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Volumn 94, Issue , 2016, Pages 81-140

Nuclear Egress of Herpesviruses: The Prototypic Vesicular Nucleocytoplasmic Transport

Author keywords

Herpesvirus; NEC; Nuclear egress; Nuclear egress complex; Nuclear envelope; Nucleocytoplasmic transport

Indexed keywords

CAPSID PROTEIN; CYCLIN DEPENDENT KINASE; LAMIN; NUCLEOPORIN; VIRUS DNA;

EID: 84962054204     PISSN: 00653527     EISSN: 15578399     Source Type: Book Series    
DOI: 10.1016/bs.aivir.2015.10.002     Document Type: Chapter
Times cited : (48)

References (335)
  • 1
    • 84864582150 scopus 로고    scopus 로고
    • Dynamic assembly of brambleberry mediates nuclear envelope fusion during early development
    • Abrams E.W., Zhang H., Marlow F.L., Kapp L., Lu S., Mullins M.C. Dynamic assembly of brambleberry mediates nuclear envelope fusion during early development. Cell 2012, 150(3):521-532. 10.1016/j.cell.2012.05.048.
    • (2012) Cell , vol.150 , Issue.3 , pp. 521-532
    • Abrams, E.W.1    Zhang, H.2    Marlow, F.L.3    Kapp, L.4    Lu, S.5    Mullins, M.C.6
  • 2
    • 0035853056 scopus 로고    scopus 로고
    • Herpes simplex virus DNA packaging sequences adopt novel structures that are specifically recognized by a component of the cleavage and packaging machinery
    • Adelman K., Salmon B., Baines J.D. Herpes simplex virus DNA packaging sequences adopt novel structures that are specifically recognized by a component of the cleavage and packaging machinery. Proceedings of the National Academy of Sciences of the United States of America 2001, 98(6):3086-3091. 10.1073/pnas.061555698.
    • (2001) Proceedings of the National Academy of Sciences of the United States of America , vol.98 , Issue.6 , pp. 3086-3091
    • Adelman, K.1    Salmon, B.2    Baines, J.D.3
  • 3
    • 84858176255 scopus 로고    scopus 로고
    • The yeast nuclear pore complex and transport through it
    • Aitchison J.D., Rout M.P. The yeast nuclear pore complex and transport through it. Genetics 2012, 190(3):855-883. 10.1534/genetics.111.127803.
    • (2012) Genetics , vol.190 , Issue.3 , pp. 855-883
    • Aitchison, J.D.1    Rout, M.P.2
  • 4
    • 36749045172 scopus 로고    scopus 로고
    • The molecular architecture of the nuclear pore complex
    • Alber F., Dokudovskaya S., Veenhoff L.M., et al. The molecular architecture of the nuclear pore complex. Nature 2007, 450(7170):695-701. 10.1038/nature06405.
    • (2007) Nature , vol.450 , Issue.7170 , pp. 695-701
    • Alber, F.1    Dokudovskaya, S.2    Veenhoff, L.M.3
  • 5
    • 84919431403 scopus 로고    scopus 로고
    • The putative herpes simplex virus 1 chaperone protein UL32 modulates disulfide bond formation during infection
    • Albright B.S., Kosinski A., Szczepaniak R., et al. The putative herpes simplex virus 1 chaperone protein UL32 modulates disulfide bond formation during infection. Journal of Virology 2015, 89(1):443-453. 10.1128/JVI.01913-14.
    • (2015) Journal of Virology , vol.89 , Issue.1 , pp. 443-453
    • Albright, B.S.1    Kosinski, A.2    Szczepaniak, R.3
  • 6
    • 34848870027 scopus 로고    scopus 로고
    • Nuclear envelope formation by chromatin-mediated reorganization of the endoplasmic reticulum
    • Anderson D.J., Hetzer M.W. Nuclear envelope formation by chromatin-mediated reorganization of the endoplasmic reticulum. Nature Cell Biology 2007, 9(10):1160-1166. 10.1038/ncb1636.
    • (2007) Nature Cell Biology , vol.9 , Issue.10 , pp. 1160-1166
    • Anderson, D.J.1    Hetzer, M.W.2
  • 7
    • 67749124115 scopus 로고    scopus 로고
    • Recruitment of functionally distinct membrane proteins to chromatin mediates nuclear envelope formation in vivo
    • Anderson D.J., Vargas J.D., Hsiao J.P., Hetzer M.W. Recruitment of functionally distinct membrane proteins to chromatin mediates nuclear envelope formation in vivo. The Journal of Cell Biology 2009, 186(2):183-191. 10.1083/jcb.200901106.
    • (2009) The Journal of Cell Biology , vol.186 , Issue.2 , pp. 183-191
    • Anderson, D.J.1    Vargas, J.D.2    Hsiao, J.P.3    Hetzer, M.W.4
  • 8
    • 70350700675 scopus 로고    scopus 로고
    • Plasma membrane and nuclear envelope integrity during the blebbing stage of apoptosis: A time-lapse study
    • Andrade R., Crisol L., Prado R., Boyano M.D., Arluzea J., Arechaga J. Plasma membrane and nuclear envelope integrity during the blebbing stage of apoptosis: A time-lapse study. Biology of the Cell 2010, 102(1):25-35. 10.1042/BC20090077.
    • (2010) Biology of the Cell , vol.102 , Issue.1 , pp. 25-35
    • Andrade, R.1    Crisol, L.2    Prado, R.3    Boyano, M.D.4    Arluzea, J.5    Arechaga, J.6
  • 9
    • 84872859459 scopus 로고    scopus 로고
    • Don't get stuck in the pore
    • Antonin W. Don't get stuck in the pore. The EMBO Journal 2013, 32(2):173-175. 10.1038/emboj.2012.338.
    • (2013) The EMBO Journal , vol.32 , Issue.2 , pp. 173-175
    • Antonin, W.1
  • 10
    • 12344317884 scopus 로고    scopus 로고
    • Nuclear pore complexes: Round the bend?
    • Antonin W., Mattaj I.W. Nuclear pore complexes: Round the bend?. Nature Cell Biology 2005, 7(1):10-12. 10.1038/ncb0105-10.
    • (2005) Nature Cell Biology , vol.7 , Issue.1 , pp. 10-12
    • Antonin, W.1    Mattaj, I.W.2
  • 11
    • 0025264189 scopus 로고
    • In vivo phosphorylation of the lamin B receptor. Binding of lamin B to its nuclear membrane receptor is affected by phosphorylation
    • Appelbaum J., Blobel G., Georgatos S.D. In vivo phosphorylation of the lamin B receptor. Binding of lamin B to its nuclear membrane receptor is affected by phosphorylation. The Journal of Biological Chemistry 1990, 265(8):4181-4184.
    • (1990) The Journal of Biological Chemistry , vol.265 , Issue.8 , pp. 4181-4184
    • Appelbaum, J.1    Blobel, G.2    Georgatos, S.D.3
  • 12
    • 84862287776 scopus 로고    scopus 로고
    • Untethering the nuclear envelope and cytoskeleton: Biologically distinct dystonias arising from a common cellular dysfunction
    • Atai N.A., Ryan S.D., Kothary R., Breakefield X.O., Nery F.C. Untethering the nuclear envelope and cytoskeleton: Biologically distinct dystonias arising from a common cellular dysfunction. International Journal of Cell Biology 2012, 2012:634214. 10.1155/2012/634214.
    • (2012) International Journal of Cell Biology , vol.2012 , pp. 634214
    • Atai, N.A.1    Ryan, S.D.2    Kothary, R.3    Breakefield, X.O.4    Nery, F.C.5
  • 13
    • 34249932986 scopus 로고    scopus 로고
    • Nucleocapsid assembly and envelopment of herpes simplex virus
    • Caister Academic Press, Norfolk, E.M. Sandri-Goldin (Ed.)
    • Baines J.D., Duffy C. Nucleocapsid assembly and envelopment of herpes simplex virus. Alpha herpesviruses 2006, 175-204. Caister Academic Press, Norfolk. E.M. Sandri-Goldin (Ed.).
    • (2006) Alpha herpesviruses , pp. 175-204
    • Baines, J.D.1    Duffy, C.2
  • 14
    • 33947368648 scopus 로고    scopus 로고
    • Electron tomography of nascent herpes simplex virus virions
    • Baines J.D., Hsieh C.E., Wills E., Mannella C., Marko M. Electron tomography of nascent herpes simplex virus virions. Journal of Virology 2007, 81(6):2726-2735. 10.1128/JVI.02571-06.
    • (2007) Journal of Virology , vol.81 , Issue.6 , pp. 2726-2735
    • Baines, J.D.1    Hsieh, C.E.2    Wills, E.3    Mannella, C.4    Marko, M.5
  • 15
    • 0028885225 scopus 로고
    • The herpes simplex virus 1 UL11 proteins are associated with cytoplasmic and nuclear membranes and with nuclear bodies of infected cells
    • Baines J.D., Jacob R.J., Simmerman L., Roizman B. The herpes simplex virus 1 UL11 proteins are associated with cytoplasmic and nuclear membranes and with nuclear bodies of infected cells. Journal of Virology 1995, 69(2):825-833.
    • (1995) Journal of Virology , vol.69 , Issue.2 , pp. 825-833
    • Baines, J.D.1    Jacob, R.J.2    Simmerman, L.3    Roizman, B.4
  • 16
    • 33846040281 scopus 로고    scopus 로고
    • Glycoprotein M of herpes simplex virus 1 is incorporated into virions during budding at the inner nuclear membrane
    • Baines J.D., Wills E., Jacob R.J., Pennington J., Roizman B. Glycoprotein M of herpes simplex virus 1 is incorporated into virions during budding at the inner nuclear membrane. Journal of Virology 2007, 81(2):800-812. 10.1128/JVI.01756-06.
    • (2007) Journal of Virology , vol.81 , Issue.2 , pp. 800-812
    • Baines, J.D.1    Wills, E.2    Jacob, R.J.3    Pennington, J.4    Roizman, B.5
  • 17
    • 27744487093 scopus 로고    scopus 로고
    • Common ancestry of herpesviruses and tailed DNA bacteriophages
    • Baker M.L., Jiang W., Rixon F.J., Chiu W. Common ancestry of herpesviruses and tailed DNA bacteriophages. Journal of Virology 2005, 79(23):14967-14970. 10.1128/JVI.79.23.14967-14970.2005.
    • (2005) Journal of Virology , vol.79 , Issue.23 , pp. 14967-14970
    • Baker, M.L.1    Jiang, W.2    Rixon, F.J.3    Chiu, W.4
  • 18
    • 77952569645 scopus 로고    scopus 로고
    • An integrated protein localization and interaction map for Potato yellow dwarf virus, type species of the genus Nucleorhabdovirus
    • Bandyopadhyay A., Kopperud K., Anderson G., Martin K., Goodin M. An integrated protein localization and interaction map for Potato yellow dwarf virus, type species of the genus Nucleorhabdovirus. Virology 2010, 402(1):61-71. 10.1016/j.virol.2010.03.013.
    • (2010) Virology , vol.402 , Issue.1 , pp. 61-71
    • Bandyopadhyay, A.1    Kopperud, K.2    Anderson, G.3    Martin, K.4    Goodin, M.5
  • 19
    • 60649115824 scopus 로고    scopus 로고
    • Comparative proteomic analyses of the nuclear envelope and pore complex suggests a wide range of heretofore unexpected functions
    • Batrakou D.G., Kerr A.R., Schirmer E.C. Comparative proteomic analyses of the nuclear envelope and pore complex suggests a wide range of heretofore unexpected functions. Journal of Proteomics 2009, 72(1):56-70. 10.1016/j.jprot.2008.09.004.
    • (2009) Journal of Proteomics , vol.72 , Issue.1 , pp. 56-70
    • Batrakou, D.G.1    Kerr, A.R.2    Schirmer, E.C.3
  • 20
    • 34548590272 scopus 로고    scopus 로고
    • NSF- and SNARE-mediated membrane fusion is required for nuclear envelope formation and completion of nuclear pore complex assembly in Xenopus laevis egg extracts
    • Baur T., Ramadan K., Schlundt A., Kartenbeck J., Meyer H.H. NSF- and SNARE-mediated membrane fusion is required for nuclear envelope formation and completion of nuclear pore complex assembly in Xenopus laevis egg extracts. Journal of Cell Science 2007, 120(Pt. 16):2895-2903. 10.1242/jcs.010181.
    • (2007) Journal of Cell Science , vol.120 , pp. 2895-2903
    • Baur, T.1    Ramadan, K.2    Schlundt, A.3    Kartenbeck, J.4    Meyer, H.H.5
  • 21
    • 0036239144 scopus 로고    scopus 로고
    • DNA cleavage and packaging proteins encoded by genes U(L)28, U(L)15, and U(L)33 of herpes simplex virus type 1 form a complex in infected cells
    • Beard P.M., Taus N.S., Baines J.D. DNA cleavage and packaging proteins encoded by genes U(L)28, U(L)15, and U(L)33 of herpes simplex virus type 1 form a complex in infected cells. Journal of Virology 2002, 76(10):4785-4791.
    • (2002) Journal of Virology , vol.76 , Issue.10 , pp. 4785-4791
    • Beard, P.M.1    Taus, N.S.2    Baines, J.D.3
  • 22
    • 84950268155 scopus 로고    scopus 로고
    • Structural basis of membrane budding by the nuclear egress complex of herpesviruses
    • Bigalke J.M., Heldwein E.E. Structural basis of membrane budding by the nuclear egress complex of herpesviruses. The EMBO Journal 2015, 10.15252/embj.201592359.
    • (2015) The EMBO Journal
    • Bigalke, J.M.1    Heldwein, E.E.2
  • 23
    • 84940547871 scopus 로고    scopus 로고
    • The great (nuclear) escape: New insights into the role of the nuclear egress complex of herpesviruses
    • Bigalke J.M., Heldwein E.E. The great (nuclear) escape: New insights into the role of the nuclear egress complex of herpesviruses. Journal of Virology 2015, 89(18):9150-9153. 10.1128/JVI.02530-14.
    • (2015) Journal of Virology , vol.89 , Issue.18 , pp. 9150-9153
    • Bigalke, J.M.1    Heldwein, E.E.2
  • 24
    • 84902322686 scopus 로고    scopus 로고
    • Membrane deformation and scission by the HSV-1 nuclear egress complex
    • Bigalke J.M., Heuser T., Nicastro D., Heldwein E.E. Membrane deformation and scission by the HSV-1 nuclear egress complex. Nature Communications 2014, 5:4131. 10.1038/ncomms5131.
    • (2014) Nature Communications , vol.5 , pp. 4131
    • Bigalke, J.M.1    Heuser, T.2    Nicastro, D.3    Heldwein, E.E.4
  • 25
    • 0038467608 scopus 로고    scopus 로고
    • Effects of charged cluster mutations on the function of herpes simplex virus type 1 UL34 protein
    • Bjerke S.L., Cowan J.M., Kerr J.K., Reynolds A.E., Baines J.D., Roller R.J. Effects of charged cluster mutations on the function of herpes simplex virus type 1 UL34 protein. Journal of Virology 2003, 77(13):7601-7610.
    • (2003) Journal of Virology , vol.77 , Issue.13 , pp. 7601-7610
    • Bjerke, S.L.1    Cowan, J.M.2    Kerr, J.K.3    Reynolds, A.E.4    Baines, J.D.5    Roller, R.J.6
  • 26
    • 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(2):261-276. 10.1016/j.virol.2005.11.053.
    • (2006) Virology , vol.347 , Issue.2 , pp. 261-276
    • Bjerke, S.L.1    Roller, R.J.2
  • 27
    • 0028362205 scopus 로고
    • An amino acid sequence shared by the herpes simplex virus 1 alpha regulatory proteins 0, 4, 22, and 27 predicts the nucleotidylylation of the UL21, UL31, UL47, and UL49 gene products
    • Blaho J.A., Mitchell C., Roizman B. An amino acid sequence shared by the herpes simplex virus 1 alpha regulatory proteins 0, 4, 22, and 27 predicts the nucleotidylylation of the UL21, UL31, UL47, and UL49 gene products. The Journal of Biological Chemistry 1994, 269(26):17401-17410.
    • (1994) The Journal of Biological Chemistry , vol.269 , Issue.26 , pp. 17401-17410
    • Blaho, J.A.1    Mitchell, C.2    Roizman, B.3
  • 28
    • 0031936307 scopus 로고    scopus 로고
    • The gene product of human cytomegalovirus open reading frame UL56 binds the pac motif and has specific nuclease activity
    • Bogner E., Radsak K., Stinski M.F. The gene product of human cytomegalovirus open reading frame UL56 binds the pac motif and has specific nuclease activity. Journal of Virology 1998, 72(3):2259-2264.
    • (1998) Journal of Virology , vol.72 , Issue.3 , pp. 2259-2264
    • Bogner, E.1    Radsak, K.2    Stinski, M.F.3
  • 29
    • 84908425887 scopus 로고    scopus 로고
    • Nuclear herpesvirus capsid motility is not dependent on F-actin
    • Bosse J.B., Virding S., Thiberge S.Y., et al. Nuclear herpesvirus capsid motility is not dependent on F-actin. MBio 2014, 5(5):e01909-e01914. 10.1128/mBio.01909-14.
    • (2014) MBio , vol.5 , Issue.5
    • Bosse, J.B.1    Virding, S.2    Thiberge, S.Y.3
  • 30
    • 35348855680 scopus 로고    scopus 로고
    • Molecular biology of the baculovirus occlusion-derived virus envelope
    • Braunagel S.C., Summers M.D. Molecular biology of the baculovirus occlusion-derived virus envelope. Current Drug Targets 2007, 8(10):1084-1095.
    • (2007) Current Drug Targets , vol.8 , Issue.10 , pp. 1084-1095
    • Braunagel, S.C.1    Summers, M.D.2
  • 31
    • 0034879921 scopus 로고    scopus 로고
    • TorsinA: Movement at many levels
    • Breakefield X.O., Kamm C., Hanson P.I. TorsinA: Movement at many levels. Neuron 2001, 31(1):9-12.
    • (2001) Neuron , vol.31 , Issue.1 , pp. 9-12
    • Breakefield, X.O.1    Kamm, C.2    Hanson, P.I.3
  • 33
    • 0035264543 scopus 로고    scopus 로고
    • Transmission of human papillomavirus type 11 infection by desquamated cornified cells
    • Bryan J.T., Brown D.R. Transmission of human papillomavirus type 11 infection by desquamated cornified cells. Virology 2001, 281(1):35-42. 10.1006/viro.2000.0777.
    • (2001) Virology , vol.281 , Issue.1 , pp. 35-42
    • Bryan, J.T.1    Brown, D.R.2
  • 34
    • 3242715831 scopus 로고    scopus 로고
    • Comprehensive mutational analysis of a herpesvirus gene in the viral genome context reveals a region essential for virus replication
    • Bubeck A., Wagner M., Ruzsics Z., et al. Comprehensive mutational analysis of a herpesvirus gene in the viral genome context reveals a region essential for virus replication. Journal of Virology 2004, 78(15):8026-8035. 10.1128/JVI.78.15.8026-8035.2004.
    • (2004) Journal of Virology , vol.78 , Issue.15 , pp. 8026-8035
    • Bubeck, A.1    Wagner, M.2    Ruzsics, Z.3
  • 35
    • 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. Journal of Virology 2010, 84(14):7005-7017. 10.1128/JVI.00719-10.
    • (2010) Journal of Virology , vol.84 , Issue.14 , pp. 7005-7017
    • Buchkovich, N.J.1    Maguire, T.G.2    Alwine, J.C.3
  • 36
    • 34147100237 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 tegument proteins VP1/2 and UL37 are associated with intranuclear capsids
    • Bucks M.A., O'Regan K.J., Murphy M.A., Wills J.W., Courtney R.J. Herpes simplex virus type 1 tegument proteins VP1/2 and UL37 are associated with intranuclear capsids. Virology 2007, 361(2):316-324. 10.1016/j.virol.2006.11.031.
    • (2007) Virology , vol.361 , Issue.2 , pp. 316-324
    • Bucks, M.A.1    O'Regan, K.J.2    Murphy, M.A.3    Wills, J.W.4    Courtney, R.J.5
  • 37
    • 0035197044 scopus 로고    scopus 로고
    • Dynamics of the nuclear envelope at mitosis and during apoptosis
    • Buendia B., Courvalin J.C., Collas P. Dynamics of the nuclear envelope at mitosis and during apoptosis. Cellular and Molecular Life Sciences 2001, 58(12-13):1781-1789.
