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Volumn 428, Issue 10, 2016, Pages 1949-1961

Breaching the Barrier - The Nuclear Envelope in Virus Infection

Author keywords

nuclear envelope; nuclear envelope breakdown; nuclear virus entry and egress; nucleocytoplasmic transport; virus infection

Indexed keywords

ADENOVIRIDAE; BACULOVIRIDAE; CELL NUCLEUS MEMBRANE; HEPADNAVIRIDAE; HERPESVIRIDAE; HUMAN; LENTIVIRINAE; NONHUMAN; NUCLEOCYTOPLASMIC TRANSPORT; ORTHOMYXOVIRIDAE; PAPILLOMAVIRIDAE; PARVOVIRIDAE; POLYOMAVIRUS; PRIORITY JOURNAL; REVIEW; SIGNAL TRANSDUCTION; VIRUS CELL INTERACTION; VIRUS INFECTION; ANIMAL; CELL NUCLEUS; CYTOPLASM; METABOLISM; NUCLEAR PORE; PATHOLOGY; PHYSIOLOGY; RNA VIRUS; VIRION; VIROLOGY; VIRUS REPLICATION;

EID: 84960873341     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2015.10.001     Document Type: Review
Times cited : (56)

References (106)
  • 1
    • 84937511221 scopus 로고    scopus 로고
    • Origins and evolution of viruses of eukaryotes: The ultimate modularity
    • E.V. Koonin, V.V. Dolja, and M. Krupovic Origins and evolution of viruses of eukaryotes: The ultimate modularity Virology 479-480 2015 2 25
    • (2015) Virology , vol.479-480 , pp. 2-25
    • Koonin, E.V.1    Dolja, V.V.2    Krupovic, M.3
  • 5
    • 84865983670 scopus 로고    scopus 로고
    • Effect of viral infection on the nuclear envelope and nuclear pore complex
    • S. Cohen, I. Etingov, and N. Pante Effect of viral infection on the nuclear envelope and nuclear pore complex Int. Rev. Cell Mol. Biol. 299 2012 117 159
    • (2012) Int. Rev. Cell Mol. Biol. , vol.299 , pp. 117-159
    • Cohen, S.1    Etingov, I.2    Pante, N.3
  • 6
    • 84931264874 scopus 로고    scopus 로고
    • Nuclear entry of DNA viruses
    • N. Fay, and N. Panté Nuclear entry of DNA viruses Front. Microbiol. 6 2015 467
    • (2015) Front. Microbiol. , vol.6 , pp. 467
    • Fay, N.1    Panté, N.2
  • 7
    • 84926294975 scopus 로고    scopus 로고
    • Old foes, new understandings: Nuclear entry of small non-enveloped DNA viruses
    • N. Fay, and N. Panté Old foes, new understandings: Nuclear entry of small non-enveloped DNA viruses Curr. Opin. Virol. 12 2015 59 65
    • (2015) Curr. Opin. Virol. , vol.12 , pp. 59-65
    • Fay, N.1    Panté, N.2
  • 9
    • 84932631293 scopus 로고    scopus 로고
    • Viruses and the nuclear envelope
    • T. Hening, and P. O'Hare Viruses and the nuclear envelope Curr. Opin. Cell Biol. 34 2015 113 121
    • (2015) Curr. Opin. Cell Biol. , vol.34 , pp. 113-121
    • Hening, T.1    O'Hare, P.2
  • 10
    • 84877898099 scopus 로고    scopus 로고
    • Virus entry at a glance
    • Y. Yamauchi, and A. Helenius Virus entry at a glance J. Cell Sci. 126 2013 1289 1295
    • (2013) J. Cell Sci. , vol.126 , pp. 1289-1295
    • Yamauchi, Y.1    Helenius, A.2
  • 11
    • 84935011432 scopus 로고    scopus 로고
    • Nuclear membrane diversity: Underlying tissue-specific pathologies in disease
    • H.J. Worman, and E.C. Schirmer Nuclear membrane diversity: Underlying tissue-specific pathologies in disease Curr. Opin. Cell Biol. 34 2015 101 112
    • (2015) Curr. Opin. Cell Biol. , vol.34 , pp. 101-112
    • Worman, H.J.1    Schirmer, E.C.2
  • 12
    • 0035189722 scopus 로고    scopus 로고
    • Inner nuclear membrane proteins and the nuclear lamina
    • R. Foisner Inner nuclear membrane proteins and the nuclear lamina J. Cell Sci. 114 2001 3791 3792
    • (2001) J. Cell Sci. , vol.114 , pp. 3791-3792
    • Foisner, R.1
  • 13
    • 84931266956 scopus 로고    scopus 로고
    • Nuclear envelope: Positioning nuclei and organizing synapses
    • D. Razafsky, and D. Hodzic Nuclear envelope: Positioning nuclei and organizing synapses Curr. Opin. Cell Biol. 34 2015 84 93
    • (2015) Curr. Opin. Cell Biol. , vol.34 , pp. 84-93
    • Razafsky, D.1    Hodzic, D.2
  • 14
    • 84942292361 scopus 로고    scopus 로고
    • LINC'ing form and function at the nuclear envelope
    • P. Meinke, and E. Schirmer LINC'ing form and function at the nuclear envelope FEBS Lett. 2015 10.1016/j.febslet.2015.06.011
    • (2015) FEBS Lett.
