viral ribonucleoprotein complexes is mediated by two nuclear localization sequences on viral nucleoprotein
    • Wu W.W., Sun Y.H., Pante N. Nuclear import of influenza A viral ribonucleoprotein complexes is mediated by two nuclear localization sequences on viral nucleoprotein. Virol J 2007, 4:49.
    • (2007) Virol J , vol.4 , pp. 49
    • Wu, W.W.1    Sun, Y.H.2    Pante, N.3
  • 23
    • 14544270958 scopus 로고    scopus 로고
    • An unconventional NLS is critical for the nuclear import of the influenza A virus nucleoprotein and ribonucleoprotein
    • Cros J.F., Garcia-Sastre A., Palese P. An unconventional NLS is critical for the nuclear import of the influenza A virus nucleoprotein and ribonucleoprotein. Traffic 2005, 6:205-213.
    • (2005) Traffic , vol.6 , pp. 205-213
    • Cros, J.F.1    Garcia-Sastre, A.2    Palese, P.3
  • 24
    • 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 1997, 71:1850-1856.
    • (1997) J Virol , vol.71 , pp. 1850-1856
    • Wang, P.1    Palese, P.2    O'Neill, R.E.3
  • 25
    • 84866184239 scopus 로고    scopus 로고
    • A Nuclear localization signal in herpesvirus protein VP1-2 is essential for infection via capsid routing to the nuclear pore
    • Abaitua F., Hollinshead M., Bolstad M., et al. A Nuclear localization signal in herpesvirus protein VP1-2 is essential for infection via capsid routing to the nuclear pore. J Virol 2012, 86:8998-9014.
    • (2012) J Virol , vol.86 , pp. 8998-9014
    • Abaitua, F.1    Hollinshead, M.2    Bolstad, M.3
  • 26
    • 79551691992 scopus 로고    scopus 로고
    • A single mutation responsible for temperature sensitive entry and assembly defects in the VP1-2 protein of HSV
    • Abaitua F., Daikoku T., Crump C.M., et al. A single mutation responsible for temperature sensitive entry and assembly defects in the VP1-2 protein of HSV. J Virol 2011, 85:2024-2036.
    • (2011) J Virol , vol.85 , pp. 2024-2036
    • Abaitua, F.1    Daikoku, T.2    Crump, C.M.3
  • 27
    • 67749104672 scopus 로고    scopus 로고
    • Time-dependent transformation of the herpesvirus tegument
    • Newcomb W.W., Brown J.C. Time-dependent transformation of the herpesvirus tegument. J Virol 2009, 83:8082-8089.
    • (2009) J Virol , vol.83 , pp. 8082-8089
    • Newcomb, W.W.1    Brown, J.C.2
  • 28
    • 67449089967 scopus 로고    scopus 로고
    • Herpesvirus capsid association with the nuclear pore complex and viral DNA release involve the nucleoporin CAN/Nup214 and the capsid protein pUL25
    • Pasdeloup D., Blondel D., Isidro A.L., Rixon F.J. Herpesvirus capsid association with the nuclear pore complex and viral DNA release involve the nucleoporin CAN/Nup214 and the capsid protein pUL25. J Virol 2009, 83:6610-6623.
    • (2009) J Virol , vol.83 , pp. 6610-6623
    • Pasdeloup, D.1    Blondel, D.2    Isidro, A.L.3    Rixon, F.J.4
  • 29
    • 0027376309 scopus 로고
    • A nuclear localization signal within HIV-1 matrix protein that governs infection of non-dividing cells
    • Bukrinsky M.I., Haggerty S., Dempsey M.P., et al. A nuclear localization signal within HIV-1 matrix protein that governs infection of non-dividing cells. Nature 1993, 365:666-669.
    • (1993) Nature , vol.365 , pp. 666-669
    • Bukrinsky, M.I.1    Haggerty, S.2    Dempsey, M.P.3
  • 30
    • 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 R.S., Trono D. 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 1994, 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
  • 31
    • 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 1998, 143:875-885.
    • (1998) J Cell Biol , vol.143 , pp. 875-885
    • Jenkins, Y.1    McEntee, M.2    Weis, K.3    Greene, W.C.4
  • 32
    • 0035947658 scopus 로고    scopus 로고
    • Characterization of the nuclear import pathway for HIV-1 integrase
    • Depienne C., Mousnier A., Leh H., et al. Characterization of the nuclear import pathway for HIV-1 integrase. J Biol Chem 2001, 276:18102-18107.
    • (2001) J Biol Chem , vol.276 , pp. 18102-18107
    • Depienne, C.1    Mousnier, A.2    Leh, H.3
  • 33
    • 0347298811 scopus 로고    scopus 로고
    • Docking of HIV-1 Vpr to the nuclear envelope is mediated by the interaction with the nucleoporin hCG1
    • Le Rouzic E., Mousnier A., Rustum C., et al. Docking of HIV-1 Vpr to the nuclear envelope is mediated by the interaction with the nucleoporin hCG1. J Biol Chem 2002, 277:45091-45098.
    • (2002) J Biol Chem , vol.277 , pp. 45091-45098
    • Le Rouzic, E.1    Mousnier, A.2    Rustum, C.3
  • 34
    • 0034646513 scopus 로고    scopus 로고
    • HIV-1 genome nuclear import is mediated by a central DNA flap
    • Zennou V., Petit C., Guetard D., et al. HIV-1 genome nuclear import is mediated by a central DNA flap. Cell 2000, 101:173-185.