    • (2001) Cellular and Molecular Life Sciences , vol.58 , Issue.12-13 , pp. 1781-1789
    • Buendia, B.1    Courvalin, J.C.2    Collas, P.3
  • 38
    • 84861551061 scopus 로고    scopus 로고
    • It takes KASH to hitch to the SUN
    • Burke B. It takes KASH to hitch to the SUN. Cell 2012, 149(5):961-963. 10.1016/j.cell.2012.05.004.
    • (2012) Cell , vol.149 , Issue.5 , pp. 961-963
    • Burke, B.1
  • 39
    • 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. Journal of Virology 2007, 81(6):3042-3048. 10.1128/JVI.01564-06.
    • (2007) Journal of Virology , vol.81 , Issue.6 , pp. 3042-3048
    • Buser, C.1    Walther, P.2    Mertens, T.3    Michel, D.4
  • 40
    • 33745267085 scopus 로고    scopus 로고
    • The egress of herpesviruses from cells: The unanswered questions
    • (author replies 6717-6719)
    • Campadelli-Fiume G., Roizman B. The egress of herpesviruses from cells: The unanswered questions. Journal of Virology 2006, 80(13):6716-6717. (author replies 6717-6719). 10.1128/JVI.00386-06.
    • (2006) Journal of Virology , vol.80 , Issue.13 , pp. 6716-6717
    • Campadelli-Fiume, G.1    Roizman, B.2
  • 41
    • 69249222501 scopus 로고    scopus 로고
    • Herpes simplex virus 2 UL13 protein kinase disrupts nuclear lamins
    • Cano-Monreal G.L., Wylie K.M., Cao F., Tavis J.E., Morrison L.A. Herpes simplex virus 2 UL13 protein kinase disrupts nuclear lamins. Virology 2009, 392(1):137-147. 10.1016/j.virol.2009.06.051.
    • (2009) Virology , vol.392 , Issue.1 , pp. 137-147
    • Cano-Monreal, G.L.1    Wylie, K.M.2    Cao, F.3    Tavis, J.E.4    Morrison, L.A.5
  • 42
    • 33745806517 scopus 로고    scopus 로고
    • The carboxyl-terminal nucleoplasmic region of MAN1 exhibits a DNA binding winged helix domain
    • Caputo S., Couprie J., Duband-Goulet I., et al. The carboxyl-terminal nucleoplasmic region of MAN1 exhibits a DNA binding winged helix domain. The Journal of Biological Chemistry 2006, 281(26):18208-18215. 10.1074/jbc.M601980200.
    • (2006) The Journal of Biological Chemistry , vol.281 , Issue.26 , pp. 18208-18215
    • Caputo, S.1    Couprie, J.2    Duband-Goulet, I.3
  • 43
    • 84858240360 scopus 로고    scopus 로고
    • Procapsid assembly, maturation, nuclear exit: Dynamic steps in the production of infectious herpesvirions
    • Cardone G., Heymann J.B., Cheng N., Trus B.L., Steven A.C. Procapsid assembly, maturation, nuclear exit: Dynamic steps in the production of infectious herpesvirions. Advances in Experimental Medicine and Biology 2012, 726:423-439. 10.1007/978-1-4614-0980-9_19.
    • (2012) Advances in Experimental Medicine and Biology , vol.726 , pp. 423-439
    • Cardone, G.1    Heymann, J.B.2    Cheng, N.3    Trus, B.L.4    Steven, A.C.5
  • 44
    • 0030863707 scopus 로고    scopus 로고
    • The null mutant of the U(L)31 gene of herpes simplex virus 1: Construction and phenotype in infected cells
    • Chang Y.E., Van Sant C., Krug P.W., Sears A.E., Roizman B. The null mutant of the U(L)31 gene of herpes simplex virus 1: Construction and phenotype in infected cells. Journal of Virology 1997, 71(11):8307-8315.
    • (1997) Journal of Virology , vol.71 , Issue.11 , pp. 8307-8315
    • Chang, Y.E.1    Van Sant, C.2    Krug, P.W.3    Sears, A.E.4    Roizman, B.5
  • 45
    • 0034011617 scopus 로고    scopus 로고
    • A protein kinase activity associated with Epstein-Barr virus BGLF4 phosphorylates the viral early antigen EA-D in vitro
    • Chen M.R., Chang S.J., Huang H., Chen J.Y. A protein kinase activity associated with Epstein-Barr virus BGLF4 phosphorylates the viral early antigen EA-D in vitro. Journal of Virology 2000, 74(7):3093-3104.
    • (2000) Journal of Virology , vol.74 , Issue.7 , pp. 3093-3104
    • Chen, M.R.1    Chang, S.J.2    Huang, H.3    Chen, J.Y.4
  • 46
    • 79960897397 scopus 로고    scopus 로고
    • How viruses access the nucleus
    • Cohen S., Au S., Panté N. How viruses access the nucleus. Biochimica et Biophysica Acta 2011, 1813(9):1634-1645. 10.1016/j.bbamcr.2010.12.009.
    • (2011) Biochimica et Biophysica Acta , vol.1813 , Issue.9 , pp. 1634-1645
    • Cohen, S.1    Au, S.2    Panté, N.3
  • 47
    • 33750279611 scopus 로고    scopus 로고
    • Parvoviral nuclear import: Bypassing the host nuclear-transport machinery
    • Cohen S., Behzad A.R., Carroll J.B., Panté N. Parvoviral nuclear import: Bypassing the host nuclear-transport machinery. The Journal of General Virology 2006, 87(Pt. 11):3209-3213. 10.1099/vir.0.82232-0.
    • (2006) The Journal of General Virology , vol.87 , pp. 3209-3213
    • Cohen, S.1    Behzad, A.R.2    Carroll, J.B.3    Panté, N.4
  • 48
    • 28044462666 scopus 로고    scopus 로고
    • Pushing the envelope: Microinjection of Minute virus of mice into Xenopus oocytes causes damage to the nuclear envelope
    • Cohen S., Panté N. Pushing the envelope: Microinjection of Minute virus of mice into Xenopus oocytes causes damage to the nuclear envelope. The Journal of General Virology 2005, 86(Pt. 12):3243-3252. 10.1099/vir.0.80967-0.
    • (2005) The Journal of General Virology , vol.86 , pp. 3243-3252
    • Cohen, S.1    Panté, N.2
  • 49
    • 44449095617 scopus 로고    scopus 로고
    • The nuclear envelope as an integrator of nuclear and cytoplasmic architecture
    • Crisp M., Burke B. The nuclear envelope as an integrator of nuclear and cytoplasmic architecture. FEBS Letters 2008, 582(14):2023-2032. 10.1016/j.febslet.2008.05.001.
    • (2008) FEBS Letters , vol.582 , Issue.14 , pp. 2023-2032
    • Crisp, M.1    Burke, B.2
  • 50
    • 29944445023 scopus 로고    scopus 로고
    • Coupling of the nucleus and cytoplasm: Role of the LINC complex
    • Crisp M., Liu Q., Roux K., et al. Coupling of the nucleus and cytoplasm: Role of the LINC complex. The Journal of Cell Biology 2006, 172(1):41-53. 10.1083/jcb.200509124.
    • (2006) The Journal of Cell Biology , vol.172 , Issue.1 , pp. 41-53
    • Crisp, M.1    Liu, Q.2    Roux, K.3
  • 51
    • 0034604023 scopus 로고    scopus 로고
    • PKC-delta is an apoptotic lamin kinase
    • Cross T., Griffiths G., Deacon E., et al. PKC-delta is an apoptotic lamin kinase. Oncogene 2000, 19(19):2331-2337. 10.1038/sj.onc.1203555.
    • (2000) Oncogene , vol.19 , Issue.19 , pp. 2331-2337
    • Cross, T.1    Griffiths, G.2    Deacon, E.3
  • 52
    • 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. Journal of Virology 2007, 81(14):7380-7387. 10.1128/JVI.00222-07.
    • (2007) Journal of Virology , vol.81 , Issue.14 , pp. 7380-7387
    • Crump, C.M.1    Yates, C.2    Minson, T.3
  • 53
    • 77952883755 scopus 로고    scopus 로고
    • Herpesvirus systematics
    • Davison A.J. Herpesvirus systematics. Veterinary Microbiology 2010, 143(1):52-69. 10.1016/j.vetmic.2010.02.014.
    • (2010) Veterinary Microbiology , vol.143 , Issue.1 , pp. 52-69
    • Davison, A.J.1
  • 54
    • 58149308301 scopus 로고    scopus 로고
    • The order herpesvirales
    • Davison A.J., Eberle R., Ehlers B., et al. The order herpesvirales. Archives of Virology 2009, 154(1):171-177. 10.1007/s00705-008-0278-4.
    • (2009) Archives of Virology , vol.154 , Issue.1 , pp. 171-177
    • Davison, A.J.1    Eberle, R.2    Ehlers, B.3
  • 56
    • 41649097238 scopus 로고    scopus 로고
    • Nuclear lamins: Major factors in the structural organization and function of the nucleus and chromatin
    • Dechat T., Pfleghaar K., Sengupta K., et al. Nuclear lamins: Major factors in the structural organization and function of the nucleus and chromatin. Genes and Development 2008, 22(7):832-853. 10.1101/gad.1652708.
    • (2008) Genes and Development , vol.22 , Issue.7 , pp. 832-853
    • Dechat, T.1    Pfleghaar, K.2    Sengupta, K.3
  • 57
    • 0033926099 scopus 로고    scopus 로고
    • Review: Lamina-associated polypeptide 2 isoforms and related proteins in cell cycle-dependent nuclear structure dynamics
    • Dechat T., Vlcek S., Foisner R. Review: Lamina-associated polypeptide 2 isoforms and related proteins in cell cycle-dependent nuclear structure dynamics. Journal of Structural Biology 2000, 129(2-3):335-345. 10.1006/jsbi.2000.4212.
    • (2000) Journal of Structural Biology , vol.129 , Issue.2-3 , pp. 335-345
    • Dechat, T.1    Vlcek, S.2    Foisner, R.3
  • 58
    • 84891533416 scopus 로고    scopus 로고
    • Tissue specificity in the nuclear envelope supports its functional complexity
    • de Las Heras J.I., Meinke P., Batrakou D.G., et al. Tissue specificity in the nuclear envelope supports its functional complexity. Nucleus 2013, 4(6):460-477. 10.4161/nucl.26872.
    • (2013) Nucleus , vol.4 , Issue.6 , pp. 460-477
    • de Las Heras, J.I.1    Meinke, P.2    Batrakou, D.G.3
  • 59
    • 84855961718 scopus 로고    scopus 로고
    • Reconstitution of the Kaposi's sarcoma-associated herpesvirus nuclear egress complex and formation of nuclear membrane vesicles by coexpression of ORF67 and ORF69 gene products
    • Desai P.J., Pryce E.N., Henson B.W., Luitweiler E.M., Cothran J. Reconstitution of the Kaposi's sarcoma-associated herpesvirus nuclear egress complex and formation of nuclear membrane vesicles by coexpression of ORF67 and ORF69 gene products. Journal of Virology 2012, 86(1):594-598. 10.1128/JVI.05988-11.
    • (2012) Journal of Virology , vol.86 , Issue.1 , pp. 594-598
    • Desai, P.J.1    Pryce, E.N.2    Henson, B.W.3    Luitweiler, E.M.4    Cothran, J.5
  • 60
    • 84932474722 scopus 로고
    • Nucleo-cytoplasmic interaction following meiosis in the young microspores of Lilium longiflorum; Events at the nuclear envelope
    • Dickinson H.G. Nucleo-cytoplasmic interaction following meiosis in the young microspores of Lilium longiflorum; Events at the nuclear envelope. Grana 1971, 11(2):117-127.
    • (1971) Grana , vol.11 , Issue.2 , pp. 117-127
    • Dickinson, H.G.1
  • 61
    • 77957743829 scopus 로고    scopus 로고
    • Live imaging of single nuclear pores reveals unique assembly kinetics and mechanism in interphase
    • Dultz E., Ellenberg J. Live imaging of single nuclear pores reveals unique assembly kinetics and mechanism in interphase. The Journal of Cell Biology 2010, 191(1):15-22. 10.1083/jcb.201007076.
    • (2010) The Journal of Cell Biology , vol.191 , Issue.1 , pp. 15-22
    • Dultz, E.1    Ellenberg, J.2
  • 62
    • 40849097593 scopus 로고    scopus 로고
    • Systematic kinetic analysis of mitotic dis- and reassembly of the nuclear pore in living cells
    • Dultz E., Zanin E., Wurzenberger C., et al. Systematic kinetic analysis of mitotic dis- and reassembly of the nuclear pore in living cells. The Journal of Cell Biology 2008, 180(5):857-865. 10.1083/jcb.200707026.
    • (2008) The Journal of Cell Biology , vol.180 , Issue.5 , pp. 857-865
    • Dultz, E.1    Zanin, E.2    Wurzenberger, C.3
  • 64
    • 70349641036 scopus 로고    scopus 로고
    • Nuclear membrane-derived autophagy, a novel process that participates in the presentation of endogenous viral antigens during HSV-1 infection
    • English L., Chemali M., Desjardins M. Nuclear membrane-derived autophagy, a novel process that participates in the presentation of endogenous viral antigens during HSV-1 infection. Autophagy 2009, 5(7):1026-1029.
    • (2009) Autophagy , vol.5 , Issue.7 , pp. 1026-1029
    • English, L.1    Chemali, M.2    Desjardins, M.3
  • 65
  • 66
    • 84878838773 scopus 로고    scopus 로고
    • KSHV ORF67 encoded lytic protein localizes on the nuclear membrane and alters emerin distribution
    • Farina A., Santarelli R., Bloise R., et al. KSHV ORF67 encoded lytic protein localizes on the nuclear membrane and alters emerin distribution. Virus Research 2013, 175(2):143-150. 10.1016/j.virusres.2013.04.001.
    • (2013) Virus Research , vol.175 , Issue.2 , pp. 143-150
    • Farina, A.1    Santarelli, R.2    Bloise, R.3
  • 67
    • 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. Proceedings of the National Academy of Sciences of the United States of America 2007, 104(24):10187-10192. 10.1073/pnas.0703790104.
    • (2007) Proceedings of the National Academy of Sciences of the United States of America , vol.104 , Issue.24 , pp. 10187-10192
    • Farnsworth, A.1    Wisner, T.W.2    Webb, M.3
  • 68
    • 33748065004 scopus 로고    scopus 로고
    • Alpha-herpesvirus infection induces the formation of nuclear actin filaments
    • Feierbach B., Piccinotti S., Bisher M., Denk W., Enquist L.W. Alpha-herpesvirus infection induces the formation of nuclear actin filaments. PLoS Pathogen 2006, 2(8):e85. 10.1371/journal.ppat.0020085.
    • (2006) PLoS Pathogen , vol.2 , Issue.8
    • Feierbach, B.1    Piccinotti, S.2    Bisher, M.3    Denk, W.4    Enquist, L.W.5
  • 70
    • 84889585090 scopus 로고    scopus 로고
    • Nobel 2013 physiology or medicine: Traffic control system within cells
    • Ferro-Novick S., Brose N. Nobel 2013 physiology or medicine: Traffic control system within cells. Nature 2013, 504(7478):98. 10.1038/504098a.
    • (2013) Nature , vol.504 , Issue.7478 , pp. 98
    • Ferro-Novick, S.1    Brose, N.2
  • 71
    • 0027276759 scopus 로고
    • Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation
    • Foisner R., Gerace L. Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation. Cell 1993, 73(7):1267-1279.
    • (1993) Cell , vol.73 , Issue.7 , pp. 1267-1279
    • Foisner, R.1    Gerace, L.2
  • 72
    • 17344368861 scopus 로고    scopus 로고
    • Active intranuclear movement of herpesvirus capsids
    • Forest T., Barnard S., Baines J.D. Active intranuclear movement of herpesvirus capsids. Nature Cell Biology 2005, 7(4):429-431. 10.1038/ncb1243.
    • (2005) Nature Cell Biology , vol.7 , Issue.4 , pp. 429-431
    • Forest, T.1    Barnard, S.2    Baines, J.D.3
  • 73
    • 70349677166 scopus 로고    scopus 로고
    • Evolutionarily conserved herpesviral protein interaction networks
    • Fossum E., Friedel C.C., Rajagopala S.V., et al. Evolutionarily conserved herpesviral protein interaction networks. PLoS Pathogen 2009, 5(9):e1000570. 10.1371/journal.ppat.1000570.
    • (2009) PLoS Pathogen , vol.5 , Issue.9
    • Fossum, E.1    Friedel, C.C.2    Rajagopala, S.V.3
  • 74
    • 77957735230 scopus 로고    scopus 로고
    • Kinesin-1 and dynein at the nuclear envelope mediate the bidirectional migrations of nuclei
    • Fridolfsson H.N., Starr D.A. Kinesin-1 and dynein at the nuclear envelope mediate the bidirectional migrations of nuclei. The Journal of Cell Biology 2010, 191(1):115-128. 10.1083/jcb.201004118.
    • (2010) The Journal of Cell Biology , vol.191 , Issue.1 , pp. 115-128
    • Fridolfsson, H.N.1    Starr, D.A.2
  • 75
    • 0036278491 scopus 로고    scopus 로고
    • The UL48 tegument protein of pseudorabies virus is critical for intracytoplasmic assembly of infectious virions
    • Fuchs W., Granzow H., Klupp B.G., Kopp M., Mettenleiter T.C. The UL48 tegument protein of pseudorabies virus is critical for intracytoplasmic assembly of infectious virions. Journal of Virology 2002, 76(13):6729-6742.
    • (2002) Journal of Virology , vol.76 , Issue.13 , pp. 6729-6742
    • Fuchs, W.1    Granzow, H.2    Klupp, B.G.3    Kopp, M.4    Mettenleiter, T.C.5
  • 76
    • 64049095269 scopus 로고    scopus 로고
    • Characterization of pseudorabies virus (PrV) cleavage-encapsidation proteins and functional complementation of PrV pUL32 by the homologous protein of herpes simplex virus type 1
    • Fuchs W., Klupp B.G., Granzow H., Leege T., Mettenleiter T.C. Characterization of pseudorabies virus (PrV) cleavage-encapsidation proteins and functional complementation of PrV pUL32 by the homologous protein of herpes simplex virus type 1. Journal of Virology 2009, 83(8):3930-3943. 10.1128/JVI.02636-08.
    • (2009) Journal of Virology , vol.83 , Issue.8 , pp. 3930-3943
    • Fuchs, W.1    Klupp, B.G.2    Granzow, H.3    Leege, T.4    Mettenleiter, T.C.5
  • 77
    • 6344219960 scopus 로고    scopus 로고
    • Essential function of the pseudorabies virus UL36 gene product is independent of its interaction with the UL37 protein
    • Fuchs W., Klupp B.G., Granzow H., Mettenleiter T.C. Essential function of the pseudorabies virus UL36 gene product is independent of its interaction with the UL37 protein. Journal of Virology 2004, 78(21):11879-11889. 10.1128/JVI.78.21.11879-11889.2004.
    • (2004) Journal of Virology , vol.78 , Issue.21 , pp. 11879-11889
    • Fuchs, W.1    Klupp, B.G.2    Granzow, H.3    Mettenleiter, T.C.4
  • 78
    • 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., Osterrieder N., Mettenleiter T.C. 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. Journal of Virology 2002, 76(1):364-378.
    • (2002) Journal of Virology , vol.76 , Issue.1 , pp. 364-378
    • Fuchs, W.1    Klupp, B.G.2    Granzow, H.3    Osterrieder, N.4    Mettenleiter, T.C.5
  • 79
    • 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
    • Funk C., Ott M., Raschbichler V., et al. The herpes simplex virus protein pUL31 escorts nucleocapsids to sites of nuclear egress, a process coordinated by its N-terminal domain. PLoS Pathogen 2015, 11(6):e1004957. 10.1371/journal.ppat.1004957.
    • (2015) PLoS Pathogen , vol.11 , Issue.6
    • Funk, C.1    Ott, M.2    Raschbichler, V.3
  • 80
    • 0033594083 scopus 로고    scopus 로고
    • Roles of LAP2 proteins in nuclear assembly and DNA replication: Truncated LAP2beta proteins alter lamina assembly, envelope formation, nuclear size, and DNA replication efficiency in Xenopus laevis extracts
    • Gant T.M., Harris C.A., Wilson K.L. Roles of LAP2 proteins in nuclear assembly and DNA replication: Truncated LAP2beta proteins alter lamina assembly, envelope formation, nuclear size, and DNA replication efficiency in Xenopus laevis extracts. The Journal of Cell Biology 1999, 144(6):1083-1096.