    • Meinke, P.1    Schirmer, E.2
  • 15
  • 16
    • 0036175701 scopus 로고    scopus 로고
    • Nuclear pore complex is able to transport macromolecules with diameters of about 39 nm
    • N. Panté, and M. Kann 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
    • Panté, N.1    Kann, M.2
  • 17
    • 84974717612 scopus 로고    scopus 로고
    • Herpesviridae
    • D. Knipe, P.M. Howley, sixth ed
    • P.E. Pellett, and B. Roizman Herpesviridae D. Knipe, P.M. Howley, Fields Virology sixth ed. 2013 1802 1822
    • (2013) Fields Virology , pp. 1802-1822
    • Pellett, P.E.1    Roizman, B.2
  • 19
    • 79956141898 scopus 로고    scopus 로고
    • Subversion of the actin cytoskeleton during viral infection
    • M.P. Taylor, O. Koyuncu, and L.W. Enquist Subversion of the actin cytoskeleton during viral infection Nat. Rev. Microbiol. 9 2011 427 439
    • (2011) Nat. Rev. Microbiol. , vol.9 , pp. 427-439
    • Taylor, M.P.1    Koyuncu, O.2    Enquist, L.W.3
  • 21
    • 79551691992 scopus 로고    scopus 로고
    • A single mutation responsible for temperature-sensitive entry and assembly defects in the VP1-2 protein of herpes simplex virus
    • F. Abaitua, T. Daikoku, C.M. Crump, M. Bolstad, and P. O'Hare A single mutation responsible for temperature-sensitive entry and assembly defects in the VP1-2 protein of herpes simplex virus J. Virol. 85 2011 2024 2036
    • (2011) J. Virol. , vol.85 , pp. 2024-2036
    • Abaitua, F.1    Daikoku, T.2    Crump, C.M.3    Bolstad, M.4    O'Hare, P.5
  • 22
    • 59649092592 scopus 로고    scopus 로고
    • Herpes simplex virus replication: Roles of viral proteins and nucleoporins in capsid-nucleus attachment
    • A.M. Copeland, W.W. Newcomb, and J.C. Brown Herpes simplex virus replication: Roles of viral proteins and nucleoporins in capsid-nucleus attachment J. Virol. 83 2009 1660 1668
    • (2009) J. Virol. , vol.83 , pp. 1660-1668
    • Copeland, A.M.1    Newcomb, W.W.2    Brown, J.C.3
  • 23
    • 67449089967 scopus 로고    scopus 로고
    • Herpesvirus capsid association with the nuclear pore complex and viral DNA release involve the nucleoprotein CAN/Nup214 and the capsid protein pUL25
    • D. Pasdeloup, D. Blondel, A.L. Isidro, and F.J. Rixon Herpesvirus capsid association with the nuclear pore complex and viral DNA release involve the nucleoprotein CAN/Nup214 and the capsid protein pUL25 J. Virol. 83 2009 6610 6623
    • (2009) J. Virol. , vol.83 , pp. 6610-6623
    • Pasdeloup, D.1    Blondel, D.2    Isidro, A.L.3    Rixon, F.J.4
  • 24
    • 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
    • P.M. Ojala, B. Sodeik, M.W. Ebersold, U. Kutay, and A. Helenius 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
  • 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
    • F. Abaitua, M. Hollinshead, M. Bolstad, C.M. Crump, and P. O'Hare A nuclear localization signal in herpesvirus protein VP1-2 is essential for infection via capsid routing to the nuclear pore J. Virol. 86 2012 8998 9014
    • (2012) J. Virol. , vol.86 , pp. 8998-9014
    • Abaitua, F.1    Hollinshead, M.2    Bolstad, M.3    Crump, C.M.4    O'Hare, P.5
  • 26
    • 70349286031 scopus 로고    scopus 로고
    • Intracellular localization of the pseudorabies virus large tegument protein pUL365
    • B.S. Möhl, S. Böttcher, H. Granzow, J. Kuhn, B.G. Klupp, and T.C. Mettenleiter Intracellular localization of the pseudorabies virus large tegument protein pUL365 J. Virol. 83 2009 9641 9651
    • (2009) J. Virol. , vol.83 , pp. 9641-9651
    • Möhl, B.S.1    Böttcher, S.2    Granzow, H.3    Kuhn, J.4    Klupp, B.G.5    Mettenleiter, T.C.6
  • 27
    • 41149126620 scopus 로고    scopus 로고
    • Proteolytic cleavage of VP1-2 is required for release of herpes simplex virus 1 DNA into the nucleus
    • V. Jovasevic, L. Liang, and B. Roizman Proteolytic cleavage of VP1-2 is required for release of herpes simplex virus 1 DNA into the nucleus J. Virol. 82 2008 3311 3319
    • (2008) J. Virol. , vol.82 , pp. 3311-3319
    • Jovasevic, V.1    Liang, L.2    Roizman, B.3
  • 29
    • 27744487093 scopus 로고    scopus 로고
    • Common ancestry of herpesviruses and tailed DNA bacteriophages