    • (2000) Cell , vol.101 , pp. 173-185
    • Zennou, V.1    Petit, C.2    Guetard, D.3
  • 35
    • 78751622104 scopus 로고    scopus 로고
    • Differential use of importin-alpha isoforms governs cell tropism and host adaptation of influenza virus
    • Gabriel G., Klingel K., Otte A., et al. Differential use of importin-alpha isoforms governs cell tropism and host adaptation of influenza virus. Nat Commun 2011, 2:156.
    • (2011) Nat Commun , vol.2 , pp. 156
    • Gabriel, G.1    Klingel, K.2    Otte, A.3
  • 36
    • 77956528167 scopus 로고    scopus 로고
    • Cellular networks involved in the influenza virus life cycle
    • Watanabe T., Watanabe S., Kawaoka Y. Cellular networks involved in the influenza virus life cycle. Cell Host Microbe 2010, 7:427-439.
    • (2010) Cell Host Microbe , vol.7 , pp. 427-439
    • Watanabe, T.1    Watanabe, S.2    Kawaoka, Y.3
  • 37
    • 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., et al. Import of adenovirus DNA involves the nuclear pore complex receptor CAN/Nup214 and histone H1. Nat Cell Biol 2001, 3:1092-1100.
    • (2001) Nat Cell Biol , vol.3 , pp. 1092-1100
    • Trotman, L.C.1    Mosberger, N.2    Fornerod, M.3
  • 38
    • 33748925256 scopus 로고    scopus 로고
    • Adenovirus core protein pVII is translocated into the nucleus by multiple import receptor pathways
    • Wodrich H., Cassany A., D'Angelo M.A., et al. Adenovirus core protein pVII is translocated into the nucleus by multiple import receptor pathways. J Virol 2006, 80:9608-9618.
    • (2006) J Virol , vol.80 , pp. 9608-9618
    • Wodrich, H.1    Cassany, A.2    D'Angelo, M.A.3
  • 39
    • 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 2002, 13:425-434.
    • (2002) Mol Biol Cell , vol.13 , pp. 425-434
    • Pante, N.1    Kann, M.2
  • 40
    • 33750279611 scopus 로고    scopus 로고
    • Parvoviral nuclear import: bypassing the host nuclear-transport machinery
    • Cohen S., Behzad A.R., Carroll J.B., Pante N. Parvoviral nuclear import: bypassing the host nuclear-transport machinery. J Gen Virol 2006, 87:3209-3213.
    • (2006) J Gen Virol , vol.87 , pp. 3209-3213
    • Cohen, S.1    Behzad, A.R.2    Carroll, J.B.3    Pante, N.4
  • 42
    • 84887273668 scopus 로고    scopus 로고
    • Parvoviruses cause nuclear envelope breakdown by activating key enzymes of mitosis
    • Porwal M., Cohen S., Snoussi K., et al. Parvoviruses cause nuclear envelope breakdown by activating key enzymes of mitosis. PLoS Pathogens 2013, 9:e1003671.
    • (2013) PLoS Pathogens , vol.9 , pp. e1003671
    • Porwal, M.1    Cohen, S.2    Snoussi, K.3
  • 43
    • 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 1989, 109:2721-2729.
    • (1989) J Cell Biol , vol.109 , pp. 2721-2729
    • Kartenbeck, J.1    Stukenbrok, H.2    Helenius, A.3
  • 44
    • 84862989117 scopus 로고    scopus 로고
    • GM1 structure determines SV40-induced membrane invagination and infection
    • Ewers H., Romer W., Smith A.E., et al. GM1 structure determines SV40-induced membrane invagination and infection. Nat Cell Biol 2010, 12:11-12.
    • (2010) Nat Cell Biol , vol.12 , pp. 11-12
    • Ewers, H.1    Romer, W.2    Smith, A.E.3
  • 45
    • 0042691217 scopus 로고    scopus 로고
    • Gangliosides are receptors for murine polyoma virus and SV40
    • Tsai B., Gilbert J.M., Stehle T., et al. Gangliosides are receptors for murine polyoma virus and SV40. EMBO J 2003, 22:4346-4355.
    • (2003) EMBO J , vol.22 , pp. 4346-4355
    • Tsai, B.1    Gilbert, J.M.2    Stehle, T.3
  • 46
    • 79955436301 scopus 로고    scopus 로고
    • Role of endosomes in simian virus 40 entry and infection
    • Engel S., Heger T., Mancini R., et al. Role of endosomes in simian virus 40 entry and infection. J Virol 2011, 85:4198-4211.
    • (2011) J Virol , vol.85 , pp. 4198-4211
    • Engel, S.1    Heger, T.2    Mancini, R.3
  • 47
    • 80455143829 scopus 로고    scopus 로고
    • BAP31 and BiP are essential for dislocation of SV40 from the endoplasmic reticulum to the cytosol
    • Geiger R., Andritschke D., Friebe S., et al. BAP31 and BiP are essential for dislocation of SV40 from the endoplasmic reticulum to the cytosol. Nat Cell Biol 2011, 13:1305-1314.
    • (2011) Nat Cell Biol , vol.13 , pp. 1305-1314
    • Geiger, R.1    Andritschke, D.2    Friebe, S.3
  • 48
    • 26944450514 scopus 로고    scopus 로고
    • ERp29 triggers a conformational change in polyomavirus to stimulate membrane binding
    • Magnuson B., Rainey E.K., Benjamin T., et al. ERp29 triggers a conformational change in polyomavirus to stimulate membrane binding. Mol Cell 2005, 20:289-300.