    • (1999) The Journal of Cell Biology , vol.144 , Issue.6 , pp. 1083-1096
    • Gant, T.M.1    Harris, C.A.2    Wilson, K.L.3
  • 82
    • 77951177406 scopus 로고    scopus 로고
    • Activation of cyclin B1-Cdk1 synchronizes events in the nucleus and the cytoplasm at mitosis
    • Gavet O., Pines J. Activation of cyclin B1-Cdk1 synchronizes events in the nucleus and the cytoplasm at mitosis. The Journal of Cell Biology 2010, 189(2):247-259. 10.1083/jcb.200909144.
    • (2010) The Journal of Cell Biology , vol.189 , Issue.2 , pp. 247-259
    • Gavet, O.1    Pines, J.2
  • 83
    • 0035875916 scopus 로고    scopus 로고
    • The inner nuclear membrane: Simple, or very complex?
    • Georgatos S.D. The inner nuclear membrane: Simple, or very complex?. The EMBO Journal 2001, 20(12):2989-2994. 10.1093/emboj/20.12.2989.
    • (2001) The EMBO Journal , vol.20 , Issue.12 , pp. 2989-2994
    • Georgatos, S.D.1
  • 84
    • 84901473315 scopus 로고    scopus 로고
    • Lamina-associated polypeptide (LAP)2alpha and nucleoplasmic lamins in adult stem cell regulation and disease
    • Gesson K., Vidak S., Foisner R. Lamina-associated polypeptide (LAP)2alpha and nucleoplasmic lamins in adult stem cell regulation and disease. Seminars in Cell and Developmental Biology 2014, 29:116-124. 10.1016/j.semcdb.2013.12.009.
    • (2014) Seminars in Cell and Developmental Biology , vol.29 , pp. 116-124
    • Gesson, K.1    Vidak, S.2    Foisner, R.3
  • 85
    • 84892661895 scopus 로고    scopus 로고
    • When yeast cells meet, karyogamy!: An example of nuclear migration slowly resolved
    • Gibeaux R., Knop M. When yeast cells meet, karyogamy!: An example of nuclear migration slowly resolved. Nucleus 2013, 4(3):182-188. 10.4161/nucl.25021.
    • (2013) Nucleus , vol.4 , Issue.3 , pp. 182-188
    • Gibeaux, R.1    Knop, M.2
  • 86
    • 84857974470 scopus 로고    scopus 로고
    • The Simian virus 40 late viral protein VP4 disrupts the nuclear envelope for viral release
    • Giorda K.M., Raghava S., Hebert D.N. The Simian virus 40 late viral protein VP4 disrupts the nuclear envelope for viral release. Journal of Virology 2012, 86(6):3180-3192. 10.1128/JVI.07047-11.
    • (2012) Journal of Virology , vol.86 , Issue.6 , pp. 3180-3192
    • Giorda, K.M.1    Raghava, S.2    Hebert, D.N.3
  • 87
    • 0022516246 scopus 로고
    • Synthetic peptides as nuclear localization signals
    • Goldfarb D.S., Gariepy J., Schoolnik G., Kornberg R.D. Synthetic peptides as nuclear localization signals. Nature 1986, 322(6080):641-644. 10.1038/322641a0.
    • (1986) Nature , vol.322 , Issue.6080 , pp. 641-644
    • Goldfarb, D.S.1    Gariepy, J.2    Schoolnik, G.3    Kornberg, R.D.4
  • 88
    • 20044393307 scopus 로고    scopus 로고
    • Characterization and intracellular localization of the Epstein-Barr virus protein BFLF2: Interactions with BFRF1 and with the nuclear lamina
    • Gonnella R., Farina A., Santarelli R., et al. Characterization and intracellular localization of the Epstein-Barr virus protein BFLF2: Interactions with BFRF1 and with the nuclear lamina. Journal of Virology 2005, 79(6):3713-3727. 10.1128/JVI.79.6.3713-3727.2005.
    • (2005) Journal of Virology , vol.79 , Issue.6 , pp. 3713-3727
    • Gonnella, R.1    Farina, A.2    Santarelli, R.3
  • 89
    • 84948579265 scopus 로고    scopus 로고
    • Access of torsinA to the inner nuclear membrane is activity dependent and regulated in the endoplasmic reticulum
    • Goodchild R.E., Buchwalter A.L., Naismith T.V., et al. Access of torsinA to the inner nuclear membrane is activity dependent and regulated in the endoplasmic reticulum. Journal of Cell Science 2015, 128(15):2854-2865. 10.1242/jcs.167452.
    • (2015) Journal of Cell Science , vol.128 , Issue.15 , pp. 2854-2865
    • Goodchild, R.E.1    Buchwalter, A.L.2    Naismith, T.V.3
  • 91
    • 15444374750 scopus 로고    scopus 로고
    • The AAA+ protein torsinA interacts with a conserved domain present in LAP1 and a novel ER protein
    • Goodchild R.E., Dauer W.T. The AAA+ protein torsinA interacts with a conserved domain present in LAP1 and a novel ER protein. The Journal of Cell Biology 2005, 168(6):855-862. 10.1083/jcb.200411026.
    • (2005) The Journal of Cell Biology , vol.168 , Issue.6 , pp. 855-862
    • Goodchild, R.E.1    Dauer, W.T.2
  • 92
    • 34249775773 scopus 로고    scopus 로고
    • Membrane and protein dynamics in live plant nuclei infected with Sonchus yellow net virus, a plant-adapted rhabdovirus
    • Goodin M.M., Chakrabarty R., Yelton S., Martin K., Clark A., Brooks R. Membrane and protein dynamics in live plant nuclei infected with Sonchus yellow net virus, a plant-adapted rhabdovirus. The Journal of General Virology 2007, 88(Pt. 6):1810-1820. 10.1099/vir.0.82698-0.
    • (2007) The Journal of General Virology , vol.88 , pp. 1810-1820
    • Goodin, M.M.1    Chakrabarty, R.2    Yelton, S.3    Martin, K.4    Clark, A.5    Brooks, R.6
  • 93
    • 84855221276 scopus 로고    scopus 로고
    • Single-molecule studies of nucleocytoplasmic transport: From one dimension to three dimensions
    • Goryaynov A., Ma J., Yang W. Single-molecule studies of nucleocytoplasmic transport: From one dimension to three dimensions. Integrative Biology (Cambridge) 2012, 4(1):10-21. 10.1039/c1ib00041a.
    • (2012) Integrative Biology (Cambridge) , vol.4 , Issue.1 , pp. 10-21
    • Goryaynov, A.1    Ma, J.2    Yang, W.3
  • 94
    • 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. Journal of Virology 2008, 82(8):4042-4051. 10.1128/JVI.02436-07.
    • (2008) Journal of Virology , vol.82 , Issue.8 , pp. 4042-4051
    • Granato, M.1    Feederle, R.2    Farina, A.3
  • 96
    • 0346373717 scopus 로고    scopus 로고
    • The pseudorabies virus US3 protein is a component of primary and of mature virions
    • Granzow H., Klupp B.G., Mettenleiter T.C. The pseudorabies virus US3 protein is a component of primary and of mature virions. Journal of Virology 2004, 78(3):1314-1323.
    • (2004) Journal of Virology , vol.78 , Issue.3 , pp. 1314-1323
    • Granzow, H.1    Klupp, B.G.2    Mettenleiter, T.C.3
  • 97
    • 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., Müller F.M., Fuchs W., Mettenleiter T.C. Analysis of viral and cellular factors influencing herpesvirus-induced nuclear envelope breakdown. Journal of Virology 2012, 86(12):6512-6521. 10.1128/JVI.00068-12.
    • (2012) Journal of Virology , vol.86 , Issue.12 , pp. 6512-6521
    • Grimm, K.S.1    Klupp, B.G.2    Granzow, H.3    Müller, F.M.4    Fuchs, W.5    Mettenleiter, T.C.6
  • 98
    • 79960631283 scopus 로고    scopus 로고
    • Nuclear export dynamics of RNA-protein complexes
    • Grünwald D., Singer R.H., Rout M. Nuclear export dynamics of RNA-protein complexes. Nature 2011, 475(7356):333-341. 10.1038/nature10318.
    • (2011) Nature , vol.475 , Issue.7356 , pp. 333-341
    • Grünwald, D.1    Singer, R.H.2    Rout, M.3
  • 99
    • 60749108426 scopus 로고    scopus 로고
    • Orchestrating nuclear envelope disassembly and reassembly during mitosis
    • Güttinger S., Laurell E., Kutay U. Orchestrating nuclear envelope disassembly and reassembly during mitosis. Nature Reviews. Molecular Cell Biology 2009, 10(3):178-191. 10.1038/nrm2641.
    • (2009) Nature Reviews. Molecular Cell Biology , vol.10 , Issue.3 , pp. 178-191
    • Güttinger, S.1    Laurell, E.2    Kutay, U.3
  • 100
    • 80052230265 scopus 로고    scopus 로고
    • Ran-dependent nuclear export mediators: A structural perspective
    • Güttler T., Görlich D. Ran-dependent nuclear export mediators: A structural perspective. The EMBO Journal 2011, 30(17):3457-3474. 10.1038/emboj.2011.287.
    • (2011) The EMBO Journal , vol.30 , Issue.17 , pp. 3457-3474
    • Güttler, T.1    Görlich, D.2
  • 101
    • 37349112878 scopus 로고
    • Nuclear extrusion and intracisternal inclusions in the rabbit blastocyst
    • Hadek R., Swift H. Nuclear extrusion and intracisternal inclusions in the rabbit blastocyst. The Journal of Cell Biology 1962, 13:445-451.
    • (1962) The Journal of Cell Biology , vol.13 , pp. 445-451
    • Hadek, R.1    Swift, H.2
  • 102
    • 84950262686 scopus 로고    scopus 로고
    • Structural basis of vesicle formation at the inner nuclear membrane
    • Hagen C., Dent K.C., Zeev-Ben-Mordehai T., et al. Structural basis of vesicle formation at the inner nuclear membrane. Cell 2015, 163:1692-1701.
    • (2015) Cell , vol.163 , pp. 1692-1701
    • Hagen, C.1    Dent, K.C.2    Zeev-Ben-Mordehai, T.3
  • 103
    • 84903174021 scopus 로고    scopus 로고
    • Multimodal nanoparticles as alignment and correlation markers in fluorescence/soft X-ray cryo-microscopy/tomography of nucleoplasmic reticulum and apoptosis in mammalian cells
    • Hagen C., Werner S., Carregal-Romero S., et al. Multimodal nanoparticles as alignment and correlation markers in fluorescence/soft X-ray cryo-microscopy/tomography of nucleoplasmic reticulum and apoptosis in mammalian cells. Ultramicroscopy 2014, 146:46-54. 10.1016/j.ultramic.2014.05.009.
    • (2014) Ultramicroscopy , vol.146 , pp. 46-54
    • Hagen, C.1    Werner, S.2    Carregal-Romero, S.3
  • 104
    • 59249092261 scopus 로고    scopus 로고
    • Viral mimicry of Cdc2/cyclin-dependent kinase 1 mediates disruption of nuclear lamina during human cytomegalovirus nuclear egress
    • Hamirally S., Kamil J.P., Ndassa-Colday Y.M., et al. Viral mimicry of Cdc2/cyclin-dependent kinase 1 mediates disruption of nuclear lamina during human cytomegalovirus nuclear egress. PLoS Pathogen 2009, 5(1):e1000275. 10.1371/journal.ppat.1000275.
    • (2009) PLoS Pathogen , vol.5 , Issue.1
    • Hamirally, S.1    Kamil, J.P.2    Ndassa-Colday, Y.M.3
  • 105
    • 33646555082 scopus 로고    scopus 로고
    • SUN1 interacts with nuclear lamin A and cytoplasmic nesprins to provide a physical connection between the nuclear lamina and the cytoskeleton
    • Haque F., Lloyd D.J., Smallwood D.T., et al. SUN1 interacts with nuclear lamin A and cytoplasmic nesprins to provide a physical connection between the nuclear lamina and the cytoskeleton. Molecular and Cellular Biology 2006, 26(10):3738-3751. 10.1128/MCB.26.10.3738-3751.2006.
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.10 , pp. 3738-3751
    • Haque, F.1    Lloyd, D.J.2    Smallwood, D.T.3
  • 106
    • 79960432712 scopus 로고    scopus 로고
    • Herpes simplex virus 1 pUL34 plays a critical role in cell-to-cell spread of virus in addition to its role in virus replication
    • Haugo A.C., Szpara M.L., Parsons L., Enquist L.W., Roller R.J. Herpes simplex virus 1 pUL34 plays a critical role in cell-to-cell spread of virus in addition to its role in virus replication. Journal of Virology 2011, 85(14):7203-7215. 10.1128/JVI.00262-11.
    • (2011) Journal of Virology , vol.85 , Issue.14 , pp. 7203-7215
    • Haugo, A.C.1    Szpara, M.L.2    Parsons, L.3    Enquist, L.W.4    Roller, R.J.5
  • 107
    • 0025352896 scopus 로고
    • Mutations of phosphorylation sites in lamin A that prevent nuclear lamina disassembly in mitosis
    • Heald R., McKeon F. Mutations of phosphorylation sites in lamin A that prevent nuclear lamina disassembly in mitosis. Cell 1990, 61(4):579-589.
    • (1990) Cell , vol.61 , Issue.4 , pp. 579-589
    • Heald, R.1    McKeon, F.2
  • 108
    • 84876339135 scopus 로고    scopus 로고
    • Analysis of the early steps of herpes simplex virus 1 capsid tegumentation
    • Henaff D., Remillard-Labrosse G., Loret S., Lippe R. Analysis of the early steps of herpes simplex virus 1 capsid tegumentation. Journal of Virology 2013, 87(9):4895-4906. 10.1128/JVI.03292-12.
    • (2013) Journal of Virology , vol.87 , Issue.9 , pp. 4895-4906
    • Henaff, D.1    Remillard-Labrosse, G.2    Loret, S.3    Lippe, R.4
  • 109
    • 17844402668 scopus 로고    scopus 로고
    • Bacteriophage HK97: Assembly of the capsid and evolutionary connections
    • Hendrix R.W. Bacteriophage HK97: Assembly of the capsid and evolutionary connections. Advances in Virus Research 2005, 64:1-14. 10.1016/S0065-3527(05)64001-8.
    • (2005) Advances in Virus Research , vol.64 , pp. 1-14
    • Hendrix, R.W.1
  • 111
    • 33846597192 scopus 로고    scopus 로고
    • Viral and cell cycle-regulated kinases in cytomegalovirus-induced pseudomitosis and replication
    • Hertel L., Chou S., Mocarski E.S. Viral and cell cycle-regulated kinases in cytomegalovirus-induced pseudomitosis and replication. PLoS Pathogen 2007, 3(1):e6. 10.1371/journal.ppat.0030006.
    • (2007) PLoS Pathogen , vol.3 , Issue.1
    • Hertel, L.1    Chou, S.2    Mocarski, E.S.3
  • 112
    • 6344270058 scopus 로고    scopus 로고
    • Global analysis of host cell gene expression late during cytomegalovirus infection reveals extensive dysregulation of cell cycle gene expression and induction of Pseudomitosis independent of US28 function
    • Hertel L., Mocarski E.S. Global analysis of host cell gene expression late during cytomegalovirus infection reveals extensive dysregulation of cell cycle gene expression and induction of Pseudomitosis independent of US28 function. Journal of Virology 2004, 78(21):11988-12011. 10.1128/JVI.78.21.11988-12011.2004.
    • (2004) Journal of Virology , vol.78 , Issue.21 , pp. 11988-12011
    • Hertel, L.1    Mocarski, E.S.2
  • 114
    • 84937685221 scopus 로고    scopus 로고
    • Herpes simplex virus 1 recruits CD98 heavy chain and beta1 integrin to the nuclear membrane for viral de-envelopment
    • Hirohata Y., Arii J., Liu Z., et al. Herpes simplex virus 1 recruits CD98 heavy chain and beta1 integrin to the nuclear membrane for viral de-envelopment. Journal of Virology 2015, 89(15):7799-7812. 10.1128/JVI.00741-15.
    • (2015) Journal of Virology , vol.89 , Issue.15 , pp. 7799-7812
    • Hirohata, Y.1    Arii, J.2    Liu, Z.3
  • 115
    • 50149097733 scopus 로고    scopus 로고
    • Nuclear pore composition and gating in herpes simplex virus-infected cells
    • Hofemeister H., O'Hare P. Nuclear pore composition and gating in herpes simplex virus-infected cells. Journal of Virology 2008, 82(17):8392-8399. 10.1128/JVI.00951-08.
    • (2008) Journal of Virology , vol.82 , Issue.17 , pp. 8392-8399
    • Hofemeister, H.1    O'Hare, P.2
  • 116
    • 34547642520 scopus 로고    scopus 로고
    • An emerin "proteome": Purification of distinct emerin-containing complexes from HeLa cells suggests molecular basis for diverse roles including gene regulation, mRNA splicing, signaling, mechanosensing, and nuclear architecture
    • Holaska J.M., Wilson K.L. An emerin "proteome": Purification of distinct emerin-containing complexes from HeLa cells suggests molecular basis for diverse roles including gene regulation, mRNA splicing, signaling, mechanosensing, and nuclear architecture. Biochemistry 2007, 46(30):8897-8908. 10.1021/bi602636m.
    • (2007) Biochemistry , vol.46 , Issue.30 , pp. 8897-8908
    • Holaska, J.M.1    Wilson, K.L.2
  • 117
    • 0035197416 scopus 로고    scopus 로고
    • Inner nuclear membrane proteins: Functions and targeting
    • Holmer L., Worman H.J. Inner nuclear membrane proteins: Functions and targeting. Cellular and Molecular Life Sciences 2001, 58(12-13):1741-1747.
    • (2001) Cellular and Molecular Life Sciences , vol.58 , Issue.12-13 , pp. 1741-1747
    • Holmer, L.1    Worman, H.J.2
  • 118
    • 84883272572 scopus 로고    scopus 로고
    • Structure of the pseudorabies virus capsid: Comparison with herpes simplex virus type 1 and differential binding of essential minor proteins
    • Homa F.L., Huffman J.B., Toropova K., Lopez H.R., Makhov A.M., Conway J.F. Structure of the pseudorabies virus capsid: Comparison with herpes simplex virus type 1 and differential binding of essential minor proteins. Journal of Molecular Biology 2013, 425(18):3415-3428. 10.1016/j.jmb.2013.06.034.
    • (2013) Journal of Molecular Biology , vol.425 , Issue.18 , pp. 3415-3428
    • Homa, F.L.1    Huffman, J.B.2    Toropova, K.3    Lopez, H.R.4    Makhov, A.M.5    Conway, J.F.6
  • 119
    • 45749157594 scopus 로고    scopus 로고
    • Amino acids 143 to 150 of the herpes simplex virus type 1 scaffold protein are required for the formation of portal-containing capsids
    • Huffman J.B., Newcomb W.W., Brown J.C., Homa F.L. Amino acids 143 to 150 of the herpes simplex virus type 1 scaffold protein are required for the formation of portal-containing capsids. Journal of Virology 2008, 82(13):6778-6781. 10.1128/JVI.00473-08.
    • (2008) Journal of Virology , vol.82 , Issue.13 , pp. 6778-6781
    • Huffman, J.B.1    Newcomb, W.W.2    Brown, J.C.3    Homa, F.L.4
  • 120
    • 44049107548 scopus 로고    scopus 로고
    • Phosphorylation of retinoblastoma protein by viral protein with cyclin-dependent kinase function
    • Hume A.J., Finkel J.S., Kamil J.P., Coen D.M., Culbertson M.R., Kalejta R.F. Phosphorylation of retinoblastoma protein by viral protein with cyclin-dependent kinase function. Science 2008, 320(5877):797-799. 10.1126/science.1152095.
    • (2008) Science , vol.320 , Issue.5877 , pp. 797-799
    • Hume, A.J.1    Finkel, J.S.2    Kamil, J.P.3    Coen, D.M.4    Culbertson, M.R.5    Kalejta, R.F.6
  • 121
    • 0009998217 scopus 로고
    • Movement and intracellular location of sonchus yellow net virus within infected Nicotiana edwardsonii
    • Ismail I.D., Hamilton I.D., Robertson E., Milner J.J. Movement and intracellular location of sonchus yellow net virus within infected Nicotiana edwardsonii. The Journal of General Virology 1987, 68:2429-2438.