    • M.L. Baker, W. Jiang, F.J. Rikxon, and W. Chiu Common ancestry of herpesviruses and tailed DNA bacteriophages J. Virol. 79 2005 14967 14970
    • (2005) J. Virol. , vol.79 , pp. 14967-14970
    • Baker, M.L.1    Jiang, W.2    Rikxon, F.J.3    Chiu, W.4
  • 32
    • 77954980510 scopus 로고    scopus 로고
    • Actin-based motility drives baculovirus transit to the nucleus and cell surface
    • T. Ohkawa, L.E. Volkman, and M.D. Welch Actin-based motility drives baculovirus transit to the nucleus and cell surface J. Cell Biol. 190 2010 187 195
    • (2010) J. Cell Biol. , vol.190 , pp. 187-195
    • Ohkawa, T.1    Volkman, L.E.2    Welch, M.D.3
  • 34
    • 84880736131 scopus 로고    scopus 로고
    • Baculovirus nuclear import: Open, nuclear pore complex (NPC) sesame
    • S. Au, W. Wu, and N. Panté Baculovirus nuclear import: Open, nuclear pore complex (NPC) sesame Viruses 5 2013 1885 1900
    • (2013) Viruses , vol.5 , pp. 1885-1900
    • Au, S.1    Wu, W.2    Panté, N.3
  • 35
    • 84855858712 scopus 로고    scopus 로고
    • Nuclear transport of baculovirus: Revealing the nuclear pore complex passage
    • S. Au, and N. Panté Nuclear transport of baculovirus: Revealing the nuclear pore complex passage J. Struct. Biol. 177 2012 90 98
    • (2012) J. Struct. Biol. , vol.177 , pp. 90-98
    • Au, S.1    Panté, N.2
  • 36
    • 0033526096 scopus 로고    scopus 로고
    • Phosphorylation-dependent binding of hepatitis B virus core particles to the nuclear pore complex
    • M. Kann, B. Sodeik, A. Vlachou, W.H. Gerlich, and A. Helenius 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    Vlachou, A.3    Gerlich, W.H.4    Helenius, A.5
  • 40
    • 84921467160 scopus 로고    scopus 로고
    • Nuclear import of adenovirus DNA involves direct interaction of hexon with an N-terminal domain of the nucleoprotein Nup214
    • A. Cassany, J. Ragues, T. Guan, D. Bégu, H. Wodrich, M. Kann, G.R. Nemerow, and L. Gerace Nuclear import of adenovirus DNA involves direct interaction of hexon with an N-terminal domain of the nucleoprotein Nup214 J. Virol. 89 2015 1719 1730
    • (2015) J. Virol. , vol.89 , pp. 1719-1730
    • Cassany, A.1    Ragues, J.2    Guan, T.3    Bégu, D.4    Wodrich, H.5    Kann, M.6    Nemerow, G.R.7    Gerace, L.8
  • 42
    • 84897016759 scopus 로고    scopus 로고
    • Recombinant adeno-associated virus utilizes host cell nuclear import machinery to enter the nucleus
    • S. Nicolson, and R.J. Samulski Recombinant adeno-associated virus utilizes host cell nuclear import machinery to enter the nucleus J. Virol. 88 2014 4132 4144
    • (2014) J. Virol. , vol.88 , pp. 4132-4144
    • Nicolson, S.1    Samulski, R.J.2
  • 43
    • 79955440194 scopus 로고    scopus 로고
    • Nuclear envelope disruption involving host caspases plays a role in the parvovirus life cycle
    • S. Cohen, A.K. Marr, P. Garcin, and N. Pante Nuclear envelope disruption involving host caspases plays a role in the parvovirus life cycle J. Virol. 85 2011 4853 4859
    • (2011) J. Virol. , vol.85 , pp. 4853-4859
    • Cohen, S.1    Marr, A.K.2    Garcin, P.3    Pante, N.4
  • 45
    • 84937511588 scopus 로고    scopus 로고
    • DNA virus uncoating
    • S. Kilcher, and J. Mercer DNA virus uncoating Virology 479-480 2015 578 590
    • (2015) Virology , vol.479-480 , pp. 578-590
    • Kilcher, S.1    Mercer, J.2
  • 46
    • 79958051219 scopus 로고    scopus 로고
    • A large and intact viral particle penetrates the endoplasmic reticulum membrane to reach the cytosol
    • T. Inoue, and B. Tsai A large and intact viral particle penetrates the endoplasmic reticulum membrane to reach the cytosol PLoS Pathog. 7 2011 e1002037
    • (2011) PLoS Pathog. , vol.7 , pp. e1002037
    • Inoue, T.1    Tsai, B.2
  • 47
    • 84857067637 scopus 로고    scopus 로고
    • Disassembly of simian virus 40 during passage through the endoplasmic reticulum and in the cytoplasm
    • D. Kuksin, and L. Norkin Disassembly of simian virus 40 during passage through the endoplasmic reticulum and in the cytoplasm J. Virol. 86 2012 1555 1562
    • (2012) J. Virol. , vol.86 , pp. 1555-1562
    • Kuksin, D.1    Norkin, L.2
  • 51