    • (2005) Mol Cell , vol.20 , pp. 289-300
    • Magnuson, B.1    Rainey, E.K.2    Benjamin, T.3
  • 49
    • 36348964305 scopus 로고    scopus 로고
    • A chaperone-activated nonenveloped virus perforates the physiologically relevant endoplasmic reticulum membrane
    • Rainey-Barger E.K., Magnuson B., Tsai B. A chaperone-activated nonenveloped virus perforates the physiologically relevant endoplasmic reticulum membrane. J Virol 2007, 81:12996-13004.
    • (2007) J Virol , vol.81 , pp. 12996-13004
    • Rainey-Barger, E.K.1    Magnuson, B.2    Tsai, B.3
  • 50
    • 33845655873 scopus 로고    scopus 로고
    • VP3 insertion into ER membranes is controlled by the capsid protein VP1: implications for DNA translocation out of the ER
    • Daniels R., Rusan N.M., Wadsworth P., Hebert D.N., SV40 VP2 VP3 insertion into ER membranes is controlled by the capsid protein VP1: implications for DNA translocation out of the ER. Mol Cell 2006, 24:955-966.
    • (2006) Mol Cell , vol.24 , pp. 955-966
    • Daniels, R.1    Rusan, N.M.2    Wadsworth, P.3    Hebert, D.N.4    SV40, VP25
  • 51
    • 84884808978 scopus 로고    scopus 로고
    • Viroporins customize host cells for efficient viral propagation
    • Giorda K.M., Hebert D.N. Viroporins customize host cells for efficient viral propagation. DNA Cell Biol 2013, 32:557-564.
    • (2013) DNA Cell Biol , vol.32 , pp. 557-564
    • Giorda, K.M.1    Hebert, D.N.2
  • 52
    • 0030053585 scopus 로고    scopus 로고
    • Association with capsid proteins promotes nuclear targeting of simian virus 40 DNA
    • Nakanishi A., Clever J., Yamada M., et al. Association with capsid proteins promotes nuclear targeting of simian virus 40 DNA. Proc Natl Acad Sci USA 1996, 93:96-100.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 96-100
    • Nakanishi, A.1    Clever, J.2    Yamada, M.3
  • 53
    • 33846829982 scopus 로고    scopus 로고
    • Molecular dissection of nuclear entry-competent SV40 during infection
    • Nakanishi A., Li P.P., Qu Q., et al. Molecular dissection of nuclear entry-competent SV40 during infection. Virus Res 2007, 124:226-230.
    • (2007) Virus Res , vol.124 , pp. 226-230
    • Nakanishi, A.1    Li, P.P.2    Qu, Q.3
  • 54
    • 0036720837 scopus 로고    scopus 로고
    • Interaction of the Vp3 nuclear localization signal with the importin alpha 2/beta heterodimer directs nuclear entry of infecting simian virus 40
    • Nakanishi A., Shum D., Morioka H., et al. Interaction of the Vp3 nuclear localization signal with the importin alpha 2/beta heterodimer directs nuclear entry of infecting simian virus 40. J Virol 2002, 76:9368-9377.
    • (2002) J Virol , vol.76 , pp. 9368-9377
    • Nakanishi, A.1    Shum, D.2    Morioka, H.3
  • 55
    • 83455163834 scopus 로고    scopus 로고
    • Simian virus 40 induces lamin A/C fluctuations and nuclear envelope deformation during cell entry
    • Butin-Israeli V., Ben-nun-Shaul O., Kopatz I., et al. Simian virus 40 induces lamin A/C fluctuations and nuclear envelope deformation during cell entry. Nucleus 2011, 2:320-330.
    • (2011) Nucleus , vol.2 , pp. 320-330
    • Butin-Israeli, V.1    Ben-nun-Shaul, O.2    Kopatz, I.3
  • 56
    • 2642520334 scopus 로고    scopus 로고
    • Novel nuclear herniations induced by nuclear localization of a viral protein
    • Hoyt C.C., Bouchard R.J., Tyler K.L. Novel nuclear herniations induced by nuclear localization of a viral protein. J Virol 2004, 78:6360-6369.
    • (2004) J Virol , vol.78 , pp. 6360-6369
    • Hoyt, C.C.1    Bouchard, R.J.2    Tyler, K.L.3
  • 57
    • 11344285489 scopus 로고    scopus 로고
    • VSV disrupts the Rae1/mrnp41 mRNA nuclear export pathway
    • Faria P.A., Chakraborty P., Levay A., et al. VSV disrupts the Rae1/mrnp41 mRNA nuclear export pathway. Mol Cell 2005, 17:93-102.
    • (2005) Mol Cell , vol.17 , pp. 93-102
    • Faria, P.A.1    Chakraborty, P.2    Levay, A.3
  • 58
    • 84866932844 scopus 로고    scopus 로고
    • Complexes of vesicular stomatitis virus matrix protein with host Rae1 and Nup98 involved in inhibition of host transcription
    • Rajani K.R., Pettit Kneller E.L., McKenzie M.O., et al. Complexes of vesicular stomatitis virus matrix protein with host Rae1 and Nup98 involved in inhibition of host transcription. PLoS Pathogens 2012, 8:e1002929.
    • (2012) PLoS Pathogens , vol.8 , pp. e1002929
    • Rajani, K.R.1    Pettit Kneller, E.L.2    McKenzie, M.O.3
  • 59
    • 4444274231 scopus 로고    scopus 로고
    • Bidirectional increase in permeability of nuclear envelope upon poliovirus infection and accompanying alterations of nuclear pores
    • Belov G.A., Lidsky P.V., Mikitas O.V., et al. Bidirectional increase in permeability of nuclear envelope upon poliovirus infection and accompanying alterations of nuclear pores. J Virol 2004, 78:10166-10177.