    • (1987) The Journal of General Virology , vol.68 , pp. 2429-2438
    • Ismail, I.D.1    Hamilton, I.D.2    Robertson, E.3    Milner, J.J.4
  • 122
    • 0031940067 scopus 로고    scopus 로고
    • Herpes simplex virus type 1-infected human embryonic lung cells studied by optimized immunogold cryosection electron microscopy
    • Jensen H.L., Norrild B. Herpes simplex virus type 1-infected human embryonic lung cells studied by optimized immunogold cryosection electron microscopy. The Journal of Histochemistry and Cytochemistry 1998, 46(4):487-496.
    • (1998) The Journal of Histochemistry and Cytochemistry , vol.46 , Issue.4 , pp. 487-496
    • Jensen, H.L.1    Norrild, B.2
  • 123
    • 79954599465 scopus 로고    scopus 로고
    • Herpesviruses remodel host membranes for virus egress
    • Johnson D.C., Baines J.D. Herpesviruses remodel host membranes for virus egress. Nature Reviews Microbiology 2011, 9(5):382-394. 10.1038/nrmicro2559.
    • (2011) Nature Reviews Microbiology , vol.9 , Issue.5 , pp. 382-394
    • Johnson, D.C.1    Baines, J.D.2
  • 124
    • 0019918329 scopus 로고
    • Monensin inhibits the processing of herpes simplex virus glycoproteins, their transport to the cell surface, and the egress of virions from infected cells
    • Johnson D.C., Spear P.G. Monensin inhibits the processing of herpes simplex virus glycoproteins, their transport to the cell surface, and the egress of virions from infected cells. Journal of Virology 1982, 43(3):1102-1112.
    • (1982) Journal of Virology , vol.43 , Issue.3 , pp. 1102-1112
    • Johnson, D.C.1    Spear, P.G.2
  • 125
    • 84876955658 scopus 로고    scopus 로고
    • Torsin mediates primary envelopment of large ribonucleoprotein granules at the nuclear envelope
    • Jokhi V., Ashley J., Nunnari J., et al. Torsin mediates primary envelopment of large ribonucleoprotein granules at the nuclear envelope. Cell Reports 2013, 3(4):988-995. 10.1016/j.celrep.2013.03.015.
    • (2013) Cell Reports , vol.3 , Issue.4 , pp. 988-995
    • Jokhi, V.1    Ashley, J.2    Nunnari, J.3
  • 126
    • 77950528101 scopus 로고    scopus 로고
    • Relative tissue expression of homologous torsinB correlates with the neuronal specific importance of DYT1 dystonia-associated torsinA
    • Jungwirth M., Dear M.L., Brown P., Holbrook K., Goodchild R. Relative tissue expression of homologous torsinB correlates with the neuronal specific importance of DYT1 dystonia-associated torsinA. Human Molecular Genetics 2010, 19(5):888-900. 10.1093/hmg/ddp557.
    • (2010) Human Molecular Genetics , vol.19 , Issue.5 , pp. 888-900
    • Jungwirth, M.1    Dear, M.L.2    Brown, P.3    Holbrook, K.4    Goodchild, R.5
  • 127
    • 27744458480 scopus 로고    scopus 로고
    • Cell cycle sibling rivalry: Cdc2 vs. Cdk2
    • Kaldis P., Aleem E. Cell cycle sibling rivalry: Cdc2 vs. Cdk2. Cell Cycle 2005, 4(11):1491-1494.
    • (2005) Cell Cycle , vol.4 , Issue.11 , pp. 1491-1494
    • Kaldis, P.1    Aleem, E.2
  • 128
    • 58149382622 scopus 로고    scopus 로고
    • Herpes simplex virus 1 protein kinase Us3 phosphorylates viral envelope glycoprotein B and regulates its expression on the cell surface
    • Kato A., Arii J., Shiratori I., Akashi H., Arase H., Kawaguchi Y. Herpes simplex virus 1 protein kinase Us3 phosphorylates viral envelope glycoprotein B and regulates its expression on the cell surface. Journal of Virology 2009, 83(1):250-261. 10.1128/JVI.01451-08.
    • (2009) Journal of Virology , vol.83 , Issue.1 , pp. 250-261
    • Kato, A.1    Arii, J.2    Shiratori, I.3    Akashi, H.4    Arase, H.5    Kawaguchi, Y.6
  • 129
    • 80052461746 scopus 로고    scopus 로고
    • Herpes simplex virus 1 protein kinase Us3 and major tegument protein UL47 reciprocally regulate their subcellular localization in infected cells
    • Kato A., Liu Z., Minowa A., et al. Herpes simplex virus 1 protein kinase Us3 and major tegument protein UL47 reciprocally regulate their subcellular localization in infected cells. Journal of Virology 2011, 85(18):9599-9613. 10.1128/JVI.00845-11.
    • (2011) Journal of Virology , vol.85 , Issue.18 , pp. 9599-9613
    • Kato, A.1    Liu, Z.2    Minowa, A.3
  • 130
    • 21444459417 scopus 로고    scopus 로고
    • Identification of proteins phosphorylated directly by the Us3 protein kinase encoded by herpes simplex virus 1
    • Kato A., Yamamoto M., Ohno T., Kodaira H., Nishiyama Y., Kawaguchi Y. Identification of proteins phosphorylated directly by the Us3 protein kinase encoded by herpes simplex virus 1. Journal of Virology 2005, 79(14):9325-9331. 10.1128/JVI.79.14.9325-9331.2005.
    • (2005) Journal of Virology , vol.79 , Issue.14 , pp. 9325-9331
    • Kato, A.1    Yamamoto, M.2    Ohno, T.3    Kodaira, H.4    Nishiyama, Y.5    Kawaguchi, Y.6
  • 132
    • 0041837470 scopus 로고    scopus 로고
    • Protein kinases conserved in herpesviruses potentially share a function mimicking the cellular protein kinase cdc2
    • Kawaguchi Y., Kato K. Protein kinases conserved in herpesviruses potentially share a function mimicking the cellular protein kinase cdc2. Reviews in Medical Virology 2003, 13(5):331-340. 10.1002/rmv.402.
    • (2003) Reviews in Medical Virology , vol.13 , Issue.5 , pp. 331-340
    • Kawaguchi, Y.1    Kato, K.2
  • 133
    • 84863507534 scopus 로고    scopus 로고
    • Geneious basic: An integrated and extendable desktop software platform for the organization and analysis of sequence data
    • Kearse M., Moir R., Wilson A., et al. Geneious basic: An integrated and extendable desktop software platform for the organization and analysis of sequence data. Bioinformatics 2012, 28(12):1647-1649. 10.1093/bioinformatics/bts199.
    • (2012) Bioinformatics , vol.28 , Issue.12 , pp. 1647-1649
    • Kearse, M.1    Moir, R.2    Wilson, A.3
  • 134
    • 45749112586 scopus 로고    scopus 로고
    • Glycoproteins required for entry are not necessary for egress of pseudorabies virus
    • Klupp B.G., Altenschmidt J., Granzow H., Fuchs W., Mettenleiter T.C. Glycoproteins required for entry are not necessary for egress of pseudorabies virus. Journal of Virology 2008, 82(13):6299-6309. 10.1128/JVI.00386-08.
    • (2008) Journal of Virology , vol.82 , Issue.13 , pp. 6299-6309
    • Klupp, B.G.1    Altenschmidt, J.2    Granzow, H.3    Fuchs, W.4    Mettenleiter, T.C.5
  • 136
    • 27144531191 scopus 로고    scopus 로고
    • Identification, subviral localization, and functional characterization of the pseudorabies virus UL17 protein
    • Klupp B.G., Granzow H., Karger A., Mettenleiter T.C. Identification, subviral localization, and functional characterization of the pseudorabies virus UL17 protein. Journal of Virology 2005, 79(21):13442-13453. 10.1128/JVI.79.21.13442-13453.2005.
    • (2005) Journal of Virology , vol.79 , Issue.21 , pp. 13442-13453
    • Klupp, B.G.1    Granzow, H.2    Karger, A.3    Mettenleiter, T.C.4
  • 137
    • 33745245616 scopus 로고    scopus 로고
    • The capsid-associated UL25 protein of the alphaherpesvirus pseudorabies virus is nonessential for cleavage and encapsidation of genomic DNA but is required for nuclear egress of capsids
    • Klupp B.G., Granzow H., Keil G.M., Mettenleiter T.C. The capsid-associated UL25 protein of the alphaherpesvirus pseudorabies virus is nonessential for cleavage and encapsidation of genomic DNA but is required for nuclear egress of capsids. Journal of Virology 2006, 80(13):6235-6246. 10.1128/JVI.02662-05.
    • (2006) Journal of Virology , vol.80 , Issue.13 , pp. 6235-6246
    • Klupp, B.G.1    Granzow, H.2    Keil, G.M.3    Mettenleiter, T.C.4
  • 138
    • 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. Journal of Virology 2000, 74(21):10063-10073.
    • (2000) Journal of Virology , vol.74 , Issue.21 , pp. 10063-10073
    • Klupp, B.G.1    Granzow, H.2    Mettenleiter, T.C.3
  • 139
    • 0034784870 scopus 로고    scopus 로고
    • Effect of the pseudorabies virus US3 protein on nuclear membrane localization of the UL34 protein and virus egress from the nucleus
    • Klupp B.G., Granzow H., Mettenleiter T.C. Effect of the pseudorabies virus US3 protein on nuclear membrane localization of the UL34 protein and virus egress from the nucleus. The Journal of General Virology 2001, 82(Pt. 10):2363-2371.
    • (2001) The Journal of General Virology , vol.82 , pp. 2363-2371
    • Klupp, B.G.1    Granzow, H.2    Mettenleiter, T.C.3
  • 140
    • 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. Journal of Virology 2011, 85(16):8285-8292. 10.1128/JVI.00741-11.
    • (2011) Journal of Virology , vol.85 , Issue.16 , pp. 8285-8292
    • Klupp, B.G.1    Granzow, H.2    Mettenleiter, T.C.3
  • 141
    • 0034849764 scopus 로고    scopus 로고
    • Pseudorabies virus UL37 gene product is involved in secondary envelopment
    • Klupp B.G., Granzow H., Mundt E., Mettenleiter T.C. Pseudorabies virus UL37 gene product is involved in secondary envelopment. Journal of Virology 2001, 75(19):8927-8936. 10.1128/JVI.75.19.8927-8936.2001.
    • (2001) Journal of Virology , vol.75 , Issue.19 , pp. 8927-8936
    • Klupp, B.G.1    Granzow, H.2    Mundt, E.3    Mettenleiter, T.C.4
  • 143
    • 0016872066 scopus 로고
    • Replication of nuclear polyhedrosis virus in a continuous cell culture of Spodoptera frugiperda: Microscopy study of the sequence of events of the virus infection
    • Knudson D.L., Harrap K.A. Replication of nuclear polyhedrosis virus in a continuous cell culture of Spodoptera frugiperda: Microscopy study of the sequence of events of the virus infection. Journal of Virology 1975, 17(1):254-268.
    • (1975) Journal of Virology , vol.17 , Issue.1 , pp. 254-268
    • Knudson, D.L.1    Harrap, K.A.2
  • 144
    • 0344080584 scopus 로고    scopus 로고
    • The pseudorabies virus UL11 protein is a virion component involved in secondary envelopment in the cytoplasm
    • Kopp M., Granzow H., Fuchs W., et al. The pseudorabies virus UL11 protein is a virion component involved in secondary envelopment in the cytoplasm. Journal of Virology 2003, 77(9):5339-5351.
    • (2003) Journal of Virology , vol.77 , Issue.9 , pp. 5339-5351
    • Kopp, M.1    Granzow, H.2    Fuchs, W.3
  • 145
    • 0036337330 scopus 로고    scopus 로고
    • Identification and characterization of the pseudorabies virus tegument proteins UL46 and UL47: Role for UL47 in virion morphogenesis in the cytoplasm
    • Kopp M., Klupp B.G., Granzow H., Fuchs W., Mettenleiter T.C. Identification and characterization of the pseudorabies virus tegument proteins UL46 and UL47: Role for UL47 in virion morphogenesis in the cytoplasm. Journal of Virology 2002, 76(17):8820-8833.
    • (2002) Journal of Virology , vol.76 , Issue.17 , pp. 8820-8833
    • Kopp, M.1    Klupp, B.G.2    Granzow, H.3    Fuchs, W.4    Mettenleiter, T.C.5
  • 146
    • 84872483388 scopus 로고    scopus 로고
    • The nuclear envelope proteome differs notably between tissues
    • Korfali N., Wilkie G.S., Swanson S.K., et al. The nuclear envelope proteome differs notably between tissues. Nucleus 2012, 3(6):552-564. 10.4161/nucl.22257.
    • (2012) Nucleus , vol.3 , Issue.6 , pp. 552-564
    • Korfali, N.1    Wilkie, G.S.2    Swanson, S.K.3
  • 147
    • 0032949986 scopus 로고    scopus 로고
    • Physical and functional interactions between the herpes simplex virus UL15 and UL28 DNA cleavage and packaging proteins
    • Koslowski K.M., Shaver P.R., Casey J.T., et al. Physical and functional interactions between the herpes simplex virus UL15 and UL28 DNA cleavage and packaging proteins. Journal of Virology 1999, 73(2):1704-1707.
    • (1999) Journal of Virology , vol.73 , Issue.2 , pp. 1704-1707
    • Koslowski, K.M.1    Shaver, P.R.2    Casey, J.T.3
  • 148
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • Krogh A., Larsson B., von Heijne G., Sonnhammer E.L. Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes. Journal of Molecular Biology 2001, 305(3):567-580. 10.1006/jmbi.2000.4315.
    • (2001) Journal of Molecular Biology , vol.305 , Issue.3 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    von Heijne, G.3    Sonnhammer, E.L.4
  • 149
    • 0037225808 scopus 로고    scopus 로고
    • The human cytomegalovirus UL97 protein kinase, an antiviral drug target, is required at the stage of nuclear egress
    • Krosky P.M., Baek M.C., Coen D.M. The human cytomegalovirus UL97 protein kinase, an antiviral drug target, is required at the stage of nuclear egress. Journal of Virology 2003, 77(2):905-914.
    • (2003) Journal of Virology , vol.77 , Issue.2 , pp. 905-914
    • Krosky, P.M.1    Baek, M.C.2    Coen, D.M.3
  • 150
    • 44949180011 scopus 로고    scopus 로고
    • Partial functional complementation of a pseudorabies virus UL25 deletion mutant by herpes simplex virus type 1 pUL25 indicates overlapping functions of alphaherpesvirus pUL25 proteins
    • Kuhn J., Leege T., Klupp B.G., Granzow H., Fuchs W., Mettenleiter T.C. Partial functional complementation of a pseudorabies virus UL25 deletion mutant by herpes simplex virus type 1 pUL25 indicates overlapping functions of alphaherpesvirus pUL25 proteins. Journal of Virology 2008, 82(12):5725-5734. 10.1128/JVI.02441-07.
    • (2008) Journal of Virology , vol.82 , Issue.12 , pp. 5725-5734
    • Kuhn, J.1    Leege, T.2    Klupp, B.G.3    Granzow, H.4    Fuchs, W.5    Mettenleiter, T.C.6
  • 151
    • 78149328426 scopus 로고    scopus 로고
    • Cyclin-dependent kinase-like function is shared by the beta- and gamma- subset of the conserved herpesvirus protein kinases
    • Kuny C.V., Chinchilla K., Culbertson M.R., Kalejta R.F. Cyclin-dependent kinase-like function is shared by the beta- and gamma- subset of the conserved herpesvirus protein kinases. PLoS Pathogen 2010, 6(9):e1001092. 10.1371/journal.ppat.1001092.
    • (2010) PLoS Pathogen , vol.6 , Issue.9
    • Kuny, C.V.1    Chinchilla, K.2    Culbertson, M.R.3    Kalejta, R.F.4
  • 152
    • 56949083763 scopus 로고    scopus 로고
    • Reorganization of the nuclear envelope during open mitosis
    • Kutay U., Hetzer M.W. Reorganization of the nuclear envelope during open mitosis. Current Opinion in Cell Biology 2008, 20(6):669-677. 10.1016/j.ceb.2008.09.010.
    • (2008) Current Opinion in Cell Biology , vol.20 , Issue.6 , pp. 669-677
    • Kutay, U.1    Hetzer, M.W.2
  • 153
    • 0034984585 scopus 로고    scopus 로고
    • Structural characterization of the LEM motif common to three human inner nuclear membrane proteins
    • Laguri C., Gilquin B., Wolff N., et al. Structural characterization of the LEM motif common to three human inner nuclear membrane proteins. Structure 2001, 9(6):503-511.
    • (2001) Structure , vol.9 , Issue.6 , pp. 503-511
    • Laguri, C.1    Gilquin, B.2    Wolff, N.3
  • 154
    • 0031952179 scopus 로고    scopus 로고
    • The herpes simplex virus type 1 cleavage/packaging protein, UL32, is involved in efficient localization of capsids to replication compartments
    • Lamberti C., Weller S.K. The herpes simplex virus type 1 cleavage/packaging protein, UL32, is involved in efficient localization of capsids to replication compartments. Journal of Virology 1998, 72(3):2463-2473.
    • (1998) Journal of Virology , vol.72 , Issue.3 , pp. 2463-2473
    • Lamberti, C.1    Weller, S.K.2
  • 155
    • 66849126974 scopus 로고    scopus 로고
    • Nuclear envelope formation: Mind the gaps
    • Larijani B., Poccia D.L. Nuclear envelope formation: Mind the gaps. Annual Review of Biophysics 2009, 38:107-124. 10.1146/annurev.biophys.050708.133625.
    • (2009) Annual Review of Biophysics , vol.38 , pp. 107-124
    • Larijani, B.1    Poccia, D.L.2
  • 156
    • 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. Journal of Virology 2007, 81(19):10792-10803. 10.1128/JVI.00196-07.
    • (2007) Journal of Virology , vol.81 , Issue.19 , pp. 10792-10803
    • Leach, N.1    Bjerke, S.L.2    Christensen, D.K.3
  • 157
    • 77956186490 scopus 로고    scopus 로고
    • Significance of host cell kinases in herpes simplex virus type 1 egress and lamin-associated protein disassembly from the nuclear lamina
    • Leach N.R., Roller R.J. Significance of host cell kinases in herpes simplex virus type 1 egress and lamin-associated protein disassembly from the nuclear lamina. Virology 2010, 406(1):127-137. 10.1016/j.virol.2010.07.002.
    • (2010) Virology , vol.406 , Issue.1 , pp. 127-137
    • Leach, N.R.1    Roller, R.J.2
  • 159
    • 56449106108 scopus 로고    scopus 로고
    • Epstein-Barr virus BGLF4 kinase induces disassembly of the nuclear lamina to facilitate virion production
    • Lee C.P., Huang Y.H., Lin S.F., et al. Epstein-Barr virus BGLF4 kinase induces disassembly of the nuclear lamina to facilitate virion production. Journal of Virology 2008, 82(23):11913-11926. 10.1128/JVI.01100-08.
    • (2008) Journal of Virology , vol.82 , Issue.23 , pp. 11913-11926
    • Lee, C.P.1    Huang, Y.H.2    Lin, S.F.3
  • 160
    • 84866920100 scopus 로고    scopus 로고
    • The ESCRT machinery is recruited by the viral BFRF1 protein to the nucleus-associated membrane for the maturation of Epstein-Barr virus
    • Lee C.P., Liu P.T., Kung H.N., et al. The ESCRT machinery is recruited by the viral BFRF1 protein to the nucleus-associated membrane for the maturation of Epstein-Barr virus. PLoS Pathogen 2012, 8(9):e1002904. 10.1371/journal.ppat.1002904.
    • (2012) PLoS Pathogen , vol.8 , Issue.9
    • Lee, C.P.1    Liu, P.T.2    Kung, H.N.3
  • 161
    • 33845421600 scopus 로고    scopus 로고
    • Identification of an essential domain in the herpesvirus VP1/2 tegument protein: The carboxy terminus directs incorporation into capsid assemblons
    • Lee J.I., Luxton G.W., Smith G.A. Identification of an essential domain in the herpesvirus VP1/2 tegument protein: The carboxy terminus directs incorporation into capsid assemblons. Journal of Virology 2006, 80(24):12086-12094. 10.1128/JVI.01184-06.