    • 84890544306 scopus 로고    scopus 로고
    • Concepts of papillomavirus entry into host cells
    • P. Day, and M. Schelhaas Concepts of papillomavirus entry into host cells Curr. Opin. Virol. 4 2014 24 31
    • (2014) Curr. Opin. Virol. , vol.4 , pp. 24-31
    • Day, P.1    Schelhaas, M.2
  • 54
    • 14544270958 scopus 로고    scopus 로고
    • An unconventional NLS is critical for the nuclear import of the influenza A virus nucleoprotein and ribonucleoprotein
    • J.F. Cros, A. Garcia-Sastre, and P. Palese An unconventional NLS is critical for the nuclear import of the influenza A virus nucleoprotein and ribonucleoprotein Traffic 6 2005 205 213
    • (2005) Traffic , vol.6 , pp. 205-213
    • Cros, J.F.1    Garcia-Sastre, A.2    Palese, P.3
  • 56
    • 77956528167 scopus 로고    scopus 로고
    • Cellular networks involved in the influenza virus life cycle
    • T. Watanabe, S. Watanabe, and Y. Kawaoka Cellular networks involved in the influenza virus life cycle Cell Host Microbe 7 2010 427 439
    • (2010) Cell Host Microbe , vol.7 , pp. 427-439
    • Watanabe, T.1    Watanabe, S.2    Kawaoka, Y.3
  • 57
    • 33847139800 scopus 로고    scopus 로고
    • The road to chromatin-nuclear entry of retroviruses
    • Y. Suzuki, and R. Craigie The road to chromatin-nuclear entry of retroviruses Nat. Rev. Microbiol. 5 2007 187 196
    • (2007) Nat. Rev. Microbiol. , vol.5 , pp. 187-196
    • Suzuki, Y.1    Craigie, R.2
  • 58
    • 67349288596 scopus 로고    scopus 로고
    • Integrase interacts with nucleoprotein NUP153 to mediate the nuclear import of human immunodeficiency virus type 1
    • C.L. Woodward, S. Prakobwanakit, S. Mosessian, and S.A. Chow Integrase interacts with nucleoprotein NUP153 to mediate the nuclear import of human immunodeficiency virus type 1 J. Virol. 83 2009 6522 6533
    • (2009) J. Virol. , vol.83 , pp. 6522-6533
    • Woodward, C.L.1    Prakobwanakit, S.2    Mosessian, S.3    Chow, S.A.4
  • 59
    • 84928527060 scopus 로고    scopus 로고
    • The road less traveled: HIV's use of alternative routes through cellular pathways
    • A. Marx, and A. Alian The road less traveled: HIV's use of alternative routes through cellular pathways J. Virol. 89 2015 5204 5212
    • (2015) J. Virol. , vol.89 , pp. 5204-5212
    • Marx, A.1    Alian, A.2
  • 61
    • 84885138769 scopus 로고    scopus 로고
    • Viral and cellular requirements for the nuclear entry of retroviral preintegration nucleoprotein complexes
    • K.A. Matreyek, and A. Engelman Viral and cellular requirements for the nuclear entry of retroviral preintegration nucleoprotein complexes Viruses 5 2013 2483 2511
    • (2013) Viruses , vol.5 , pp. 2483-2511
    • Matreyek, K.A.1    Engelman, A.2
  • 62
    • 84921478466 scopus 로고    scopus 로고
    • BGLF4 kinase modulates the structure and transport preference of the nuclear pore complex to facilitate nuclear import of Epstein-Barr virus lytic proteins
    • C.-W. Chang, C.-P. Lee, M.-T. Su, C.-H. Tsai, and M.-R. Chen BGLF4 kinase modulates the structure and transport preference of the nuclear pore complex to facilitate nuclear import of Epstein-Barr virus lytic proteins J. Virol. 89 2015 1703 1718
    • (2015) J. Virol. , vol.89 , pp. 1703-1718
    • Chang, C.-W.1    Lee, C.-P.2    Su, M.-T.3    Tsai, C.-H.4    Chen, M.-R.5
  • 63
    • 79954599465 scopus 로고    scopus 로고
    • Herpesviruses remodel host membranes for virus egress
    • D.C. Johnson, and J.D. Baines Herpesviruses remodel host membranes for virus egress Nat. Rev. Microbiol. 9 2011 382 394
    • (2011) Nat. Rev. Microbiol. , vol.9 , pp. 382-394
    • Johnson, D.C.1    Baines, J.D.2
  • 64
    • 84872616937 scopus 로고    scopus 로고
    • The way out: What we know and do not know about herpesvirus nuclear egress
    • T.C. Mettenleiter, F. Müller, H. Granzow, and B.G. Klupp The way out: What we know and do not know about herpesvirus nuclear egress Cell. Microbiol. 15 2013 170 179
    • (2013) Cell. Microbiol. , vol.15 , pp. 170-179
    • Mettenleiter, T.C.1    Müller, F.2    Granzow, H.3    Klupp, B.G.4
  • 66
    • 34249844954 scopus 로고    scopus 로고