    • (2004) J Virol , vol.78 , pp. 10166-10177
    • Belov, G.A.1    Lidsky, P.V.2    Mikitas, O.V.3
  • 60
    • 0035863125 scopus 로고    scopus 로고
    • Effects of poliovirus infection on nucleo-cytoplasmic trafficking and nuclear pore complex composition
    • Gustin K.E., Sarnow P. Effects of poliovirus infection on nucleo-cytoplasmic trafficking and nuclear pore complex composition. EMBO J 2001, 20:240-249.
    • (2001) EMBO J , vol.20 , pp. 240-249
    • Gustin, K.E.1    Sarnow, P.2
  • 61
    • 33646754920 scopus 로고    scopus 로고
    • Ebola virus VP24 binds karyopherin alpha1 and blocks STAT1 nuclear accumulation
    • Reid S.P., Leung L.W., Hartman A.L., et al. Ebola virus VP24 binds karyopherin alpha1 and blocks STAT1 nuclear accumulation. J Virol 2006, 80:5156-5167.
    • (2006) J Virol , vol.80 , pp. 5156-5167
    • Reid, S.P.1    Leung, L.W.2    Hartman, A.L.3
  • 62
    • 77953302554 scopus 로고    scopus 로고
    • Escape of herpesviruses from the nucleus
    • Lee C.P., Chen M.R. Escape of herpesviruses from the nucleus. Rev Med Virol 2010, 20:214-230.
    • (2010) Rev Med Virol , vol.20 , pp. 214-230
    • Lee, C.P.1    Chen, M.R.2
  • 64
    • 84872616937 scopus 로고    scopus 로고
    • The way out: what we know and do not know about herpesvirus nuclear egress
    • Mettenleiter T.C., Muller F., Granzow H., Klupp B.G. The way out: what we know and do not know about herpesvirus nuclear egress. Cell Microbiol 2013, 15:170-178.
    • (2013) Cell Microbiol , vol.15 , pp. 170-178
    • Mettenleiter, T.C.1    Muller, F.2    Granzow, H.3    Klupp, B.G.4
  • 65
    • 0034892692 scopus 로고    scopus 로고
    • Fate of the inner nuclear membrane protein lamin B receptor and nuclear lamins in herpes simplex virus type 1 infection
    • Scott E.S., O'Hare P. Fate of the inner nuclear membrane protein lamin B receptor and nuclear lamins in herpes simplex virus type 1 infection. J Virol 2001, 75:8818-8830.
    • (2001) J Virol , vol.75 , pp. 8818-8830
    • Scott, E.S.1    O'Hare, P.2
  • 66
    • 0037008483 scopus 로고    scopus 로고
    • Cytomegalovirus recruitment of cellular kinases to dissolve the nuclear lamina
    • Muranyi W., Haas J., Wagner M., et al. Cytomegalovirus recruitment of cellular kinases to dissolve the nuclear lamina. Science 2002, 297:854-857.
    • (2002) Science , vol.297 , pp. 854-857
    • Muranyi, W.1    Haas, J.2    Wagner, M.3
  • 67
    • 2442719000 scopus 로고    scopus 로고
    • Herpes Simplex Virus 1 UL31 and UL34 gene products promote the late maturation of viral replication compartments to the nuclear periphery
    • Simpson-Holley M., Baines J., Roller R., Knipe D.M. Herpes Simplex Virus 1 UL31 and UL34 gene products promote the late maturation of viral replication compartments to the nuclear periphery. J Virol 2004, 78:5591-5600.
    • (2004) J Virol , vol.78 , pp. 5591-5600
    • Simpson-Holley, M.1    Baines, J.2    Roller, R.3    Knipe, D.M.4
  • 68
    • 33646018621 scopus 로고    scopus 로고
    • Roles for herpes simplex virus type 1 UL34 and US3 proteins in disrupting the nuclear lamina during herpes simplex virus type 1 egress
    • Bjerke S.L., Roller R.J. Roles for herpes simplex virus type 1 UL34 and US3 proteins in disrupting the nuclear lamina during herpes simplex virus type 1 egress. Virology 2006, 347:261-276.
    • (2006) Virology , vol.347 , pp. 261-276
    • Bjerke, S.L.1    Roller, R.J.2
  • 69
    • 0035087651 scopus 로고    scopus 로고
    • Egress of alphaherpesviruses: comparative ultrastructural study
    • Granzow H., Klupp B.G., Fuchs W., et al. Egress of alphaherpesviruses: comparative ultrastructural study. J Virol 2001, 75:3675-3684.
    • (2001) J Virol , vol.75 , pp. 3675-3684
    • Granzow, H.1    Klupp, B.G.2    Fuchs, W.3
  • 70
    • 31144448686 scopus 로고    scopus 로고
    • Egress of alphaherpesviruses
    • Mettenleiter T.C., Minson T. Egress of alphaherpesviruses. J Virol 2006, 80:1610-1611.
    • (2006) J Virol , vol.80 , pp. 1610-1611
    • Mettenleiter, T.C.1    Minson, T.2
  • 71
    • 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 1998, 51:237-347.
    • (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
  • 72
    • 0035024157 scopus 로고    scopus 로고
    • Herpes simplex virus nucleocapsids mature to progeny virions by an envelopment→deenvelopment→reenvelopment pathway
    • Skepper J.N., Whiteley A., Browne H., Minson A. Herpes simplex virus nucleocapsids mature to progeny virions by an envelopment→deenvelopment→reenvelopment pathway. J Virol 2001, 75:5697-5702.