    • (2006) Journal of Virology , vol.80 , Issue.24 , pp. 12086-12094
    • Lee, J.I.1    Luxton, G.W.2    Smith, G.A.3
  • 162
    • 80655143483 scopus 로고    scopus 로고
    • A physical link between the pseudorabies virus capsid and the nuclear egress complex
    • Leelawong M., Guo D., Smith G.A. A physical link between the pseudorabies virus capsid and the nuclear egress complex. Journal of Virology 2011, 85(22):11675-11684. 10.1128/JVI.05614-11.
    • (2011) Journal of Virology , vol.85 , Issue.22 , pp. 11675-11684
    • Leelawong, M.1    Guo, D.2    Smith, G.A.3
  • 163
    • 84937459160 scopus 로고    scopus 로고
    • Structure of a herpesvirus nuclear egress complex subunit reveals an interaction groove that is essential for viral replication
    • Leigh K.E., Sharma M., Mansueto M.S., et al. Structure of a herpesvirus nuclear egress complex subunit reveals an interaction groove that is essential for viral replication. Proceedings of the National Academy of Sciences of the United States of America 2015, 112(29):9010-9015. 10.1073/pnas.1511140112.
    • (2015) Proceedings of the National Academy of Sciences of the United States of America , vol.112 , Issue.29 , pp. 9010-9015
    • Leigh, K.E.1    Sharma, M.2    Mansueto, M.S.3
  • 164
    • 0344835675 scopus 로고    scopus 로고
    • Nuclear envelope breakdown in starfish oocytes proceeds by partial NPC disassembly followed by a rapidly spreading fenestration of nuclear membranes
    • Lenart P., Rabut G., Daigle N., Hand A.R., Terasaki M., Ellenberg J. Nuclear envelope breakdown in starfish oocytes proceeds by partial NPC disassembly followed by a rapidly spreading fenestration of nuclear membranes. The Journal of Cell Biology 2003, 160(7):1055-1068. 10.1083/jcb.200211076.
    • (2003) The Journal of Cell Biology , vol.160 , Issue.7 , pp. 1055-1068
    • Lenart, P.1    Rabut, G.2    Daigle, N.3    Hand, A.R.4    Terasaki, M.5    Ellenberg, J.6
  • 165
    • 26444574766 scopus 로고    scopus 로고
    • Herpes simplex virus 1 envelopment follows two diverse pathways
    • Leuzinger H., Ziegler U., Schraner E.M., et al. Herpes simplex virus 1 envelopment follows two diverse pathways. Journal of Virology 2005, 79(20):13047-13059. 10.1128/JVI.79.20.13047-13059.2005.
    • (2005) Journal of Virology , vol.79 , Issue.20 , pp. 13047-13059
    • Leuzinger, H.1    Ziegler, U.2    Schraner, E.M.3
  • 166
    • 14744280502 scopus 로고    scopus 로고
    • Identification of an essential domain in the herpes simplex virus 1 UL34 protein that is necessary and sufficient to interact with UL31 protein
    • Liang L., Baines J.D. Identification of an essential domain in the herpes simplex virus 1 UL34 protein that is necessary and sufficient to interact with UL31 protein. Journal of Virology 2005, 79(6):3797-3806. 10.1128/JVI.79.6.3797-3806.2005.
    • (2005) Journal of Virology , vol.79 , Issue.6 , pp. 3797-3806
    • Liang, L.1    Baines, J.D.2
  • 167
    • 0034681345 scopus 로고    scopus 로고
    • MAN1, an inner nuclear membrane protein that shares the LEM domain with lamina-associated polypeptide 2 and emerin
    • Lin F., Blake D.L., Callebaut I., et al. MAN1, an inner nuclear membrane protein that shares the LEM domain with lamina-associated polypeptide 2 and emerin. The Journal of Biological Chemistry 2000, 275(7):4840-4847.
    • (2000) The Journal of Biological Chemistry , vol.275 , Issue.7 , pp. 4840-4847
    • Lin, F.1    Blake, D.L.2    Callebaut, I.3
  • 168
    • 0030034034 scopus 로고    scopus 로고
    • Autoantibodies from patients with primary biliary cirrhosis recognize a region within the nucleoplasmic domain of inner nuclear membrane protein LBR
    • Lin F., Noyer C.M., Ye Q., Courvalin J.C., Worman H.J. Autoantibodies from patients with primary biliary cirrhosis recognize a region within the nucleoplasmic domain of inner nuclear membrane protein LBR. Hepatology 1996, 23(1):57-61. 10.1002/hep.510230109.
    • (1996) Hepatology , vol.23 , Issue.1 , pp. 57-61
    • Lin, F.1    Noyer, C.M.2    Ye, Q.3    Courvalin, J.C.4    Worman, H.J.5
  • 169
    • 84938939142 scopus 로고    scopus 로고
    • Role of host cell p32 in herpes simplex virus 1 de-envelopment during viral nuclear egress
    • Liu Z., Kato A., Oyama M., Kozuka-Hata H., Arii J., Kawaguchi Y. Role of host cell p32 in herpes simplex virus 1 de-envelopment during viral nuclear egress. Journal of Virology 2015, 89(17):8982-8998. 10.1128/JVI.01220-15.
    • (2015) Journal of Virology , vol.89 , Issue.17 , pp. 8982-8998
    • Liu, Z.1    Kato, A.2    Oyama, M.3    Kozuka-Hata, H.4    Arii, J.5    Kawaguchi, Y.6
  • 170
    • 84897525181 scopus 로고    scopus 로고
    • Herpes simplex virus 1 UL47 interacts with viral nuclear egress factors UL31, UL34, and Us3 and regulates viral nuclear egress
    • Liu Z., Kato A., Shindo K., et al. Herpes simplex virus 1 UL47 interacts with viral nuclear egress factors UL31, UL34, and Us3 and regulates viral nuclear egress. Journal of Virology 2014, 88(9):4657-4667. 10.1128/JVI.00137-14.
    • (2014) Journal of Virology , vol.88 , Issue.9 , pp. 4657-4667
    • Liu, Z.1    Kato, A.2    Shindo, K.3
  • 171
    • 84863241919 scopus 로고    scopus 로고
    • Varicella-Zoster virus ORF12 protein triggers phosphorylation of ERK1/2 and inhibits apoptosis
    • Liu X., Li Q., Dowdell K., Fischer E.R., Cohen J.I. Varicella-Zoster virus ORF12 protein triggers phosphorylation of ERK1/2 and inhibits apoptosis. Journal of Virology 2012, 86(6):3143-3151. 10.1128/JVI.06923-11.
    • (2012) Journal of Virology , vol.86 , Issue.6 , pp. 3143-3151
    • Liu, X.1    Li, Q.2    Dowdell, K.3    Fischer, E.R.4    Cohen, J.I.5
  • 172
    • 79960685238 scopus 로고    scopus 로고
    • The interaction between nesprins and sun proteins at the nuclear envelope is critical for force transmission between the nucleus and cytoskeleton
    • Lombardi M.L., Jaalouk D.E., Shanahan C.M., Burke B., Roux K.J., Lammerding J. The interaction between nesprins and sun proteins at the nuclear envelope is critical for force transmission between the nucleus and cytoskeleton. The Journal of Biological Chemistry 2011, 286(30):26743-26753. 10.1074/jbc.M111.233700.
    • (2011) The Journal of Biological Chemistry , vol.286 , Issue.30 , pp. 26743-26753
    • Lombardi, M.L.1    Jaalouk, D.E.2    Shanahan, C.M.3    Burke, B.4    Roux, K.J.5    Lammerding, J.6
  • 173
    • 84924871387 scopus 로고    scopus 로고
    • A single herpesvirus protein can mediate vesicle formation in the nuclear envelope
    • Lorenz M., Vollmer B., Unsay J.D., et al. A single herpesvirus protein can mediate vesicle formation in the nuclear envelope. The Journal of Biological Chemistry 2015, 290(11):6962-6974. 10.1074/jbc.M114.627521.
    • (2015) The Journal of Biological Chemistry , vol.290 , Issue.11 , pp. 6962-6974
    • Lorenz, M.1    Vollmer, B.2    Unsay, J.D.3
  • 174
    • 79960915158 scopus 로고    scopus 로고
    • The importin beta binding domain as a master regulator of nucleocytoplasmic transport
    • Lott K., Cingolani G. The importin beta binding domain as a master regulator of nucleocytoplasmic transport. Biochimica et Biophysica Acta 2011, 1813(9):1578-1592. 10.1016/j.bbamcr.2010.10.012.
    • (2011) Biochimica et Biophysica Acta , vol.1813 , Issue.9 , pp. 1578-1592
    • Lott, K.1    Cingolani, G.2
  • 175
    • 33645980333 scopus 로고    scopus 로고
    • Functional domains of murine cytomegalovirus nuclear egress protein M53/p38
    • Lötzerich M., Ruzsics Z., Koszinowski U.H. Functional domains of murine cytomegalovirus nuclear egress protein M53/p38. Journal of Virology 2006, 80(1):73-84. 10.1128/JVI.80.1.73-84.2006.
    • (2006) Journal of Virology , vol.80 , Issue.1 , pp. 73-84
    • Lötzerich, M.1    Ruzsics, Z.2    Koszinowski, U.H.3
  • 176
    • 84875489857 scopus 로고    scopus 로고
    • Interactions of the Kaposi's Sarcoma-associated herpesvirus nuclear egress complex: ORF69 is a potent factor for remodeling cellular membranes
    • Luitweiler E.M., Henson B.W., Pryce E.N., et al. Interactions of the Kaposi's Sarcoma-associated herpesvirus nuclear egress complex: ORF69 is a potent factor for remodeling cellular membranes. Journal of Virology 2013, 87(7):3915-3929. 10.1128/JVI.03418-12.
    • (2013) Journal of Virology , vol.87 , Issue.7 , pp. 3915-3929
    • Luitweiler, E.M.1    Henson, B.W.2    Pryce, E.N.3
  • 177
    • 84950277486 scopus 로고    scopus 로고
    • Unexpected features and mechanism of heterodimer formation of a herpesvirus nuclear egress complex
    • Lye M., Sharma M., El Omari K., et al. Unexpected features and mechanism of heterodimer formation of a herpesvirus nuclear egress complex. The EMBO Journal 2015, 10.15252/embj.201592651.
    • (2015) The EMBO Journal
    • Lye, M.1    Sharma, M.2    El Omari, K.3
  • 178
    • 79957856854 scopus 로고    scopus 로고
    • The nucleoplasmic reticulum: Form and function
    • Malhas A., Goulbourne C., Vaux D.J. The nucleoplasmic reticulum: Form and function. Trends in Cell Biology 2011, 21(6):362-373. 10.1016/j.tcb.2011.03.008.
    • (2011) Trends in Cell Biology , vol.21 , Issue.6 , pp. 362-373
    • Malhas, A.1    Goulbourne, C.2    Vaux, D.J.3
  • 179
    • 84908473540 scopus 로고    scopus 로고
    • Cyclin-dependent kinases
    • Malumbres M. Cyclin-dependent kinases. Genome Biology 2014, 15(6):122.
    • (2014) Genome Biology , vol.15 , Issue.6 , pp. 122
    • Malumbres, M.1
  • 180
    • 17144380019 scopus 로고    scopus 로고
    • Direct binding of nuclear membrane protein MAN1 to emerin in vitro and two modes of binding to barrier-to-autointegration factor
    • Mansharamani M., Wilson K.L. Direct binding of nuclear membrane protein MAN1 to emerin in vitro and two modes of binding to barrier-to-autointegration factor. The Journal of Biological Chemistry 2005, 280(14):13863-13870. 10.1074/jbc.M413020200.
    • (2005) The Journal of Biological Chemistry , vol.280 , Issue.14 , pp. 13863-13870
    • Mansharamani, M.1    Wilson, K.L.2
  • 181
    • 79960928189 scopus 로고    scopus 로고
    • Molecular basis for specificity of nuclear import and prediction of nuclear localization
    • Marfori M., Mynott A., Ellis J.J., et al. Molecular basis for specificity of nuclear import and prediction of nuclear localization. Biochimica et Biophysica Acta 2011, 1813(9):1562-1577. 10.1016/j.bbamcr.2010.10.013.
    • (2011) Biochimica et Biophysica Acta , vol.1813 , Issue.9 , pp. 1562-1577
    • Marfori, M.1    Mynott, A.2    Ellis, J.J.3
  • 183
    • 84901507034 scopus 로고    scopus 로고
    • Nuclear envelope breakdown induced by herpes simplex virus type 1 involves the activity of viral fusion proteins
    • Maric M., Haugo A.C., Dauer W., Johnson D., Roller R.J. Nuclear envelope breakdown induced by herpes simplex virus type 1 involves the activity of viral fusion proteins. Virology 2014, 460-461:128-137. 10.1016/j.virol.2014.05.010.
    • (2014) Virology , pp. 128-137
    • Maric, M.1    Haugo, A.C.2    Dauer, W.3    Johnson, D.4    Roller, R.J.5
  • 185
    • 79960216982 scopus 로고    scopus 로고
    • Regulatory roles of protein kinases in cytomegalovirus replication
    • Marschall M., Feichtinger S., Milbradt J. Regulatory roles of protein kinases in cytomegalovirus replication. Advances in Virus Research 2011, 80:69-101. 10.1016/B978-0-12-385987-7.00004-X.
    • (2011) Advances in Virus Research , vol.80 , pp. 69-101
    • Marschall, M.1    Feichtinger, S.2    Milbradt, J.3
  • 186
    • 25844443739 scopus 로고    scopus 로고
    • Cellular p32 recruits cytomegalovirus kinase pUL97 to redistribute the nuclear lamina
    • Marschall M., Marzi A., aus dem Siepen P., et al. Cellular p32 recruits cytomegalovirus kinase pUL97 to redistribute the nuclear lamina. The Journal of Biological Chemistry 2005, 280(39):33357-33367. 10.1074/jbc.M502672200.
    • (2005) The Journal of Biological Chemistry , vol.280 , Issue.39 , pp. 33357-33367
    • Marschall, M.1    Marzi, A.2    aus dem Siepen, P.3
  • 187
    • 0035986315 scopus 로고    scopus 로고
    • Molecular characterization of protein kinase C-alpha binding to lamin A
    • Martelli A.M., Bortul R., Tabellini G., et al. Molecular characterization of protein kinase C-alpha binding to lamin A. Journal of Cellular Biochemistry 2002, 86(2):320-330. 10.1002/jcb.10227.
    • (2002) Journal of Cellular Biochemistry , vol.86 , Issue.2 , pp. 320-330
    • Martelli, A.M.1    Bortul, R.2    Tabellini, G.3
  • 188
    • 0031778720 scopus 로고    scopus 로고
    • Sonchus yellow net rhabdovirus nuclear viroplasms contain polymerase-associated proteins
    • Martins C.R., Johnson J.A., Lawrence D.M., et al. Sonchus yellow net rhabdovirus nuclear viroplasms contain polymerase-associated proteins. Journal of Virology 1998, 72(7):5669-5679.
    • (1998) Journal of Virology , vol.72 , Issue.7 , pp. 5669-5679
    • Martins, C.R.1    Johnson, J.A.2    Lawrence, D.M.3
  • 189
    • 0031707505 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: The soluble phase
    • Mattaj I.W., Englmeier L. Nucleocytoplasmic transport: The soluble phase. Annual Review of Biochemistry 1998, 67:265-306. 10.1146/annurev.biochem.67.1.265.
    • (1998) Annual Review of Biochemistry , vol.67 , pp. 265-306
    • Mattaj, I.W.1    Englmeier, L.2
  • 190
    • 0015160139 scopus 로고
    • Formation and distribution of nuclear pore complexes in interphase
    • Maul G.G., Price J.W., Lieberman M.W. Formation and distribution of nuclear pore complexes in interphase. The Journal of Cell Biology 1971, 51(21):405-418.
    • (1971) The Journal of Cell Biology , vol.51 , Issue.21 , pp. 405-418
    • Maul, G.G.1    Price, J.W.2    Lieberman, M.W.3
  • 191
    • 0031907093 scopus 로고    scopus 로고
    • The product of the herpes simplex virus type 1 UL25 gene is required for encapsidation but not for cleavage of replicated viral DNA
    • McNab A.R., Desai P., Person S., et al. The product of the herpes simplex virus type 1 UL25 gene is required for encapsidation but not for cleavage of replicated viral DNA. Journal of Virology 1998, 72(2):1060-1070.
    • (1998) Journal of Virology , vol.72 , Issue.2 , pp. 1060-1070
    • McNab, A.R.1    Desai, P.2    Person, S.3
  • 192
    • 77957678443 scopus 로고    scopus 로고
    • LINC complexes in health and disease
    • Mejat A., Misteli T. LINC complexes in health and disease. Nucleus 2010, 1(1):40-52. 10.4161/nucl.1.1.10530.
    • (2010) Nucleus , vol.1 , Issue.1 , pp. 40-52
    • Mejat, A.1    Misteli, T.2
  • 193
    • 36348938749 scopus 로고    scopus 로고
    • Nuclear fusion during yeast mating occurs by a three-step pathway
    • Melloy P., Shen S., White E., McIntosh J.R., Rose M.D. Nuclear fusion during yeast mating occurs by a three-step pathway. The Journal of Cell Biology 2007, 179(4):659-670. 10.1083/jcb.200706151.
    • (2007) The Journal of Cell Biology , vol.179 , Issue.4 , pp. 659-670
    • Melloy, P.1    Shen, S.2    White, E.3    McIntosh, J.R.4    Rose, M.D.5
  • 194
    • 16544387171 scopus 로고    scopus 로고
    • Bacteriophage T4: Structure, assembly, and initiation infection studied in three dimensions
    • Mesyanzhinov V.V. Bacteriophage T4: Structure, assembly, and initiation infection studied in three dimensions. Advances in Virus Research 2004, 63:287-352. 10.1016/S0065-3527(04)63005-3.
    • (2004) Advances in Virus Research , vol.63 , pp. 287-352
    • Mesyanzhinov, V.V.1
  • 195
    • 84928968782 scopus 로고    scopus 로고
    • Pseudorabies virus
    • Academic Press, Oxford, B.W.J. Mahy, M.H.V. van Regenmortel (Eds.)
    • Mettenleiter T.C. Pseudorabies virus. Encyclopedia of virology 2008, 341-351. Academic Press, Oxford. 3rd ed. B.W.J. Mahy, M.H.V. van Regenmortel (Eds.).
    • (2008) Encyclopedia of virology , pp. 341-351
    • Mettenleiter, T.C.1
  • 196
    • 68749090845 scopus 로고    scopus 로고
    • Herpesvirus assembly: An update
    • Mettenleiter T.C., Klupp B.G., Granzow H. Herpesvirus assembly: An update. Virus Research 2009, 143(2):222-234. 10.1016/j.virusres.2009.03.018.
    • (2009) Virus Research , vol.143 , Issue.2 , pp. 222-234
    • Mettenleiter, T.C.1    Klupp, B.G.2    Granzow, H.3
  • 197
    • 31144448686 scopus 로고    scopus 로고
    • Egress of alphaherpesviruses
    • (author reply 1611-1612)
    • Mettenleiter T.C., Minson T. Egress of alphaherpesviruses. Journal of Virology 2006, 80(3):1610-1611. (author reply 1611-1612). 10.1128/JVI.80.3.1610-1612.2006.
    • (2006) Journal of Virology , vol.80 , Issue.3 , pp. 1610-1611
    • Mettenleiter, T.C.1    Minson, T.2
  • 198
    • 84872616937 scopus 로고    scopus 로고
    • The way out: What we know and do not know about herpesvirus nuclear egress
    • Mettenleiter T.C., Müller F., Granzow H., Klupp B.G. The way out: What we know and do not know about herpesvirus nuclear egress. Cellular Microbiology 2013, 15(2):170-178. 10.1111/cmi.12044.
    • (2013) Cellular Microbiology , vol.15 , Issue.2 , pp. 170-178
    • Mettenleiter, T.C.1    Müller, F.2    Granzow, H.3    Klupp, B.G.4
  • 199
    • 84960873341 scopus 로고    scopus 로고
    • Breaching the barrier - the nuclear envelope in virus infection
    • Mettenleiter T.C. Breaching the barrier - the nuclear envelope in virus infection. Journal of Molecular Biology 2015, 10.1016/j.jmb.2015.10.001.