    • Vesicle formation from the nuclear membrane is induced by coexpression of two conserved herpesvirus proteins
    • B.G. Klupp, H. Granzow, W. Fuchs, G. Keil, S. Finke, and T.C. Mettenleiter Vesicle formation from the nuclear membrane is induced by coexpression of two conserved herpesvirus proteins Proc. Natl. Acad. Sci. U. S. A. 104 2007 7241 7246
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 7241-7246
    • Klupp, B.G.1    Granzow, H.2    Fuchs, W.3    Keil, G.4    Finke, S.5    Mettenleiter, T.C.6
  • 67
    • 84902322686 scopus 로고    scopus 로고
    • Membrane deformation and scission by the HSV-1 nuclear egress complex
    • J.M. Bigalke, T. Heuser, D. Nicastro, and E.E. Heldwein Membrane deformation and scission by the HSV-1 nuclear egress complex Nat. Commun. 5 2014 4131
    • (2014) Nat. Commun. , vol.5 , pp. 4131
    • Bigalke, J.M.1    Heuser, T.2    Nicastro, D.3    Heldwein, E.E.4
  • 69
    • 84940547871 scopus 로고    scopus 로고
    • The great (nuclear) escape: New insights into the role of the nuclear egress complex of herpesviruses
    • J.M. Bigalke, and E.E. Heldwein The great (nuclear) escape: New insights into the role of the nuclear egress complex of herpesviruses J. Virol. 89 2015 9150 9153
    • (2015) J. Virol. , vol.89 , pp. 9150-9153
    • Bigalke, J.M.1    Heldwein, E.E.2
  • 70
    • 84936774563 scopus 로고    scopus 로고
    • The herpes simplex virus protein pUL31 escorts nucleocapsids to sites of nuclear egress, a process coordinated by its N-terminal domain
    • C. Funk, M. Ott, V. Rauschbichler, C.-H. Nagel, A. Binz, B. Sodeik, R. Bauerfeind, and S.M. Bailer The herpes simplex virus protein pUL31 escorts nucleocapsids to sites of nuclear egress, a process coordinated by its N-terminal domain PLoS Pathog. 11 6 2015 e1004957
    • (2015) PLoS Pathog. , vol.11 , Issue.6 , pp. e1004957
    • Funk, C.1    Ott, M.2    Rauschbichler, V.3    Nagel, C.-H.4    Binz, A.5    Sodeik, B.6    Bauerfeind, R.7    Bailer, S.M.8
  • 71
    • 80655143483 scopus 로고    scopus 로고
    • A physical link between the pseudorabies virus capsid and the nuclear egress complex
    • M. Leelawong, D. Guo, and G.A. Smith A physical link between the pseudorabies virus capsid and the nuclear egress complex J. Virol. 85 2011 11675 11684
    • (2011) J. Virol. , vol.85 , pp. 11675-11684
    • Leelawong, M.1    Guo, D.2    Smith, G.A.3
  • 72
    • 77953797194 scopus 로고    scopus 로고
    • Role of endoplasmic reticulum chaperone BiP, SUN domain proteins, and dynein in altering nuclear morphology during human cytomegalovirus infection
    • N.J. Buchkovich, T.G. Maguire, and J.C. Alwine Role of endoplasmic reticulum chaperone BiP, SUN domain proteins, and dynein in altering nuclear morphology during human cytomegalovirus infection J. Virol. 84 2010 7005 7017
    • (2010) J. Virol. , vol.84 , pp. 7005-7017
    • Buchkovich, N.J.1    Maguire, T.G.2    Alwine, J.C.3
  • 73
    • 34547232297 scopus 로고    scopus 로고
    • Herpes simplex virus glycoproteins Gb and gH function in fusion between the virion envelope and the outer nuclear membrane
    • A. Farnsworth, T.W. Wisner, M. Webb, R. Roller, G. Cohen, R. Eisenberg, and D.C. Johnson Herpes simplex virus glycoproteins gB and gH function in fusion between the virion envelope and the outer nuclear membrane Proc. Natl. Acad. Sci. U. S. A. 104 2007 10187 10192
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 10187-10192
    • Farnsworth, A.1    Wisner, T.W.2    Webb, M.3    Roller, R.4    Cohen, G.5    Eisenberg, R.6    Johnson, D.C.7
  • 74
    • 45749112586 scopus 로고    scopus 로고
    • Glycoproteins required for entry are not necessary for egress of pseudorabies virus
    • B.G. Klupp, J. Altenschmidt, H. Granzow, W. Fuchs, and T.C. Mettenleiter Glycoproteins required for entry are not necessary for egress of pseudorabies virus J. Virol. 82 2008 6299 6309
    • (2008) J. Virol. , vol.82 , pp. 6299-6309
    • Klupp, B.G.1    Altenschmidt, J.2    Granzow, H.3    Fuchs, W.4    Mettenleiter, T.C.5
  • 75
    • 84938939142 scopus 로고    scopus 로고
    • Role of host cell p32 in herpes simplex virus 1 de-envelopment during viral nuclear egress