    • (2001) J Virol , vol.75 , pp. 5697-5702
    • Skepper, J.N.1    Whiteley, A.2    Browne, H.3    Minson, A.4
  • 73
    • 84868587398 scopus 로고    scopus 로고
    • Endocytic tubules regulated by Rab GTPases 5 and 11 are used for envelopment of herpes simplex virus
    • Hollinshead M., Johns H.L., Sayers C.L., et al. Endocytic tubules regulated by Rab GTPases 5 and 11 are used for envelopment of herpes simplex virus. EMBO J 2012, 31:4204-4220.
    • (2012) EMBO J , vol.31 , pp. 4204-4220
    • Hollinshead, M.1    Johns, H.L.2    Sayers, C.L.3
  • 74
    • 34447265020 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 cytoplasmic envelopment requires functional Vps4
    • Crump C.M., Yates C., Minson T. Herpes simplex virus type 1 cytoplasmic envelopment requires functional Vps4. J Virol 2007, 81:7380-7387.
    • (2007) J Virol , vol.81 , pp. 7380-7387
    • Crump, C.M.1    Yates, C.2    Minson, T.3
  • 75
    • 21644443202 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 capsids transit by the trans-Golgi network, where viral glycoproteins accumulate independently of capsid egress
    • Turcotte S., Letellier J., Lippe R. Herpes simplex virus type 1 capsids transit by the trans-Golgi network, where viral glycoproteins accumulate independently of capsid egress. J Virol 2005, 79:8847-8860.
    • (2005) J Virol , vol.79 , pp. 8847-8860
    • Turcotte, S.1    Letellier, J.2    Lippe, R.3
  • 76
    • 67649891816 scopus 로고    scopus 로고
    • Protein kinase D-dependent trafficking of the large Herpes simplex virus type 1 capsids from the TGN to plasma membrane
    • Remillard-Labrosse G., Mihai C., Duron J., et al. Protein kinase D-dependent trafficking of the large Herpes simplex virus type 1 capsids from the TGN to plasma membrane. Traffic 2009, 10:1074-1083.
    • (2009) Traffic , vol.10 , pp. 1074-1083
    • Remillard-Labrosse, G.1    Mihai, C.2    Duron, J.3
  • 77
    • 84867232564 scopus 로고    scopus 로고
    • Herpesviruses exploit several host compartments for envelopment
    • Henaff D., Radtke K., Lippe R. Herpesviruses exploit several host compartments for envelopment. Traffic 2012, 13:1443-1449.
    • (2012) Traffic , vol.13 , pp. 1443-1449
    • Henaff, D.1    Radtke, K.2    Lippe, R.3
  • 78
    • 26444466028 scopus 로고    scopus 로고
    • Identification and functional evaluation of cellular and viral factors involved in the alteration of nuclear architecture during herpes simplex virus 1 infection
    • Simpson-Holley M., Colgrove R.C., Nalepa G., et al. Identification and functional evaluation of cellular and viral factors involved in the alteration of nuclear architecture during herpes simplex virus 1 infection. J Virol 2005, 79:12840-12851.
    • (2005) J Virol , vol.79 , pp. 12840-12851
    • Simpson-Holley, M.1    Colgrove, R.C.2    Nalepa, G.3
  • 79
    • 34247642597 scopus 로고    scopus 로고
    • Herpes simplex virus infection induces phosphorylation and delocalization of emerin, a key inner nuclear membrane protein
    • Morris J.B., Hofemeister H., O'Hare P. Herpes simplex virus infection induces phosphorylation and delocalization of emerin, a key inner nuclear membrane protein. J Virol 2007, 81:4429-4437.
    • (2007) J Virol , vol.81 , pp. 4429-4437
    • Morris, J.B.1    Hofemeister, H.2    O'Hare, P.3
  • 80
    • 34648822335 scopus 로고    scopus 로고
    • Emerin is hyperphosphorylated and redistributed in herpes simplex virus type 1-infected cells in a manner dependent on both UL34 and US3
    • Leach N., Bjerke S.L., Christensen D.K., et al. Emerin is hyperphosphorylated and redistributed in herpes simplex virus type 1-infected cells in a manner dependent on both UL34 and US3. J Virol 2007, 81:10792-10803.
    • (2007) J Virol , vol.81 , pp. 10792-10803
    • Leach, N.1    Bjerke, S.L.2    Christensen, D.K.3
  • 81
    • 0036333663 scopus 로고    scopus 로고
    • Ultrastructural localization of the herpes simplex virus type 1 UL31, UL34, and US3 proteins suggests specific roles in primary envelopment and egress of nucleocapsids,
    • Reynolds A.E., Wills E.G., Roller R.J., et al. Ultrastructural localization of the herpes simplex virus type 1 UL31, UL34, and US3 proteins suggests specific roles in primary envelopment and egress of nucleocapsids,. J Virol 2002, 76:8939-8952.
    • (2002) J Virol , vol.76 , pp. 8939-8952
    • Reynolds, A.E.1    Wills, E.G.2    Roller, R.J.3
  • 82
    • 0033986875 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 U(L)34 gene product is required for viral envelopment
    • Roller R.J., Zhou Y., Schnetzer R., et al. Herpes simplex virus type 1 U(L)34 gene product is required for viral envelopment. J Virol 2000, 74:117-129.