    • (2015) Journal of Molecular Biology
    • Mettenleiter, T.C.1
  • 201
    • 0034635392 scopus 로고    scopus 로고
    • Identification of a novel signal sequence that targets transmembrane proteins to the nuclear envelope inner membrane
    • Meyer G.A., Radsak K.D. Identification of a novel signal sequence that targets transmembrane proteins to the nuclear envelope inner membrane. The Journal of Biological Chemistry 2000, 275(6):3857-3866.
    • (2000) The Journal of Biological Chemistry , vol.275 , Issue.6 , pp. 3857-3866
    • Meyer, G.A.1    Radsak, K.D.2
  • 202
    • 77957655181 scopus 로고    scopus 로고
    • The intricacy of nuclear membrane dynamics during nucleophagy
    • Mijaljica D., Prescott M., Devenish R.J. The intricacy of nuclear membrane dynamics during nucleophagy. Nucleus 2010, 1(3):213-223. 10.4161/nucl.1.3.11738.
    • (2010) Nucleus , vol.1 , Issue.3 , pp. 213-223
    • Mijaljica, D.1    Prescott, M.2    Devenish, R.J.3
  • 203
    • 84863614597 scopus 로고    scopus 로고
    • Specific residues of a conserved domain in the N terminus of the human cytomegalovirus pUL50 protein determine its intranuclear interaction with pUL53
    • Milbradt J., Auerochs S., Sevvana M., Muller Y.A., Sticht H., Marschall M. Specific residues of a conserved domain in the N terminus of the human cytomegalovirus pUL50 protein determine its intranuclear interaction with pUL53. The Journal of Biological Chemistry 2012, 287(28):24004-24016. 10.1074/jbc.M111.331207.
    • (2012) The Journal of Biological Chemistry , vol.287 , Issue.28 , pp. 24004-24016
    • Milbradt, J.1    Auerochs, S.2    Sevvana, M.3    Muller, Y.A.4    Sticht, H.5    Marschall, M.6
  • 204
    • 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. The Journal of General Virology 2009, 90(Pt. 3):579-590. 10.1099/vir.0.005231-0.
    • (2009) The Journal of General Virology , vol.90 , pp. 579-590
    • Milbradt, J.1    Auerochs, S.2    Sticht, H.3    Marschall, M.4
  • 205
    • 84905253291 scopus 로고    scopus 로고
    • Proteomic analysis of the multimeric nuclear egress complex of human cytomegalovirus
    • Milbradt J., Kraut A., Hutterer C., et al. Proteomic analysis of the multimeric nuclear egress complex of human cytomegalovirus. Molecular and Cellular Proteomics 2014, 13(8):2132-2146. 10.1074/mcp.M113.035782.
    • (2014) Molecular and Cellular Proteomics , vol.13 , Issue.8 , pp. 2132-2146
    • Milbradt, J.1    Kraut, A.2    Hutterer, C.3
  • 206
    • 77951577056 scopus 로고    scopus 로고
    • Novel mode of phosphorylation-triggered reorganization of the nuclear lamina during nuclear egress of human cytomegalovirus
    • Milbradt J., Webel R., Auerochs S., Sticht H., Marschall M. Novel mode of phosphorylation-triggered reorganization of the nuclear lamina during nuclear egress of human cytomegalovirus. The Journal of Biological Chemistry 2010, 285(18):13979-13989. 10.1074/jbc.M109.063628.
    • (2010) The Journal of Biological Chemistry , vol.285 , Issue.18 , pp. 13979-13989
    • Milbradt, J.1    Webel, R.2    Auerochs, S.3    Sticht, H.4    Marschall, M.5
  • 207
    • 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. Journal of Virology 2002, 76(19):9934-9951.
    • (2002) Journal of Virology , vol.76 , Issue.19 , pp. 9934-9951
    • Miranda-Saksena, M.1    Boadle, R.A.2    Armati, P.3    Cunningham, A.L.4
  • 208
    • 0037106323 scopus 로고    scopus 로고
    • Sequence analysis of bacteriophage T4 DNA packaging/terminase genes 16 and 17 reveals a common ATPase center in the large subunit of viral terminases
    • Mitchell M.S., Matsuzaki S., Imai S., Rao V.B. Sequence analysis of bacteriophage T4 DNA packaging/terminase genes 16 and 17 reveals a common ATPase center in the large subunit of viral terminases. Nucleic Acids Research 2002, 30(18):4009-4021.
    • (2002) Nucleic Acids Research , vol.30 , Issue.18 , pp. 4009-4021
    • Mitchell, M.S.1    Matsuzaki, S.2    Imai, S.3    Rao, V.B.4
  • 209
    • 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. Journal of Virology 2007, 81(9):4429-4437. 10.1128/JVI.02354-06.
    • (2007) Journal of Virology , vol.81 , Issue.9 , pp. 4429-4437
    • Morris, J.B.1    Hofemeister, H.2    O'Hare, P.3
  • 210
    • 65349156839 scopus 로고    scopus 로고
    • Phosphorylation of the U(L)31 protein of herpes simplex virus 1 by the U(S)3-encoded kinase regulates localization of the nuclear envelopment complex and egress of nucleocapsids
    • Mou F., Wills E., Baines J.D. Phosphorylation of the U(L)31 protein of herpes simplex virus 1 by the U(S)3-encoded kinase regulates localization of the nuclear envelopment complex and egress of nucleocapsids. Journal of Virology 2009, 83(10):5181-5191. 10.1128/JVI.00090-09.
    • (2009) Journal of Virology , vol.83 , Issue.10 , pp. 5181-5191
    • Mou, F.1    Wills, E.2    Baines, J.D.3
  • 211
    • 49149090155 scopus 로고    scopus 로고
    • Effects of lamin A/C, lamin B1, and viral US3 kinase activity on viral infectivity, virion egress, and the targeting of herpes simplex virus U(L)34-encoded protein to the inner nuclear membrane
    • Mou F., Wills E.G., Park R., Baines J.D. Effects of lamin A/C, lamin B1, and viral US3 kinase activity on viral infectivity, virion egress, and the targeting of herpes simplex virus U(L)34-encoded protein to the inner nuclear membrane. Journal of Virology 2008, 82(16):8094-8104. 10.1128/JVI.00874-08.
    • (2008) Journal of Virology , vol.82 , Issue.16 , pp. 8094-8104
    • Mou, F.1    Wills, E.G.2    Park, R.3    Baines, J.D.4
  • 212
    • 0037008483 scopus 로고    scopus 로고
    • Cytomegalovirus recruitment of cellular kinases to dissolve the nuclear lamina
    • Muranyi W., Haas J., Wagner M., Krohne G., Koszinowski U.H. Cytomegalovirus recruitment of cellular kinases to dissolve the nuclear lamina. Science 2002, 297(5582):854-857. 10.1126/science.1071506.
    • (2002) Science , vol.297 , Issue.5582 , pp. 854-857
    • Muranyi, W.1    Haas, J.2    Wagner, M.3    Krohne, G.4    Koszinowski, U.H.5
  • 213
    • 40149086016 scopus 로고    scopus 로고
    • Nuclear egress and envelopment of herpes simplex virus capsids analyzed with dual-color fluorescence HSV1(17+)
    • Nagel C.H., Döhner K., Fathollahy M., et al. Nuclear egress and envelopment of herpes simplex virus capsids analyzed with dual-color fluorescence HSV1(17+). Journal of Virology 2008, 82(6):3109-3124. 10.1128/JVI.02124-07.
    • (2008) Journal of Virology , vol.82 , Issue.6 , pp. 3109-3124
    • Nagel, C.H.1    Döhner, K.2    Fathollahy, M.3
  • 214
    • 33144465751 scopus 로고    scopus 로고
    • Herpes simplex virus tegument protein VP16 is a component of primary enveloped virions
    • Naldinho-Souto R., Browne H., Minson T. Herpes simplex virus tegument protein VP16 is a component of primary enveloped virions. Journal of Virology 2006, 80(5):2582-2584. 10.1128/JVI.80.5.2582-2584.2006.
    • (2006) Journal of Virology , vol.80 , Issue.5 , pp. 2582-2584
    • Naldinho-Souto, R.1    Browne, H.2    Minson, T.3
  • 215
    • 56349160730 scopus 로고    scopus 로고
    • TorsinA binds the KASH domain of nesprins and participates in linkage between nuclear envelope and cytoskeleton
    • Nery F.C., Zeng J., Niland B.P., et al. TorsinA binds the KASH domain of nesprins and participates in linkage between nuclear envelope and cytoskeleton. Journal of Cell Science 2008, 121(Pt. 20):3476-3486. 10.1242/jcs.029454.
    • (2008) Journal of Cell Science , vol.121 , pp. 3476-3486
    • Nery, F.C.1    Zeng, J.2    Niland, B.P.3
  • 216
    • 23244438898 scopus 로고    scopus 로고
    • Involvement of the portal at an early step in herpes simplex virus capsid assembly
    • Newcomb W.W., Homa F.L., Brown J.C. Involvement of the portal at an early step in herpes simplex virus capsid assembly. Journal of Virology 2005, 79(16):10540-10546. 10.1128/JVI.79.16.10540-10546.2005.
    • (2005) Journal of Virology , vol.79 , Issue.16 , pp. 10540-10546
    • Newcomb, W.W.1    Homa, F.L.2    Brown, J.C.3
  • 217
    • 0141570625 scopus 로고    scopus 로고
    • Assembly of the herpes simplex virus capsid: Identification of soluble scaffold-portal complexes and their role in formation of portal-containing capsids
    • Newcomb W.W., Thomsen D.R., Homa F.L., Brown J.C. Assembly of the herpes simplex virus capsid: Identification of soluble scaffold-portal complexes and their role in formation of portal-containing capsids. Journal of Virology 2003, 77(18):9862-9871.
    • (2003) Journal of Virology , vol.77 , Issue.18 , pp. 9862-9871
    • Newcomb, W.W.1    Thomsen, D.R.2    Homa, F.L.3    Brown, J.C.4
  • 218
    • 67650718130 scopus 로고    scopus 로고
    • NLStradamus: A simple Hidden Markov Model for nuclear localization signal prediction
    • Nguyen Ba A.N., Pogoutse A., Provart N., Moses A.M. NLStradamus: A simple Hidden Markov Model for nuclear localization signal prediction. BMC Bioinformatics 2009, 10:202. 10.1186/1471-2105-10-202.
    • (2009) BMC Bioinformatics , vol.10 , pp. 202
    • Nguyen Ba, A.N.1    Pogoutse, A.2    Provart, N.3    Moses, A.M.4
  • 219
    • 0028210056 scopus 로고
    • Localization of the herpes simplex virus type 1 major capsid protein VP5 to the cell nucleus requires the abundant scaffolding protein VP22a
    • Nicholson P., Addison C., Cross A.M., Kennard J., Preston V.G., Rixon F.J. Localization of the herpes simplex virus type 1 major capsid protein VP5 to the cell nucleus requires the abundant scaffolding protein VP22a. The Journal of General Virology 1994, 75(Pt. 5):1091-1099.
    • (1994) The Journal of General Virology , vol.75 , pp. 1091-1099
    • Nicholson, P.1    Addison, C.2    Cross, A.M.3    Kennard, J.4    Preston, V.G.5    Rixon, F.J.6
  • 221
    • 84877946500 scopus 로고    scopus 로고
    • Comparative genomics in Chlamydomonas and Plasmodium identifies an ancient nuclear envelope protein family essential for sexual reproduction in protists, fungi, plants, and vertebrates
    • Ning J., Otto T.D., Pfander C., et al. Comparative genomics in Chlamydomonas and Plasmodium identifies an ancient nuclear envelope protein family essential for sexual reproduction in protists, fungi, plants, and vertebrates. Genes and Development 2013, 27(10):1198-1215. 10.1101/gad.212746.112.
    • (2013) Genes and Development , vol.27 , Issue.10 , pp. 1198-1215
    • Ning, J.1    Otto, T.D.2    Pfander, C.3
  • 222
    • 84868215286 scopus 로고    scopus 로고
    • Parvovirus transmission by blood products-A cause for concern?
    • Norja P., Lassila R., Makris M. Parvovirus transmission by blood products-A cause for concern?. British Journal of Haematology 2012, 159(4):385-393. 10.1111/bjh.12060.
    • (2012) British Journal of Haematology , vol.159 , Issue.4 , pp. 385-393
    • Norja, P.1    Lassila, R.2    Makris, M.3
  • 223
    • 0036901957 scopus 로고    scopus 로고
    • Cyclin dependent kinases and cell cycle control (nobel lecture)
    • Nurse P. Cyclin dependent kinases and cell cycle control (nobel lecture). ChemBioChem 2002, 3(7):596-603. 10.1002/1439-7633(20020703)3:7<596::AID-CBIC596>3.0.CO;2-U.
    • (2002) ChemBioChem , vol.3 , Issue.7 , pp. 596-603
    • Nurse, P.1
  • 224
    • 20144370936 scopus 로고    scopus 로고
    • Dissociation of heterochromatin protein 1 from lamin B receptor induced by human polyomavirus agnoprotein: Role in nuclear egress of viral particles
    • Okada Y., Suzuki T., Sunden Y., et al. Dissociation of heterochromatin protein 1 from lamin B receptor induced by human polyomavirus agnoprotein: Role in nuclear egress of viral particles. EMBO Reports 2005, 6(5):452-457. 10.1038/sj.embor.7400406.
    • (2005) EMBO Reports , vol.6 , Issue.5 , pp. 452-457
    • Okada, Y.1    Suzuki, T.2    Sunden, Y.3
  • 225
    • 77958036071 scopus 로고    scopus 로고
    • Lamin B receptor: Multi-tasking at the nuclear envelope
    • Olins A.L., Rhodes G., Welch D.B., Zwerger M., Olins D.E. Lamin B receptor: Multi-tasking at the nuclear envelope. Nucleus 2010, 1(1):53-70. 10.4161/nucl.1.1.10515.
    • (2010) Nucleus , vol.1 , Issue.1 , pp. 53-70
    • Olins, A.L.1    Rhodes, G.2    Welch, D.B.3    Zwerger, M.4    Olins, D.E.5
  • 226
    • 69249205412 scopus 로고    scopus 로고
    • Homotypic fusion of ER membranes requires the dynamin-like GTPase atlastin
    • Orso G., Pendin D., Liu S., et al. Homotypic fusion of ER membranes requires the dynamin-like GTPase atlastin. Nature 2009, 460(7258):978-983. 10.1038/nature08280.
    • (2009) Nature , vol.460 , Issue.7258 , pp. 978-983
    • Orso, G.1    Pendin, D.2    Liu, S.3
  • 227
    • 70849084351 scopus 로고    scopus 로고
    • Dynamics and molecular interactions of linker of nucleoskeleton and cytoskeleton (LINC) complex proteins
    • Östlund C., Folker E.S., Choi J.C., Gomes E.R., Gundersen G.G., Worman H.J. Dynamics and molecular interactions of linker of nucleoskeleton and cytoskeleton (LINC) complex proteins. Journal of Cell Science 2009, 122(Pt. 22):4099-4108. 10.1242/jcs.057075.
    • (2009) Journal of Cell Science , vol.122 , pp. 4099-4108
    • Östlund, C.1    Folker, E.S.2    Choi, J.C.3    Gomes, E.R.4    Gundersen, G.G.5    Worman, H.J.6
  • 228
    • 81255195647 scopus 로고    scopus 로고
    • Functional characterization of the essential tail anchor of the herpes simplex virus type 1 nuclear egress protein pUL34
    • Ott M., Tascher G., Hassdenteufel S., Zimmermann R., Haas J., Bailer S.M. Functional characterization of the essential tail anchor of the herpes simplex virus type 1 nuclear egress protein pUL34. The Journal of General Virology 2011, 92(Pt. 12):2734-2745. 10.1099/vir.0.032730-0.
    • (2011) The Journal of General Virology , vol.92 , pp. 2734-2745
    • Ott, M.1    Tascher, G.2    Hassdenteufel, S.3    Zimmermann, R.4    Haas, J.5    Bailer, S.M.6
  • 229
    • 84868197448 scopus 로고    scopus 로고
    • Programmed cell death pathways in cancer: A review of apoptosis, autophagy and programmed necrosis
    • Ouyang L., Shi Z., Zhao S., et al. Programmed cell death pathways in cancer: A review of apoptosis, autophagy and programmed necrosis. Cell Proliferation 2012, 45(6):487-498. 10.1111/j.1365-2184.2012.00845.x.
    • (2012) Cell Proliferation , vol.45 , Issue.6 , pp. 487-498
    • Ouyang, L.1    Shi, Z.2    Zhao, S.3
  • 230
    • 65349109171 scopus 로고    scopus 로고
    • Isolation and preliminary characterization of herpes simplex virus 1 primary enveloped virions from the perinuclear space
    • Padula M.E., Sydnor M.L., Wilson D.W. Isolation and preliminary characterization of herpes simplex virus 1 primary enveloped virions from the perinuclear space. Journal of Virology 2009, 83(10):4757-4765. 10.1128/JVI.01927-08.
    • (2009) Journal of Virology , vol.83 , Issue.10 , pp. 4757-4765
    • Padula, M.E.1    Sydnor, M.L.2    Wilson, D.W.3
  • 231
    • 0036175701 scopus 로고    scopus 로고
    • Nuclear pore complex is able to transport macromolecules with diameters of about 39 nm
    • Panté N., Kann M. Nuclear pore complex is able to transport macromolecules with diameters of about 39 nm. Molecular Biology of the Cell 2002, 13(2):425-434. 10.1091/mbc.01-06-0308.
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.2 , pp. 425-434
    • Panté, N.1    Kann, M.2
  • 232
    • 33645961583 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 infection induces activation and recruitment of protein kinase C to the nuclear membrane and increased phosphorylation of lamin B
    • Park R., Baines J.D. Herpes simplex virus type 1 infection induces activation and recruitment of protein kinase C to the nuclear membrane and increased phosphorylation of lamin B. Journal of Virology 2006, 80(1):494-504. 10.1128/JVI.80.1.494-504.2006.
    • (2006) Journal of Virology , vol.80 , Issue.1 , pp. 494-504
    • Park, R.1    Baines, J.D.2
  • 233
    • 0022546016 scopus 로고
    • Structural studies on lamin. Similarities and differences between lamin and intermediate-filament proteins
    • Parry D.A., Conway J.F., Steinert P.M. Structural studies on lamin. Similarities and differences between lamin and intermediate-filament proteins. The Biochemical Journal 1986, 238(1):305-308.
    • (1986) The Biochemical Journal , vol.238 , Issue.1 , pp. 305-308
    • Parry, D.A.1    Conway, J.F.2    Steinert, P.M.3
  • 234
    • 84899861422 scopus 로고    scopus 로고
    • Identification of conserved amino acids in pUL34 which are critical for function of the pseudorabies virus nuclear egress complex
    • Paßvogel L., Janke U., Klupp B.G., Granzow H., Mettenleiter T.C. Identification of conserved amino acids in pUL34 which are critical for function of the pseudorabies virus nuclear egress complex. Journal of Virology 2014, 88(11):6224-6231. 10.1128/JVI.00595-14.
    • (2014) Journal of Virology , vol.88 , Issue.11 , pp. 6224-6231
    • Paßvogel, L.1    Janke, U.2    Klupp, B.G.3    Granzow, H.4    Mettenleiter, T.C.5
  • 235
    • 84921688883 scopus 로고    scopus 로고
    • Functional characterization of nuclear trafficking signals in pseudorabies virus pUL31
    • Paßvogel L., Klupp B.G., Granzow H., Fuchs W., Mettenleiter T.C. Functional characterization of nuclear trafficking signals in pseudorabies virus pUL31. Journal of Virology 2015, 89(4):2002-2012. 10.1128/JVI.03143-14.
    • (2015) Journal of Virology , vol.89 , Issue.4 , pp. 2002-2012
    • Paßvogel, L.1    Klupp, B.G.2    Granzow, H.3    Fuchs, W.4    Mettenleiter, T.C.5
  • 236
    • 84875761236 scopus 로고    scopus 로고
    • Mapping of sequences in Pseudorabies virus pUL34 that are required for formation and function of the nuclear egress complex
    • Paßvogel L., Trübe P., Schuster F., Klupp B.G., Mettenleiter T.C. Mapping of sequences in Pseudorabies virus pUL34 that are required for formation and function of the nuclear egress complex. Journal of Virology 2013, 87(8):4475-4485. 10.1128/JVI.00021-13.