    • Z. Liu, A. Kato, M. Oyama, H. Kozuka-Hata, J. Arii, and et al. Role of host cell p32 in herpes simplex virus 1 de-envelopment during viral nuclear egress J. Virol. 89 2015 8982 8998
    • (2015) J. Virol. , vol.89 , pp. 8982-8998
    • Liu, Z.1    Kato, A.2    Oyama, M.3    Kozuka-Hata, H.4    Arii, J.5
  • 76
    • 84937685221 scopus 로고    scopus 로고
    • Herpes simplex virus 1 recruits CD98 heavy chain and beta 1 integrin to the nuclear membrane for viral de-envelopment
    • Y. Hirohata, J. Arii, Z. Liu, K. Shindo, M. Oyama, and et al. Herpes simplex virus 1 recruits CD98 heavy chain and beta 1 integrin to the nuclear membrane for viral de-envelopment J. Virol. 89 2015 7799 7812
    • (2015) J. Virol. , vol.89 , pp. 7799-7812
    • Hirohata, Y.1    Arii, J.2    Liu, Z.3    Shindo, K.4    Oyama, M.5
  • 77
    • 84860852545 scopus 로고    scopus 로고
    • Nuclear envelope budding enables large ribonucleoprotein particle export during synaptic Wnt signalling
    • S.D. Speese, J. Ashley, V. Jokhi, J. Nunnari, R. Barria, Y. Li, B. Ataman, A. Koon, Y.-T. Chang, Q. Li, and et al. Nuclear envelope budding enables large ribonucleoprotein particle export during synaptic Wnt signalling Cell 149 2012 832 846
    • (2012) Cell , vol.149 , pp. 832-846
    • Speese, S.D.1    Ashley, J.2    Jokhi, V.3    Nunnari, J.4    Barria, R.5    Li, Y.6    Ataman, B.7    Koon, A.8    Chang, Y.-T.9    Li, Q.10
  • 79
    • 84866854226 scopus 로고    scopus 로고
    • Alternative nuclear transport for cellular protein quality control
    • A. Rose, and C. Schlieker Alternative nuclear transport for cellular protein quality control Trends Cell Biol. 22 2012 509 514
    • (2012) Trends Cell Biol. , vol.22 , pp. 509-514
    • Rose, A.1    Schlieker, C.2
  • 80
    • 84861208901 scopus 로고    scopus 로고
    • An alternative route for nuclear mRNP export by membrane budding
    • B. Monpetit, and K. Weis An alternative route for nuclear mRNP export by membrane budding Science 336 2012 809 810
    • (2012) Science , vol.336 , pp. 809-810
    • Monpetit, B.1    Weis, K.2
  • 81
    • 79961175272 scopus 로고    scopus 로고
    • Nuclear envelope breakdown can substitute for primary envelopment-mediated nuclear egress of herpesviruses
    • B.G. Klupp, H. Granzow, and T.C. Mettenleiter Nuclear envelope breakdown can substitute for primary envelopment-mediated nuclear egress of herpesviruses J. Virol. 85 2011 8285 8292
    • (2011) J. Virol. , vol.85 , pp. 8285-8292
    • Klupp, B.G.1    Granzow, H.2    Mettenleiter, T.C.3
  • 82
    • 84959538569 scopus 로고    scopus 로고
    • Herpesvirus nuclear egress: Pseudorabies virus can simultaneously induce nuclear envelope breakdown and exit the nucleus via the envelopment-deenvelopment pathway
    • K.S. Schulz, B.G. Klupp, H. Granzow, L. Paßvogel, and T.C. Mettenleiter Herpesvirus nuclear egress: Pseudorabies virus can simultaneously induce nuclear envelope breakdown and exit the nucleus via the envelopment-deenvelopment pathway Virus Res. 209 2015 76 86
    • (2015) Virus Res. , vol.209 , pp. 76-86
    • Schulz, K.S.1    Klupp, B.G.2    Granzow, H.3    Paßvogel, L.4    Mettenleiter, T.C.5
  • 83
    • 84862782520 scopus 로고    scopus 로고
    • BM61 of Bombyx mori nucleopolyhedrovirus: Its involvement in the egress of nucleocapsids from the nucleus
    • H. Shen, and K. Chen BM61 of Bombyx mori nucleopolyhedrovirus: Its involvement in the egress of nucleocapsids from the nucleus FEBS Lett. 586 2012 990 995
    • (2012) FEBS Lett. , vol.586 , pp. 990-995
    • Shen, H.1    Chen, K.2
  • 84
    • 80655125521 scopus 로고    scopus 로고
    • Identification of Autographa californica nucleopolyhedrovirus ac93 as a core gene and its requirement for intranuclear microvesicle formation and nuclear egress of nucleocapsids
    • M. Yuan, Z. Huang, D. Wei, Z. Hu, K. Yang, and Y. Pang Identification of Autographa californica nucleopolyhedrovirus ac93 as a core gene and its requirement for intranuclear microvesicle formation and nuclear egress of nucleocapsids J. Virol. 85 2011 11664 11674
    • (2011) J. Virol. , vol.85 , pp. 11664-11674
    • Yuan, M.1    Huang, Z.2    Wei, D.3    Hu, Z.4    Yang, K.5    Pang, Y.6