    • (2000) J Virol , vol.74 , pp. 117-129
    • Roller, R.J.1    Zhou, Y.2    Schnetzer, R.3
  • 83
    • 0034892972 scopus 로고    scopus 로고
    • U(L)31 and U(L)34 proteins of herpes simplex virus type 1 form a complex that accumulates at the nuclear rim and is required for envelopment of nucleocapsids
    • Reynolds A.E., Ryckman B.J., Baines J.D., et al. U(L)31 and U(L)34 proteins of herpes simplex virus type 1 form a complex that accumulates at the nuclear rim and is required for envelopment of nucleocapsids. J Virol 2001, 75:8803-8817.
    • (2001) J Virol , vol.75 , pp. 8803-8817
    • Reynolds, A.E.1    Ryckman, B.J.2    Baines, J.D.3
  • 84
    • 0033775156 scopus 로고    scopus 로고
    • Primary envelopment of pseudorabies virus at the nuclear membrane requires the UL34 gene product
    • Klupp B.G., Granzow H., Mettenleiter T.C. Primary envelopment of pseudorabies virus at the nuclear membrane requires the UL34 gene product. J Virol 2000, 74:10063-10073.
    • (2000) J Virol , vol.74 , pp. 10063-10073
    • Klupp, B.G.1    Granzow, H.2    Mettenleiter, T.C.3
  • 85
    • 0036133234 scopus 로고    scopus 로고
    • The interacting UL31 and UL34 gene products of pseudorabies virus are involved in egress from the host-cell nucleus and represent components of primary enveloped but not mature virions
    • Fuchs W., Klupp B.G., Granzow H., et al. The interacting UL31 and UL34 gene products of pseudorabies virus are involved in egress from the host-cell nucleus and represent components of primary enveloped but not mature virions. J Virol 2002, 76:364-378.
    • (2002) J Virol , vol.76 , pp. 364-378
    • Fuchs, W.1    Klupp, B.G.2    Granzow, H.3
  • 86
    • 35048861785 scopus 로고    scopus 로고
    • Cytomegaloviral proteins pUL50 and pUL53 are associated with the nuclear lamina and interact with cellular protein kinase C
    • Milbradt J., Auerochs S., Marschall M. Cytomegaloviral proteins pUL50 and pUL53 are associated with the nuclear lamina and interact with cellular protein kinase C. J Gen Virol 2007, 88:2642-2650.
    • (2007) J Gen Virol , vol.88 , pp. 2642-2650
    • Milbradt, J.1    Auerochs, S.2    Marschall, M.3
  • 87
    • 63449129336 scopus 로고    scopus 로고
    • Cytomegaloviral proteins that associate with the nuclear lamina: components of a postulated nuclear egress complex
    • Milbradt J., Auerochs S., Sticht H., Marschall M. Cytomegaloviral proteins that associate with the nuclear lamina: components of a postulated nuclear egress complex. J Gen Virol 2009, 90:579-590.
    • (2009) J Gen Virol , vol.90 , pp. 579-590
    • Milbradt, J.1    Auerochs, S.2    Sticht, H.3    Marschall, M.4
  • 88
    • 20044384534 scopus 로고    scopus 로고
    • BFRF1 of Epstein-Barr virus is essential for efficient primary viral envelopment and egress
    • Farina A., Feederle R., Raffa S., et al. BFRF1 of Epstein-Barr virus is essential for efficient primary viral envelopment and egress. J Virol 2005, 79:3703-3712.
    • (2005) J Virol , vol.79 , pp. 3703-3712
    • Farina, A.1    Feederle, R.2    Raffa, S.3
  • 89
    • 41949117422 scopus 로고    scopus 로고
    • Deletion of Epstein-Barr virus BFLF2 leads to impaired viral DNA packaging and primary egress as well as to the production of defective viral particles
    • Granato M., Feederle R., Farina A., et al. Deletion of Epstein-Barr virus BFLF2 leads to impaired viral DNA packaging and primary egress as well as to the production of defective viral particles. J Virol 2008, 82:4042-4051.
    • (2008) J Virol , vol.82 , pp. 4042-4051
    • Granato, M.1    Feederle, R.2    Farina, A.3
  • 90
    • 33947399237 scopus 로고    scopus 로고
    • Cytomegalovirus primary envelopment occurs at large infoldings of the inner nuclear membrane
    • Buser C., Walther P., Mertens T., Michel D. Cytomegalovirus primary envelopment occurs at large infoldings of the inner nuclear membrane. J Virol 2007, 81:3042-3048.
    • (2007) J Virol , vol.81 , pp. 3042-3048
    • Buser, C.1    Walther, P.2    Mertens, T.3    Michel, D.4
  • 91
    • 42449130222 scopus 로고    scopus 로고
    • Remodelling of the nuclear lamina during human cytomegalovirus infection: role of the viral proteins pUL50 and pUL53
    • Camozzi D., Pignatelli S., Valvo C., et al. Remodelling of the nuclear lamina during human cytomegalovirus infection: role of the viral proteins pUL50 and pUL53. J Gen Virol 2008, 89:731-740.
    • (2008) J Gen Virol , vol.89 , pp. 731-740
    • Camozzi, D.1    Pignatelli, S.2    Valvo, C.3
  • 92
    • 0036389915 scopus 로고    scopus 로고
    • The equine herpesvirus 1 UL34 gene product is involved in an early step in virus egress and can be efficiently replaced by a UL34-GFP fusion protein
    • Neubauer A., Rudolph J., Brandmuller C., et al. The equine herpesvirus 1 UL34 gene product is involved in an early step in virus egress and can be efficiently replaced by a UL34-GFP fusion protein. Virology 2002, 300:189-204.