    • (2013) Journal of Virology , vol.87 , Issue.8 , pp. 4475-4485
    • Paßvogel, L.1    Trübe, P.2    Schuster, F.3    Klupp, B.G.4    Mettenleiter, T.C.5
  • 237
    • 84974717612 scopus 로고    scopus 로고
    • Herpesviridae
    • Lippincott Williams & Wilkins, Philadelphia, PA, D.M. Knipe, P.M. Howley (Eds.)
    • Pellet P.E., Roizman B. Herpesviridae. Fields virology 2013, 1802-1822. Lippincott Williams & Wilkins, Philadelphia, PA. 6th ed. D.M. Knipe, P.M. Howley (Eds.).
    • (2013) Fields virology , pp. 1802-1822
    • Pellet, P.E.1    Roizman, B.2
  • 238
    • 14544299215 scopus 로고    scopus 로고
    • Mechanisms of receptor-mediated nuclear import and nuclear export
    • Pemberton L.F., Paschal B.M. Mechanisms of receptor-mediated nuclear import and nuclear export. Traffic 2005, 6(3):187-198. 10.1111/j.1600-0854.2005.00270.x.
    • (2005) Traffic , vol.6 , Issue.3 , pp. 187-198
    • Pemberton, L.F.1    Paschal, B.M.2
  • 239
    • 47049094548 scopus 로고    scopus 로고
    • Small capsid protein pORF65 is essential for assembly of Kaposi's sarcoma-associated herpesvirus capsids
    • Perkins E.M., Anacker D., Davis A., Sankar V., Ambinder R.F., Desai P. Small capsid protein pORF65 is essential for assembly of Kaposi's sarcoma-associated herpesvirus capsids. Journal of Virology 2008, 82(14):7201-7211. 10.1128/JVI.00423-08.
    • (2008) Journal of Virology , vol.82 , Issue.14 , pp. 7201-7211
    • Perkins, E.M.1    Anacker, D.2    Davis, A.3    Sankar, V.4    Ambinder, R.F.5    Desai, P.6
  • 240
    • 84869239546 scopus 로고    scopus 로고
    • Characterization of conserved region 2-deficient mutants of the cytomegalovirus egress protein pM53
    • Pogoda M., Bosse J.B., Wagner F.M., et al. Characterization of conserved region 2-deficient mutants of the cytomegalovirus egress protein pM53. Journal of Virology 2012, 86(23):12512-12524. 10.1128/JVI.00471-12.
    • (2012) Journal of Virology , vol.86 , Issue.23 , pp. 12512-12524
    • Pogoda, M.1    Bosse, J.B.2    Wagner, F.M.3
  • 241
    • 77956019599 scopus 로고    scopus 로고
    • Dominant negative mutants of the murine cytomegalovirus M53 gene block nuclear egress and inhibit capsid maturation
    • Popa M., Ruzsics Z., Lötzerich M., et al. Dominant negative mutants of the murine cytomegalovirus M53 gene block nuclear egress and inhibit capsid maturation. Journal of Virology 2010, 84(18):9035-9046. 10.1128/JVI.00681-10.
    • (2010) Journal of Virology , vol.84 , Issue.18 , pp. 9035-9046
    • Popa, M.1    Ruzsics, Z.2    Lötzerich, M.3
  • 242
    • 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 Pathogen 2013, 9(10):e1003671. 10.1371/journal.ppat.1003671.
    • (2013) PLoS Pathogen , vol.9 , Issue.10
    • Porwal, M.1    Cohen, S.2    Snoussi, K.3
  • 244
    • 0025932334 scopus 로고
    • The herpes simplex virus 1 protein kinase encoded by the US3 gene mediates posttranslational modification of the phosphoprotein encoded by the UL34 gene
    • Purves F.C., Spector D., Roizman B. The herpes simplex virus 1 protein kinase encoded by the US3 gene mediates posttranslational modification of the phosphoprotein encoded by the UL34 gene. Journal of Virology 1991, 65(11):5757-5764.
    • (1991) Journal of Virology , vol.65 , Issue.11 , pp. 5757-5764
    • Purves, F.C.1    Spector, D.2    Roizman, B.3
  • 245
    • 0026612847 scopus 로고
    • UL34, the target of the herpes simplex virus U(S)3 protein kinase, is a membrane protein which in its unphosphorylated state associates with novel phosphoproteins
    • Purves F.C., Spector D., Roizman B. UL34, the target of the herpes simplex virus U(S)3 protein kinase, is a membrane protein which in its unphosphorylated state associates with novel phosphoproteins. Journal of Virology 1992, 66(7):4295-4303.
    • (1992) Journal of Virology , vol.66 , Issue.7 , pp. 4295-4303
    • Purves, F.C.1    Spector, D.2    Roizman, B.3
  • 246
    • 78549246735 scopus 로고    scopus 로고
    • Cytosol-dependent membrane fusion in ER, nuclear envelope and nuclear pore assembly: Biological implications
    • Rafikova E.R., Melikov K., Chernomordik L.V. Cytosol-dependent membrane fusion in ER, nuclear envelope and nuclear pore assembly: Biological implications. Nucleus 2010, 1(6):487-491. 10.4161/nucl.1.6.13514.
    • (2010) Nucleus , vol.1 , Issue.6 , pp. 487-491
    • Rafikova, E.R.1    Melikov, K.2    Chernomordik, L.V.3
  • 247
    • 84878646453 scopus 로고    scopus 로고
    • SV40 late protein VP4 forms toroidal pores to disrupt membranes for viral release
    • Raghava S., Giorda K.M., Romano F.B., Heuck A.P., Hebert D.N. SV40 late protein VP4 forms toroidal pores to disrupt membranes for viral release. Biochemistry 2013, 52(22):3939-3948. 10.1021/bi400036z.
    • (2013) Biochemistry , vol.52 , Issue.22 , pp. 3939-3948
    • Raghava, S.1    Giorda, K.M.2    Romano, F.B.3    Heuck, A.P.4    Hebert, D.N.5
  • 248
    • 69449090753 scopus 로고    scopus 로고
    • Bringing KASH under the SUN: The many faces of nucleo-cytoskeletal connections
    • Razafsky D., Hodzic D. Bringing KASH under the SUN: The many faces of nucleo-cytoskeletal connections. The Journal of Cell Biology 2009, 186(4):461-472. 10.1083/jcb.200906068.
    • (2009) The Journal of Cell Biology , vol.186 , Issue.4 , pp. 461-472
    • Razafsky, D.1    Hodzic, D.2
  • 249
    • 84898774183 scopus 로고    scopus 로고
    • Temporal and tissue-specific disruption of LINC complexes in vivo
    • Razafsky D., Hodzic D. Temporal and tissue-specific disruption of LINC complexes in vivo. Genesis 2014, 52(4):359-365. 10.1002/dvg.22755.
    • (2014) Genesis , vol.52 , Issue.4 , pp. 359-365
    • Razafsky, D.1    Hodzic, D.2
  • 250
    • 33846505946 scopus 로고    scopus 로고
    • Packaging of the virion host shutoff (VHS) protein of herpes simplex virus: Two forms of the VHS polypeptide are associated with intranuclear B and C capsids, but only one is associated with enveloped virions
    • Read G.S., Patterson M. Packaging of the virion host shutoff (VHS) protein of herpes simplex virus: Two forms of the VHS polypeptide are associated with intranuclear B and C capsids, but only one is associated with enveloped virions. Journal of Virology 2007, 81(3):1148-1161. 10.1128/JVI.01812-06.
    • (2007) Journal of Virology , vol.81 , Issue.3 , pp. 1148-1161
    • Read, G.S.1    Patterson, M.2
  • 251
    • 80055091791 scopus 로고    scopus 로고
    • In vitro nuclear egress of herpes simplex virus type 1 capsids
    • Remillard-Labrosse G., Lippé R. In vitro nuclear egress of herpes simplex virus type 1 capsids. Methods 2011, 55(2):153-159. 10.1016/j.ymeth.2011.07.006.
    • (2011) Methods , vol.55 , Issue.2 , pp. 153-159
    • Remillard-Labrosse, G.1    Lippé, R.2
  • 252
    • 2442697760 scopus 로고    scopus 로고
    • Conformational changes in the nuclear lamina induced by herpes simplex virus type 1 require genes U(L)31 and U(L)34
    • Reynolds A.E., Liang L., Baines J.D. Conformational changes in the nuclear lamina induced by herpes simplex virus type 1 require genes U(L)31 and U(L)34. Journal of Virology 2004, 78(11):5564-5575. 10.1128/JVI.78.11.5564-5575.2004.
    • (2004) Journal of Virology , vol.78 , Issue.11 , pp. 5564-5575
    • Reynolds, A.E.1    Liang, L.2    Baines, J.D.3
  • 253
    • 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., Zhou Y., Liang L., Roller R.J. 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. Journal of Virology 2001, 75(18):8803-8817.
    • (2001) Journal of Virology , vol.75 , Issue.18 , pp. 8803-8817
    • Reynolds, A.E.1    Ryckman, B.J.2    Baines, J.D.3    Zhou, Y.4    Liang, L.5    Roller, R.J.6
  • 254
    • 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., Ryckman B.J., Baines J.D. Ultrastructural localization of the herpes simplex virus type 1 UL31, UL34, and US3 proteins suggests specific roles in primary envelopment and egress of nucleocapsids. Journal of Virology 2002, 76(17):8939-8952.
    • (2002) Journal of Virology , vol.76 , Issue.17 , pp. 8939-8952
    • Reynolds, A.E.1    Wills, E.G.2    Roller, R.J.3    Ryckman, B.J.4    Baines, J.D.5
  • 255
    • 0029840591 scopus 로고    scopus 로고
    • Multiple interactions control the intracellular localization of the herpes simplex virus type 1 capsid proteins
    • Rixon F.J., Addison C., McGregor A., et al. Multiple interactions control the intracellular localization of the herpes simplex virus type 1 capsid proteins. The Journal of General Virology 1996, 77(Pt. 9):2251-2260.
    • (1996) The Journal of General Virology , vol.77 , pp. 2251-2260
    • Rixon, F.J.1    Addison, C.2    McGregor, A.3
  • 256
    • 84890522876 scopus 로고    scopus 로고
    • ER-associated SNAREs and Sey1p mediate nuclear fusion at two distinct steps during yeast mating
    • Rogers J.V., Arlow T., Inkellis E.R., Koo T.S., Rose M.D. ER-associated SNAREs and Sey1p mediate nuclear fusion at two distinct steps during yeast mating. Molecular Biology of the Cell 2013, 24(24):3896-3908. 10.1091/mbc.E13-08-0441.
    • (2013) Molecular Biology of the Cell , vol.24 , Issue.24 , pp. 3896-3908
    • Rogers, J.V.1    Arlow, T.2    Inkellis, E.R.3    Koo, T.S.4    Rose, M.D.5
  • 257
    • 84921465379 scopus 로고    scopus 로고
    • Kar5p is required for multiple functions in both inner and outer nuclear envelope fusion in Saccharomyces cerevisiae
    • Rogers J.V., Rose M.D. Kar5p is required for multiple functions in both inner and outer nuclear envelope fusion in Saccharomyces cerevisiae. G3 (Bethesda, MD) 2014, 5(1):111-121. 10.1534/g3.114.015800.
    • (2014) G3 (Bethesda, MD) , vol.5 , Issue.1 , pp. 111-121
    • Rogers, J.V.1    Rose, M.D.2
  • 258
    • 0001142641 scopus 로고    scopus 로고
    • Herpes simplex viruses and their replication
    • Lippincott Williams & Wilkins, Philadelphia, PA, D.M. Knipe, P.M. Howley (Eds.)
    • Roizman B., Knipe D.M. Herpes simplex viruses and their replication. Fields virology, vol. 2 2001, Lippincott Williams & Wilkins, Philadelphia, PA. 4th ed. D.M. Knipe, P.M. Howley (Eds.).
    • (2001) Fields virology, vol. 2
    • Roizman, B.1    Knipe, D.M.2
  • 259
    • 77950466161 scopus 로고    scopus 로고
    • Analysis of a charge cluster mutation of herpes simplex virus type 1 UL34 and its extragenic suppressor suggests a novel interaction between pUL34 and pUL31 that is necessary for membrane curvature around capsids
    • Roller R.J., Bjerke S.L., Haugo A.C., Hanson S. Analysis of a charge cluster mutation of herpes simplex virus type 1 UL34 and its extragenic suppressor suggests a novel interaction between pUL34 and pUL31 that is necessary for membrane curvature around capsids. Journal of Virology 2010, 84(8):3921-3934. 10.1128/JVI.01638-09.
    • (2010) Journal of Virology , vol.84 , Issue.8 , pp. 3921-3934
    • Roller, R.J.1    Bjerke, S.L.2    Haugo, A.C.3    Hanson, S.4
  • 260
    • 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., Ferguson J., DeSalvo D. Herpes simplex virus type 1 U(L)34 gene product is required for viral envelopment. Journal of Virology 2000, 74(1):117-129.
    • (2000) Journal of Virology , vol.74 , Issue.1 , pp. 117-129
    • Roller, R.J.1    Zhou, Y.2    Schnetzer, R.3    Ferguson, J.4    DeSalvo, D.5
  • 261
    • 84866854226 scopus 로고    scopus 로고
    • Alternative nuclear transport for cellular protein quality control
    • Rose A., Schlieker C. Alternative nuclear transport for cellular protein quality control. Trends in Cell Biology 2012, 22(10):509-514. 10.1016/j.tcb.2012.07.003.
    • (2012) Trends in Cell Biology , vol.22 , Issue.10 , pp. 509-514
    • Rose, A.1    Schlieker, C.2
  • 262
    • 84885846858 scopus 로고    scopus 로고
    • The diverse functional LINCs of the nuclear envelope to the cytoskeleton and chromatin
    • Rothballer A., Kutay U. The diverse functional LINCs of the nuclear envelope to the cytoskeleton and chromatin. Chromosoma 2013, 122(5):415-429. 10.1007/s00412-013-0417-x.
    • (2013) Chromosoma , vol.122 , Issue.5 , pp. 415-429
    • Rothballer, A.1    Kutay, U.2
  • 263
    • 84899992121 scopus 로고    scopus 로고
    • Endoplasmatic reticulum shaping by generic mechanisms and protein-induced spontaneous curvature
    • Sackmann E. Endoplasmatic reticulum shaping by generic mechanisms and protein-induced spontaneous curvature. Advances in Colloid and Interface Science 2014, 208:153-160. 10.1016/j.cis.2014.02.006.
    • (2014) Advances in Colloid and Interface Science , vol.208 , pp. 153-160
    • Sackmann, E.1
  • 264
    • 63149109165 scopus 로고    scopus 로고
    • Biochemical, biophysical, and mutational analyses of subunit interactions of the human cytomegalovirus nuclear egress complex
    • Sam M.D., Evans B.T., Coen D.M., Hogle J.M. Biochemical, biophysical, and mutational analyses of subunit interactions of the human cytomegalovirus nuclear egress complex. Journal of Virology 2009, 83(7):2996-3006. 10.1128/JVI.02441-08.
    • (2009) Journal of Virology , vol.83 , Issue.7 , pp. 2996-3006
    • Sam, M.D.1    Evans, B.T.2    Coen, D.M.3    Hogle, J.M.4
  • 266
    • 0042691509 scopus 로고    scopus 로고
    • Nuclear membrane proteins with potential disease links found by subtractive proteomics
    • Schirmer E.C., Florens L., Guan T., Yates J.R., Gerace L. Nuclear membrane proteins with potential disease links found by subtractive proteomics. Science 2003, 301(5638):1380-1382. 10.1126/science.1088176.
    • (2003) Science , vol.301 , Issue.5638 , pp. 1380-1382
    • Schirmer, E.C.1    Florens, L.2    Guan, T.3    Yates, J.R.4    Gerace, L.5
  • 267
    • 34249668426 scopus 로고    scopus 로고
    • Proteins that associate with lamins: Many faces, many functions
    • Schirmer E.C., Foisner R. Proteins that associate with lamins: Many faces, many functions. Experimental Cell Research 2007, 313(10):2167-2179. 10.1016/j.yexcr.2007.03.012.
    • (2007) Experimental Cell Research , vol.313 , Issue.10 , pp. 2167-2179
    • Schirmer, E.C.1    Foisner, R.2
  • 268
    • 84881619516 scopus 로고    scopus 로고
    • The cytomegalovirus egress proteins pUL50 and pUL53 are translocated to the nuclear envelope through two distinct modes of nuclear import
    • Schmeiser C., Borst E., Sticht H., Marschall M., Milbradt J. The cytomegalovirus egress proteins pUL50 and pUL53 are translocated to the nuclear envelope through two distinct modes of nuclear import. The Journal of General Virology 2013, 94(Pt. 9):2056-2069. 10.1099/vir.0.052571-0.
    • (2013) The Journal of General Virology , vol.94 , pp. 2056-2069
    • Schmeiser, C.1    Borst, E.2    Sticht, H.3    Marschall, M.4    Milbradt, J.5
  • 269
    • 33751234823 scopus 로고    scopus 로고
    • Common and specific properties of herpesvirus UL34/UL31 protein family members revealed by protein complementation assay
    • Schnee M., Ruzsics Z., Bubeck A., Koszinowski U.H. Common and specific properties of herpesvirus UL34/UL31 protein family members revealed by protein complementation assay. Journal of Virology 2006, 80(23):11658-11666. 10.1128/JVI.01662-06.
    • (2006) Journal of Virology , vol.80 , Issue.23 , pp. 11658-11666
    • Schnee, M.1    Ruzsics, Z.2    Bubeck, A.3    Koszinowski, U.H.4
  • 270
    • 84872095628 scopus 로고    scopus 로고
    • Building a nuclear envelope at the end of mitosis: Coordinating membrane reorganization, nuclear pore complex assembly, and chromatin de-condensation
    • Schooley A., Vollmer B., Antonin W. Building a nuclear envelope at the end of mitosis: Coordinating membrane reorganization, nuclear pore complex assembly, and chromatin de-condensation. Chromosoma 2012, 121(6):539-554. 10.1007/s00412-012-0388-3.
    • (2012) Chromosoma , vol.121 , Issue.6 , pp. 539-554
    • Schooley, A.1    Vollmer, B.2    Antonin, W.3
  • 271
    • 84883298918 scopus 로고    scopus 로고
    • Glycoproteins gB and gH are required for syncytium formation but not for herpesvirus-induced nuclear envelope breakdown
    • Schulz K.S., Klupp B.G., Granzow H., Mettenleiter T.C. Glycoproteins gB and gH are required for syncytium formation but not for herpesvirus-induced nuclear envelope breakdown. Journal of Virology 2013, 87(17):9733-9741. 10.1128/JVI.01401-13.
    • (2013) Journal of Virology , vol.87 , Issue.17 , pp. 9733-9741
    • Schulz, K.S.1    Klupp, B.G.2    Granzow, H.3    Mettenleiter, T.C.4
  • 272
    • 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
    • Schulz K.S., Klupp B.G., Granzow H., Passvogel L., Mettenleiter T.C. Herpesvirus nuclear egress: Pseudorabies virus can simultaneously induce nuclear envelope breakdown and exit the nucleus via the envelopment-deenvelopment-pathway. Virus Research 2015, 209:76-86. 10.1016/j.virusres.2015.02.001.
    • (2015) Virus Research , vol.209 , pp. 76-86
    • Schulz, K.S.1    Klupp, B.G.2    Granzow, H.3    Passvogel, L.4    Mettenleiter, T.C.5
  • 273
    • 15244359449 scopus 로고    scopus 로고
    • The protein encoded by the US3 orthologue of Marek's disease virus is required for efficient de-envelopment of perinuclear virions and involved in actin stress fiber breakdown
    • Schumacher D., Tischer B.K., Trapp S., Osterrieder N. The protein encoded by the US3 orthologue of Marek's disease virus is required for efficient de-envelopment of perinuclear virions and involved in actin stress fiber breakdown. Journal of Virology 2005, 79(7):3987-3997. 10.1128/JVI.79.7.3987-3997.2005.
    • (2005) Journal of Virology , vol.79 , Issue.7 , pp. 3987-3997
    • Schumacher, D.1    Tischer, B.K.2    Trapp, S.3    Osterrieder, N.4
  • 274
    • 84857082181 scopus 로고    scopus 로고
    • Structural determinants for nuclear envelope localization and function of pseudorabies virus pUL34
    • Schuster F., Klupp B.G., Granzow H., Mettenleiter T.C. Structural determinants for nuclear envelope localization and function of pseudorabies virus pUL34. Journal of Virology 2012, 86(4):2079-2088. 10.1128/JVI.05484-11.