  • 85
    • 84867882831 scopus 로고    scopus 로고
    • Host factors involved in hepatitis B virus maturation, assembly, and egress
    • R. Prange Host factors involved in hepatitis B virus maturation, assembly, and egress Med. Microbiol. Immunol. 201 4 2012 449 461
    • (2012) Med. Microbiol. Immunol. , vol.201 , Issue.4 , pp. 449-461
    • Prange, R.1
  • 86
    • 0034758864 scopus 로고    scopus 로고
    • Role of polypyrimidine tract binding protein in the function of the hepatitis B virus posttranscriptional regulatory element
    • W.-Q. Zang, B. Li, P.-Y. Huang, M.M.C. Lai, and T.S.B. Yen Role of polypyrimidine tract binding protein in the function of the hepatitis B virus posttranscriptional regulatory element J. Virol. 75 2001 10779 10786
    • (2001) J. Virol. , vol.75 , pp. 10779-10786
    • Zang, W.-Q.1    Li, B.2    Huang, P.-Y.3    Lai, M.M.C.4    Yen, T.S.B.5
  • 87
    • 0027167564 scopus 로고
    • The adenovirus L3 23-kilodalton proteinase cleaves the amino-terminal head domain from cytokeratin 18 and disrupts the cytokeratin network of HeLa cells
    • P.H. Chen, D.A. Ornelles, and T. Shenk The adenovirus L3 23-kilodalton proteinase cleaves the amino-terminal head domain from cytokeratin 18 and disrupts the cytokeratin network of HeLa cells J. Virol. 67 1993 3507 3514
    • (1993) J. Virol. , vol.67 , pp. 3507-3514
    • Chen, P.H.1    Ornelles, D.A.2    Shenk, T.3
  • 88
    • 0029872241 scopus 로고    scopus 로고
    • The adenovirus death protein (E3-11.6K) is required at very late stages of infection for efficient cell lysis and release of adenovirus from infected cells
    • A.E. Tollefson, A. Scaria, T.W. Hermiston, J.S. Ryerse, L.J. Wold, and W.S.M. Wold The adenovirus death protein (E3-11.6K) is required at very late stages of infection for efficient cell lysis and release of adenovirus from infected cells J. Virol. 70 1996 2296 2306
    • (1996) J. Virol. , vol.70 , pp. 2296-2306
    • Tollefson, A.E.1    Scaria, A.2    Hermiston, T.W.3    Ryerse, J.S.4    Wold, L.J.5    Wold, W.S.M.6
  • 89
    • 0030003101 scopus 로고    scopus 로고
    • The E3-11.6-kDa adenovirus death protein (ADP) is required for efficient cell death: Characterization of cells infected with adp mutants
    • A.E. Tollefson, J.S. Ryerse, A. Scaria, T.W. Hermiston, and W.S. Wold The E3-11.6-kDa adenovirus death protein (ADP) is required for efficient cell death: Characterization of cells infected with adp mutants Virology 220 1996 152 162
    • (1996) Virology , vol.220 , pp. 152-162
    • Tollefson, A.E.1    Ryerse, J.S.2    Scaria, A.3    Hermiston, T.W.4    Wold, W.S.5
  • 90
    • 0031792462 scopus 로고    scopus 로고
    • Virus assembly and disassembly: The adenovirus cysteine protease as a trigger factor
    • U.F. Greber Virus assembly and disassembly: The adenovirus cysteine protease as a trigger factor Rev. Med. Virol. 8 1998 213 222
    • (1998) Rev. Med. Virol. , vol.8 , pp. 213-222
    • Greber, U.F.1
  • 91
    • 84912544572 scopus 로고    scopus 로고
    • Structure, function and dynamics in adenovirus maturation
    • W.F. Mangel, and C. San Martin Structure, function and dynamics in adenovirus maturation Viruses 6 2014 4536 4570
    • (2014) Viruses , vol.6 , pp. 4536-4570
    • Mangel, W.F.1    San Martin, C.2
  • 92
    • 77953783397 scopus 로고    scopus 로고
    • Adenovirus release from the infected cell as a key factor for adenovirus oncolysis
    • A. Gros, and S. Guedan Adenovirus release from the infected cell as a key factor for adenovirus oncolysis Open Gene Ther. J. 3 2010 24 30
    • (2010) Open Gene Ther. J. , vol.3 , pp. 24-30
    • Gros, A.1    Guedan, S.2
  • 93
    • 84884687913 scopus 로고    scopus 로고
    • Vesicular transport of progeny parvovirus particles through ER and Golgi regulates maturation and cytolysis
    • S. Bär, J. Rommelaere, and J.P.F. Nüesch Vesicular transport of progeny parvovirus particles through ER and Golgi regulates maturation and cytolysis PLoS Pathog. 9 2013 e1003605
    • (2013) PLoS Pathog. , vol.9 , pp. e1003605
    • Bär, S.1    Rommelaere, J.2    Nüesch, J.P.F.3
  • 94