    • (2002) Virology , vol.300 , pp. 189-204
    • Neubauer, A.1    Rudolph, J.2    Brandmuller, C.3
  • 93
    • 0033986875 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 U (L)34 gene product is required for viral envelopment
    • Roller R.J., Zhou Y., Schnetzer R., et al. Herpes simplex virus type 1 U (L)34 gene product is required for viral envelopment. J Virol 2000, 74:117-129.
    • (2000) J Virol , vol.74 , pp. 117-129
    • Roller, R.J.1    Zhou, Y.2    Schnetzer, R.3
  • 94
    • 0033789521 scopus 로고    scopus 로고
    • The UL34 gene product of herpes simplex virus type 2 is a tail-anchored type II membrane protein that is significant for virus envelopment
    • Shiba C., Daikoku T., Goshima F., et al. The UL34 gene product of herpes simplex virus type 2 is a tail-anchored type II membrane protein that is significant for virus envelopment. J Gen Virol 2000, 81:2397-2405.
    • (2000) J Gen Virol , vol.81 , pp. 2397-2405
    • Shiba, C.1    Daikoku, T.2    Goshima, F.3
  • 95
    • 25844443739 scopus 로고    scopus 로고
    • Cellular p32 recruits cytomegalovirus kinase pUL97 to redistribute the nuclear lamina
    • Epub 32005 Jun 33323
    • Marschall M., Marzi A., aus dem Siepen P., et al. Cellular p32 recruits cytomegalovirus kinase pUL97 to redistribute the nuclear lamina. J Biol Chem 2005, 280:33357-33367. Epub 32005 Jun 33323.
    • (2005) J Biol Chem , vol.280 , pp. 33357-33367
    • Marschall, M.1    Marzi, A.2    Aus Dem Siepen, P.3
  • 96
    • 34249844954 scopus 로고    scopus 로고
    • Vesicle formation from the nuclear membrane is induced by coexpression of two conserved herpesvirus proteins
    • Klupp B.G., Granzow H., Fuchs W., et al. Vesicle formation from the nuclear membrane is induced by coexpression of two conserved herpesvirus proteins. Proc Natl Acad Sci USA 2007, 104:7241-7246.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 7241-7246
    • Klupp, B.G.1    Granzow, H.2    Fuchs, W.3
  • 97
    • 79961175272 scopus 로고    scopus 로고
    • Nuclear envelope breakdown can substitute for primary envelopment-mediated nuclear egress of herpesviruses
    • Klupp B.G., Granzow H., Mettenleiter T.C. Nuclear envelope breakdown can substitute for primary envelopment-mediated nuclear egress of herpesviruses. J Virol 2011, 85:8285-8292.
    • (2011) J Virol , vol.85 , pp. 8285-8292
    • Klupp, B.G.1    Granzow, H.2    Mettenleiter, T.C.3
  • 98
    • 84863993436 scopus 로고    scopus 로고
    • Analysis of viral and cellular factors influencing herpesvirus-induced nuclear envelope breakdown
    • Grimm K.S., Klupp B.G., Granzow H., et al. Analysis of viral and cellular factors influencing herpesvirus-induced nuclear envelope breakdown. J Virol 2012, 86:6512-6521.
    • (2012) J Virol , vol.86 , pp. 6512-6521
    • Grimm, K.S.1    Klupp, B.G.2    Granzow, H.3
  • 99
    • 84899851889 scopus 로고    scopus 로고
    • Pseudorabies virus pUL46 induces activation of ERK1/2 and regulates herpesvirus-induced nuclear envelope breakdown
    • Schulz K.S., Liu X., Klupp B.G., et al. Pseudorabies virus pUL46 induces activation of ERK1/2 and regulates herpesvirus-induced nuclear envelope breakdown. J Virol 2014, 88:6003-6011.
    • (2014) J Virol , vol.88 , pp. 6003-6011
    • Schulz, K.S.1    Liu, X.2    Klupp, B.G.3
  • 101
    • 34547232297 scopus 로고    scopus 로고
    • Herpes simplex virus glycoproteins gB and gH function in fusion between the virion envelope and the outer nuclear membrane
    • Farnsworth A., Wisner T.W., Webb M., et al. Herpes simplex virus glycoproteins gB and gH function in fusion between the virion envelope and the outer nuclear membrane. Proc Natl Acad Sci USA 2007, 104:10187-10192.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 10187-10192
    • Farnsworth, A.1    Wisner, T.W.2    Webb, M.3
  • 102
    • 63149111461 scopus 로고    scopus 로고
    • Herpesvirus gB-induced fusion between the virion envelope and outer nuclear membrane during virus egress is regulated by the viral US3 kinase
    • Wisner T.W., Wright C.C., Kato A., et al. Herpesvirus gB-induced fusion between the virion envelope and outer nuclear membrane during virus egress is regulated by the viral US3 kinase. J Virol 2009, 83:3115-3126.
    • (2009) J Virol , vol.83 , pp. 3115-3126
    • Wisner, T.W.1    Wright, C.C.2    Kato, A.3
  • 103
    • 70350322295 scopus 로고    scopus 로고
    • Fusion between perinuclear virions and the outer nuclear membrane requires the fusogenic activity of herpes simplex virus gB
    • Wright C.C., Wisner T.W., Hannah B.P., et al. Fusion between perinuclear virions and the outer nuclear membrane requires the fusogenic activity of herpes simplex virus gB. J Virol 2009, 83:11847-11856.