    • 48749107741 scopus 로고    scopus 로고
    • A supraphysiological nuclear export signal is required for parvovirus nuclear export
    • D. Engelsma, N. Valle, A. Fish, N. Salomé, J.M. Almendral, and M. Fornerod A supraphysiological nuclear export signal is required for parvovirus nuclear export Mol. Biol. Cell 19 2008 2544 2552
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2544-2552
    • Engelsma, D.1    Valle, N.2    Fish, A.3    Salomé, N.4    Almendral, J.M.5    Fornerod, M.6
  • 95
    • 0032874346 scopus 로고    scopus 로고
    • Nuclear export factor CRM1 interacts with nonstructural proteins NS2 from parvovirus minute virus of mice
    • U. Bodendorf, C. Cziepluch, J.-C. Jauniaux, J. Rommelaere, and N. Salomé Nuclear export factor CRM1 interacts with nonstructural proteins NS2 from parvovirus minute virus of mice J. Virol. 73 1999 7769 7779
    • (1999) J. Virol. , vol.73 , pp. 7769-7779
    • Bodendorf, U.1    Cziepluch, C.2    Jauniaux, J.-C.3    Rommelaere, J.4    Salomé, N.5
  • 96
    • 84945941160 scopus 로고    scopus 로고
    • Reorganization of nuclear pore complexes and lamina in late-stage parvovirus infection
    • E. Mäntylä, E. Niskanen, T. Ihalainen, and M. Vihinen-Ranta Reorganization of nuclear pore complexes and lamina in late-stage parvovirus infection J. Virol. 2015 10.1128/JVI.01608-15
    • (2015) J. Virol.
    • Mäntylä, E.1    Niskanen, E.2    Ihalainen, T.3    Vihinen-Ranta, M.4
  • 98
    • 84878646453 scopus 로고    scopus 로고
    • SV40 late protein VP4 forms toroidal pores to disrupt membranes for viral release
    • S. Raghava, K.M. Giorda, F.B. Romano, A.P. Heuck, and D.N. Hebert SV40 late protein VP4 forms toroidal pores to disrupt membranes for viral release Biochemistry 52 2013 3939 3948
    • (2013) Biochemistry , vol.52 , pp. 3939-3948
    • Raghava, S.1    Giorda, K.M.2    Romano, F.B.3    Heuck, A.P.4    Hebert, D.N.5
  • 99
    • 77956004466 scopus 로고    scopus 로고
    • E1-E4-mediated keratin phosphorylation and ubiquitylation: A mechanism for keratin depletion in HPV16-infected epithelium
    • P.B. McIntosh, P. Laskey, C. Davy, Q. Wang, D.J. Jackson, H.M. Griffin, and J. Doorbar E1-E4-mediated keratin phosphorylation and ubiquitylation: A mechanism for keratin depletion in HPV16-infected epithelium J. Cell Sci. 123 2010 2810 2822
    • (2010) J. Cell Sci. , vol.123 , pp. 2810-2822
    • McIntosh, P.B.1    Laskey, P.2    Davy, C.3    Wang, Q.4    Jackson, D.J.5    Griffin, H.M.6    Doorbar, J.7
  • 101
    • 84885141603 scopus 로고    scopus 로고
    • Transport of the influenza virus genome from nucleus to nucleus
    • E.C. Hutchinson, and E. Fodor Transport of the influenza virus genome from nucleus to nucleus Viruses 5 2013 2424 2446
    • (2013) Viruses , vol.5 , pp. 2424-2446
    • Hutchinson, E.C.1    Fodor, E.2
  • 102
    • 84904497401 scopus 로고    scopus 로고
    • The nuclear export protein of H5N1 influenza A viruses recruits Matrix 1 (M1) protein to the viral ribonucleoprotein to mediate nuclear export
    • L. Brunotte, J. Flies, H. Bolte, P. Reuther, F. Vreede, and M. Schwemmle The nuclear export protein of H5N1 influenza A viruses recruits Matrix 1 (M1) protein to the viral ribonucleoprotein to mediate nuclear export J. Biol. Chem. 289 2014 20067 20077
    • (2014) J. Biol. Chem. , vol.289 , pp. 20067-20077
    • Brunotte, L.1    Flies, J.2    Bolte, H.3    Reuther, P.4    Vreede, F.5    Schwemmle, M.6
  • 105
    • 84875774017 scopus 로고    scopus 로고
    • Role of nucleocytoplasmic RNA transport during the life cycle of retroviruses
    • H. Shida Role of nucleocytoplasmic RNA transport during the life cycle of retroviruses Front. Microbiol. 3 2012 179
    • (2012) Front. Microbiol. , vol.3 , pp. 179
    • Shida, H.1
  • 106
    • 84946906322 scopus 로고    scopus 로고
    • Misdelivery at the nuclear pore complex - Stopping a virus dead in its tracks
    • J.W. Flatt, and J.F. Greber Misdelivery at the nuclear pore complex - Stopping a virus dead in its tracks Cells 4 2015 277 296
    • (2015) Cells , vol.4 , pp. 277-296
    • Flatt, J.W.1    Greber, J.F.2


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