    • (2009) J Virol , vol.83 , pp. 11847-11856
    • Wright, C.C.1    Wisner, T.W.2    Hannah, B.P.3
  • 104
    • 45749112586 scopus 로고    scopus 로고
    • Glycoproteins required for entry are not necessary for egress of pseudorabies virus
    • Klupp B., Altenschmidt J., Granzow H., et al. Glycoproteins required for entry are not necessary for egress of pseudorabies virus. J Virol 2008, 82:6299-6309.
    • (2008) J Virol , vol.82 , pp. 6299-6309
    • Klupp, B.1    Altenschmidt, J.2    Granzow, H.3
  • 105
    • 0036776468 scopus 로고    scopus 로고
    • In rat dorsal root ganglion neurons, herpes simplex virus type 1 tegument forms in the cytoplasm of the cell body
    • Miranda-Saksena M., Boadle R.A., Armati P., Cunningham A.L. In rat dorsal root ganglion neurons, herpes simplex virus type 1 tegument forms in the cytoplasm of the cell body. J Virol 2002, 76:9934-9951.
    • (2002) J Virol , vol.76 , pp. 9934-9951
    • Miranda-Saksena, M.1    Boadle, R.A.2    Armati, P.3    Cunningham, A.L.4
  • 106
    • 84860852545 scopus 로고    scopus 로고
    • Nuclear envelope budding enables large ribonucleoprotein particle export during synaptic Wnt signaling
    • Speese S.D., Ashley J., Jokhi V., et al. Nuclear envelope budding enables large ribonucleoprotein particle export during synaptic Wnt signaling. Cell 2012, 149:832-846.
    • (2012) Cell , vol.149 , pp. 832-846
    • Speese, S.D.1    Ashley, J.2    Jokhi, V.3
  • 107
    • 79955440194 scopus 로고    scopus 로고
    • Nuclear envelope disruption involving host caspases plays a role in the parvovirus replication cycle
    • Cohen S., Marr A.K., Garcin P., Pante N. Nuclear envelope disruption involving host caspases plays a role in the parvovirus replication cycle. J Virol 2011, 85:4863-4874.
    • (2011) J Virol , vol.85 , pp. 4863-4874
    • Cohen, S.1    Marr, A.K.2    Garcin, P.3    Pante, N.4
  • 108
    • 84889581765 scopus 로고    scopus 로고
    • Structural biology of the Bcl-2 family and its mimicry by viral proteins
    • Kvansakul M., Hinds M.G. Structural biology of the Bcl-2 family and its mimicry by viral proteins. Cell Death Dis 2013, 4:e909.
    • (2013) Cell Death Dis , vol.4 , pp. e909
    • Kvansakul, M.1    Hinds, M.G.2
  • 109
    • 84899132580 scopus 로고    scopus 로고
    • Staying alive: cell death in antiviral immunity
    • Upton J.W., Chan F.K. Staying alive: cell death in antiviral immunity. Mol Cell 2014, 54:273-280.
    • (2014) Mol Cell , vol.54 , pp. 273-280
    • Upton, J.W.1    Chan, F.K.2
  • 110
    • 80051922904 scopus 로고    scopus 로고
    • Regulation of nucleocytoplasmic trafficking of viral proteins: an integral role in pathogenesis?
    • Fulcher A.J., Jans D.A. Regulation of nucleocytoplasmic trafficking of viral proteins: an integral role in pathogenesis?. Biochim Biophys Acta 2011, 1813:2176-2190.
    • (2011) Biochim Biophys Acta , vol.1813 , pp. 2176-2190
    • Fulcher, A.J.1    Jans, D.A.2
  • 111
    • 81255157188 scopus 로고    scopus 로고
    • Examining the requirements for nucleoporins by HIV-1
    • Monette A., Pante N., Mouland A.J. Examining the requirements for nucleoporins by HIV-1. Future Microbiol 2011, 6:1247-1250.
    • (2011) Future Microbiol , vol.6 , pp. 1247-1250
    • Monette, A.1    Pante, N.2    Mouland, A.J.3
  • 112
    • 81855220949 scopus 로고    scopus 로고
    • Nesprin-3: a versatile connector between the nucleus and the cytoskeleton
    • Ketema M., Sonnenberg A. Nesprin-3: a versatile connector between the nucleus and the cytoskeleton. Biochem Soc Trans 2011, 39:1719-1724.
    • (2011) Biochem Soc Trans , vol.39 , pp. 1719-1724
    • Ketema, M.1    Sonnenberg, A.2
  • 113
    • 33749003191 scopus 로고    scopus 로고
    • SUN-domain proteins: 'Velcro' that links the nucleoskeleton to the cytoskeleton
    • Tzur Y.B., Wilson K.L., Gruenbaum Y. SUN-domain proteins: 'Velcro' that links the nucleoskeleton to the cytoskeleton. Nat Rev: Mol Cell Biol 2006, 7:782-788.
    • (2006) Nat Rev: Mol Cell Biol , vol.7 , pp. 782-788
    • Tzur, Y.B.1    Wilson, K.L.2    Gruenbaum, Y.3
  • 114
    • 77953797194 scopus 로고    scopus 로고
    • Role of the endoplasmic reticulum chaperone BiP, SUN domain proteins, and dynein in altering nuclear morphology during human cytomegalovirus infection
    • Buchkovich N.J., Maguire T.G., Alwine J.C. Role of the endoplasmic reticulum chaperone BiP, SUN domain proteins, and dynein in altering nuclear morphology during human cytomegalovirus infection. J Virol 2010, 84:7005-7017.
    • (2010) J Virol , vol.84 , pp. 7005-7017
    • Buchkovich, N.J.1    Maguire, T.G.2    Alwine, J.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.