    • (2012) Journal of Virology , vol.86 , Issue.4 , pp. 2079-2088
    • Schuster, F.1    Klupp, B.G.2    Granzow, H.3    Mettenleiter, T.C.4
  • 275
    • 84919459578 scopus 로고    scopus 로고
    • Human cytomegalovirus UL97 phosphorylates the viral nuclear egress complex
    • Sharma M., Bender B.J., Kamil J.P., et al. Human cytomegalovirus UL97 phosphorylates the viral nuclear egress complex. Journal of Virology 2015, 89(1):523-534. 10.1128/JVI.02426-14.
    • (2015) Journal of Virology , vol.89 , Issue.1 , pp. 523-534
    • Sharma, M.1    Bender, B.J.2    Kamil, J.P.3
  • 276
    • 84890880476 scopus 로고    scopus 로고
    • Human cytomegalovirus UL50 and UL53 recruit viral protein kinase UL97, not protein kinase C, for disruption of nuclear lamina and nuclear egress in infected cells
    • Sharma M., Kamil J.P., Coughlin M., Reim N.I., Coen D.M. Human cytomegalovirus UL50 and UL53 recruit viral protein kinase UL97, not protein kinase C, for disruption of nuclear lamina and nuclear egress in infected cells. Journal of Virology 2014, 88(1):249-262. 10.1128/JVI.02358-13.
    • (2014) Journal of Virology , vol.88 , Issue.1 , pp. 249-262
    • Sharma, M.1    Kamil, J.P.2    Coughlin, M.3    Reim, N.I.4    Coen, D.M.5
  • 277
    • 84901601509 scopus 로고    scopus 로고
    • Lamina-associated polypeptide 1: Protein interactions and tissue-selective functions
    • Shin J.Y., Dauer W.T., Worman H.J. Lamina-associated polypeptide 1: Protein interactions and tissue-selective functions. Seminars in Cell and Developmental Biology 2014, 29:164-168. 10.1016/j.semcdb.2014.01.010.
    • (2014) Seminars in Cell and Developmental Biology , vol.29 , pp. 164-168
    • Shin, J.Y.1    Dauer, W.T.2    Worman, H.J.3
  • 278
    • 0037221524 scopus 로고    scopus 로고
    • Binding dynamics of structural nucleoporins govern nuclear pore complex permeability and may mediate channel gating
    • Shulga N., Goldfarb D.S. Binding dynamics of structural nucleoporins govern nuclear pore complex permeability and may mediate channel gating. Molecular and Cellular Biology 2003, 23(2):534-542.
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.2 , pp. 534-542
    • Shulga, N.1    Goldfarb, D.S.2
  • 279
    • 0035794643 scopus 로고    scopus 로고
    • LAP2 binds to BAF.DNA complexes: Requirement for the LEM domain and modulation by variable regions
    • Shumaker D.K., Lee K.K., Tanhehco Y.C., Craigie R., Wilson K.L. LAP2 binds to BAF.DNA complexes: Requirement for the LEM domain and modulation by variable regions. The EMBO Journal 2001, 20(7):1754-1764. 10.1093/emboj/20.7.1754.
    • (2001) The EMBO Journal , vol.20 , Issue.7 , pp. 1754-1764
    • Shumaker, D.K.1    Lee, K.K.2    Tanhehco, Y.C.3    Craigie, R.4    Wilson, K.L.5
  • 280
    • 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., Harper J.W., Knipe D.M. Identification and functional evaluation of cellular and viral factors involved in the alteration of nuclear architecture during herpes simplex virus 1 infection. Journal of Virology 2005, 79(20):12840-12851. 10.1128/JVI.79.20.12840-12851.2005.
    • (2005) Journal of Virology , vol.79 , Issue.20 , pp. 12840-12851
    • Simpson-Holley, M.1    Colgrove, R.C.2    Nalepa, G.3    Harper, J.W.4    Knipe, D.M.5
  • 281
    • 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. Journal of Virology 2001, 75(12):5697-5702. 10.1128/JVI.75.12.5697-5702.2001.
    • (2001) Journal of Virology , vol.75 , Issue.12 , pp. 5697-5702
    • Skepper, J.N.1    Whiteley, A.2    Browne, H.3    Minson, A.4
  • 282
    • 84884548761 scopus 로고    scopus 로고
    • Breaking down the wall: The nuclear envelope during mitosis
    • Smoyer C.J., Jaspersen S.L. Breaking down the wall: The nuclear envelope during mitosis. Current Opinion in Cell Biology 2014, 26:1-9. 10.1016/j.ceb.2013.08.002.
    • (2014) Current Opinion in Cell Biology , vol.26 , pp. 1-9
    • Smoyer, C.J.1    Jaspersen, S.L.2
  • 285
    • 84861543038 scopus 로고    scopus 로고
    • LINC complexes form by binding of three KASH peptides to domain interfaces of trimeric SUN proteins
    • Sosa B.A., Rothballer A., Kutay U., Schwartz T.U. LINC complexes form by binding of three KASH peptides to domain interfaces of trimeric SUN proteins. Cell 2012, 149(5):1035-1047. 10.1016/j.cell.2012.03.046.
    • (2012) Cell , vol.149 , Issue.5 , pp. 1035-1047
    • Sosa, B.A.1    Rothballer, A.2    Kutay, U.3    Schwartz, T.U.4
  • 286
    • 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(4):832-846. 10.1016/j.cell.2012.03.032.
    • (2012) Cell , vol.149 , Issue.4 , pp. 832-846
    • Speese, S.D.1    Ashley, J.2    Jokhi, V.3
  • 287
    • 0029687939 scopus 로고    scopus 로고
    • Intra-nuclear localization of two envelope proteins, gB and gD, of herpes simplex virus
    • Stannard L.M., Himmelhoch S., Wynchank S. Intra-nuclear localization of two envelope proteins, gB and gD, of herpes simplex virus. Archives of Virology 1996, 141(3-4):505-524.
    • (1996) Archives of Virology , vol.141 , Issue.3-4 , pp. 505-524
    • Stannard, L.M.1    Himmelhoch, S.2    Wynchank, S.3
  • 288
    • 79958041607 scopus 로고    scopus 로고
    • KASH and SUN proteins
    • Starr D.A. KASH and SUN proteins. Current Biology 2011, 21(11):R414-R415. 10.1016/j.cub.2011.04.022.
    • (2011) Current Biology , vol.21 , Issue.11 , pp. R414-R415
    • Starr, D.A.1
  • 289
    • 0034754986 scopus 로고    scopus 로고
    • Packaging of genomic and amplicon DNA by the herpes simplex virus type 1 UL25-null mutant KUL25NS
    • Stow N.D. Packaging of genomic and amplicon DNA by the herpes simplex virus type 1 UL25-null mutant KUL25NS. Journal of Virology 2001, 75(22):10755-10765. 10.1128/JVI.75.22.10755-10765.2001.
    • (2001) Journal of Virology , vol.75 , Issue.22 , pp. 10755-10765
    • Stow, N.D.1
  • 290
    • 0031686054 scopus 로고    scopus 로고
    • Nuclear lamins: Their structure, assembly, and interactions
    • Stuurman N., Heins S., Aebi U. Nuclear lamins: Their structure, assembly, and interactions. Journal of Structural Biology 1998, 122(1-2):42-66. 10.1006/jsbi.1998.3987.
    • (1998) Journal of Structural Biology , vol.122 , Issue.1-2 , pp. 42-66
    • Stuurman, N.1    Heins, S.2    Aebi, U.3
  • 291
    • 0015070046 scopus 로고
    • Electron microscopic observations on granulosis virus entry, uncoating and replication processes during infection of the midgut cells of Trichoplusia ni
    • Summers M.D. Electron microscopic observations on granulosis virus entry, uncoating and replication processes during infection of the midgut cells of Trichoplusia ni. Journal of Ultrastructure Research 1971, 35(5):606-625.
    • (1971) Journal of Ultrastructure Research , vol.35 , Issue.5 , pp. 606-625
    • Summers, M.D.1
  • 292
    • 0013784275 scopus 로고
    • Extrusion of nucleoli from pronuclei of the rat
    • Szollosi D. Extrusion of nucleoli from pronuclei of the rat. The Journal of Cell Biology 1965, 25(3):545-562.
    • (1965) The Journal of Cell Biology , vol.25 , Issue.3 , pp. 545-562
    • Szollosi, D.1
  • 293
    • 79960233453 scopus 로고    scopus 로고
    • POM121 and Sun1 play a role in early steps of interphase NPC assembly
    • Talamas J.A., Hetzer M.W. POM121 and Sun1 play a role in early steps of interphase NPC assembly. The Journal of Cell Biology 2011, 194(1):27-37. 10.1083/jcb.201012154.
    • (2011) The Journal of Cell Biology , vol.194 , Issue.1 , pp. 27-37
    • Talamas, J.A.1    Hetzer, M.W.2
  • 294
    • 84873701716 scopus 로고    scopus 로고
    • Connecting the nucleus to the cytoskeleton by SUN-KASH bridges across the nuclear envelope
    • Tapley E.C., Starr D.A. Connecting the nucleus to the cytoskeleton by SUN-KASH bridges across the nuclear envelope. Current Opinion in Cell Biology 2013, 25(1):57-62. 10.1016/j.ceb.2012.10.014.
    • (2013) Current Opinion in Cell Biology , vol.25 , Issue.1 , pp. 57-62
    • Tapley, E.C.1    Starr, D.A.2
  • 295
    • 0032488237 scopus 로고    scopus 로고
    • The herpes simplex virus 1 UL 17 gene is required for localization of capsids and major and minor capsid proteins to intranuclear sites where viral DNA is cleaved and packaged
    • Taus N.S., Salmon B., Baines J.D. The herpes simplex virus 1 UL 17 gene is required for localization of capsids and major and minor capsid proteins to intranuclear sites where viral DNA is cleaved and packaged. Virology 1998, 252(1):115-125. 10.1006/viro.1998.9439.
    • (1998) Virology , vol.252 , Issue.1 , pp. 115-125
    • Taus, N.S.1    Salmon, B.2    Baines, J.D.3
  • 296
    • 79956141898 scopus 로고    scopus 로고
    • Subversion of the actin cytoskeleton during viral infection
    • Taylor M.P., Koyuncu O.O., Enquist L.W. Subversion of the actin cytoskeleton during viral infection. Nature Reviews Microbiology 2011, 9(6):427-439. 10.1038/nrmicro2574.
    • (2011) Nature Reviews Microbiology , vol.9 , Issue.6 , pp. 427-439
    • Taylor, M.P.1    Koyuncu, O.O.2    Enquist, L.W.3
  • 298
    • 79960400096 scopus 로고    scopus 로고
    • The herpes simplex virus 1 UL17 protein is the second constituent of the capsid vertex-specific component required for DNA packaging and retention
    • Toropova K., Huffman J.B., Homa F.L., Conway J.F. The herpes simplex virus 1 UL17 protein is the second constituent of the capsid vertex-specific component required for DNA packaging and retention. Journal of Virology 2011, 85(15):7513-7522. 10.1128/JVI.00837-11.
    • (2011) Journal of Virology , vol.85 , Issue.15 , pp. 7513-7522
    • Toropova, K.1    Huffman, J.B.2    Homa, F.L.3    Conway, J.F.4
  • 300
    • 34248583632 scopus 로고    scopus 로고
    • Allosteric signaling and a nuclear exit strategy: Binding of UL25/UL17 heterodimers to DNA-filled HSV-1 capsids
    • Trus B.L., Newcomb W.W., Cheng N., et al. Allosteric signaling and a nuclear exit strategy: Binding of UL25/UL17 heterodimers to DNA-filled HSV-1 capsids. Molecular Cell 2007, 26(4):479-489. 10.1016/j.molcel.2007.04.010.
    • (2007) Molecular Cell , vol.26 , Issue.4 , pp. 479-489
    • Trus, B.L.1    Newcomb, W.W.2    Cheng, N.3
  • 301
    • 84938054462 scopus 로고    scopus 로고
    • The torsin activator LULL1 is required for efficient growth of herpes simplex virus 1
    • Turner E.M., Brown R.S., Laudermilch E., Tsai P.L., Schlieker C. The torsin activator LULL1 is required for efficient growth of herpes simplex virus 1. Journal of Virology 2015, 89(16):8444-8452. 10.1128/JVI.01143-15.
    • (2015) Journal of Virology , vol.89 , Issue.16 , pp. 8444-8452
    • Turner, E.M.1    Brown, R.S.2    Laudermilch, E.3    Tsai, P.L.4    Schlieker, C.5
  • 303
    • 66349137319 scopus 로고    scopus 로고
    • LULL1 retargets TorsinA to the nuclear envelope revealing an activity that is impaired by the DYT1 dystonia mutation
    • Vander Heyden A.B., Naismith T.V., Snapp E.L., Hodzic D., Hanson P.I. LULL1 retargets TorsinA to the nuclear envelope revealing an activity that is impaired by the DYT1 dystonia mutation. Molecular Biology of the Cell 2009, 20(11):2661-2672. 10.1091/mbc.E09-01-0094.
    • (2009) Molecular Biology of the Cell , vol.20 , Issue.11 , pp. 2661-2672
    • Vander Heyden, A.B.1    Naismith, T.V.2    Snapp, E.L.3    Hodzic, D.4    Hanson, P.I.5
  • 304
    • 0028269719 scopus 로고
    • The phospholipid composition of extracellular herpes simplex virions differs from that of host cell nuclei
    • van Genderen I.L., Brandimarti R., Torrisi M.R., Campadelli G., van Meer G. The phospholipid composition of extracellular herpes simplex virions differs from that of host cell nuclei. Virology 1994, 200(2):831-836. 10.1006/viro.1994.1252.
    • (1994) Virology , vol.200 , Issue.2 , pp. 831-836
    • van Genderen, I.L.1    Brandimarti, R.2    Torrisi, M.R.3    Campadelli, G.4    van Meer, G.5
  • 305
    • 82755198920 scopus 로고    scopus 로고
    • Varicella zoster virus ORF25 gene product: An essential hub protein linking encapsidation proteins and the nuclear egress complex
    • Vizoso Pinto M.G., Pothineni V.R., Haase R., et al. Varicella zoster virus ORF25 gene product: An essential hub protein linking encapsidation proteins and the nuclear egress complex. Journal of Proteome Research 2011, 10(12):5374-5382. 10.1021/pr200628s.
    • (2011) Journal of Proteome Research , vol.10 , Issue.12 , pp. 5374-5382
    • Vizoso Pinto, M.G.1    Pothineni, V.R.2    Haase, R.3
  • 306
    • 84946909060 scopus 로고    scopus 로고
    • Crystal structure of the human cytomegalovirus pUL50-pUL53 nuclear egress complex provides insight into a unique assembly scaffold for virus-host protein interactions
    • Walzer S.A., Egerer-Sieber C., Sticht H., et al. Crystal structure of the human cytomegalovirus pUL50-pUL53 nuclear egress complex provides insight into a unique assembly scaffold for virus-host protein interactions. The Journal of Biological Chemistry 2015, 290(46):27452-27458.
    • (2015) The Journal of Biological Chemistry , vol.290 , Issue.46 , pp. 27452-27458
    • Walzer, S.A.1    Egerer-Sieber, C.2    Sticht, H.3
  • 307
    • 84875162180 scopus 로고    scopus 로고
    • Enclosing chromatin: Reassembly of the nucleus after open mitosis
    • Wandke C., Kutay U. Enclosing chromatin: Reassembly of the nucleus after open mitosis. Cell 2013, 152(6):1222-1225. 10.1016/j.cell.2013.02.046.
    • (2013) Cell , vol.152 , Issue.6 , pp. 1222-1225
    • Wandke, C.1    Kutay, U.2
  • 308
    • 84867055836 scopus 로고    scopus 로고
    • Structural insights into SUN-KASH complexes across the nuclear envelope
    • Wang W., Shi Z., Jiao S., et al. Structural insights into SUN-KASH complexes across the nuclear envelope. Cell Research 2012, 22(10):1440-1452. 10.1038/cr.2012.126.
    • (2012) Cell Research , vol.22 , Issue.10 , pp. 1440-1452
    • Wang, W.1    Shi, Z.2    Jiao, S.3
  • 309
    • 84891708202 scopus 로고    scopus 로고
    • Autographa californica Nucleopolyhedrovirus Ac76: A dimeric type II integral membrane protein that contains an inner nuclear membrane-sorting motif
    • Wei D., Wang Y., Zhang X., Hu Z., Yuan M., Yang K. Autographa californica Nucleopolyhedrovirus Ac76: A dimeric type II integral membrane protein that contains an inner nuclear membrane-sorting motif. Journal of Virology 2014, 88(2):1090-1103. 10.1128/JVI.02392-13.
    • (2014) Journal of Virology , vol.88 , Issue.2 , pp. 1090-1103
    • Wei, D.1    Wang, Y.2    Zhang, X.3    Hu, Z.4    Yuan, M.5    Yang, K.6
  • 310
    • 0034717044 scopus 로고    scopus 로고
    • Gatekeepers of the nucleus
    • Wente S.R. Gatekeepers of the nucleus. Science 2000, 288(5470):1374-1377.
    • (2000) Science , vol.288 , Issue.5470 , pp. 1374-1377
    • Wente, S.R.1
  • 313
    • 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 1998, 246(1):1-23. 10.1006/viro.1998.9165.
    • (1998) Virology , vol.246 , Issue.1 , pp. 1-23
    • Whittaker, G.R.1    Helenius, A.2
  • 314
    • 19944426290 scopus 로고    scopus 로고
    • Impairment of nuclear pores in bovine herpesvirus 1-infected MDBK cells
    • Wild P., Engels M., Senn C., et al. Impairment of nuclear pores in bovine herpesvirus 1-infected MDBK cells. Journal of Virology 2005, 79(2):1071-1083. 10.1128/JVI.79.2.1071-1083.2005.
    • (2005) Journal of Virology , vol.79 , Issue.2 , pp. 1071-1083
    • Wild, P.1    Engels, M.2    Senn, C.3
  • 315
    • 0029850158 scopus 로고    scopus 로고
    • Replication patterns and cytopathology of cells infected with baculoviruses
    • Williams G.V., Faulkner P. Replication patterns and cytopathology of cells infected with baculoviruses. Cytotechnology 1996, 20(1-3):95-110. 10.1007/BF00350391.
    • (1996) Cytotechnology , vol.20 , Issue.1-3 , pp. 95-110
    • Williams, G.V.1    Faulkner, P.2
  • 316
    • 77953577950 scopus 로고    scopus 로고
    • The nuclear envelope at a glance
    • Wilson K.L., Berk J.M. The nuclear envelope at a glance. Journal of Cell Science 2010, 123(Pt. 12):1973-1978. 10.1242/jcs.019042.
    • (2010) Journal of Cell Science , vol.123 , pp. 1973-1978
    • Wilson, K.L.1    Berk, J.M.2
  • 318
    • 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. Journal of Virology 2009, 83(7):3115-3126. 10.1128/JVI.01462-08.
    • (2009) Journal of Virology , vol.83 , Issue.7 , pp. 3115-3126
    • Wisner, T.W.1    Wright, C.C.2    Kato, A.3
  • 321
    • 78649650714 scopus 로고    scopus 로고
    • Recognition of nuclear targeting signals by Karyopherin-beta proteins
    • Xu D., Farmer A., Chook Y.M. Recognition of nuclear targeting signals by Karyopherin-beta proteins. Current Opinion in Structural Biology 2010, 20(6):782-790. 10.1016/j.sbi.2010.09.008.
    • (2010) Current Opinion in Structural Biology , vol.20 , Issue.6 , pp. 782-790
    • Xu, D.1    Farmer, A.2    Chook, Y.M.3
  • 322
    • 71549173114 scopus 로고    scopus 로고
    • Acting out of character: Regulatory roles of nuclear pore complex proteins
    • Xylourgidis N., Fornerod M. Acting out of character: Regulatory roles of nuclear pore complex proteins. Developmental Cell 2009, 17(5):617-625. 10.1016/j.devcel.2009.10.015.
    • (2009) Developmental Cell , vol.17 , Issue.5 , pp. 617-625
    • Xylourgidis, N.1    Fornerod, M.2
  • 323
    • 33744931114 scopus 로고    scopus 로고
    • The putative terminase subunit of herpes simplex virus 1 encoded by UL28 is necessary and sufficient to mediate interaction between pUL15 and pUL33
    • Yang K., Baines J.D. The putative terminase subunit of herpes simplex virus 1 encoded by UL28 is necessary and sufficient to mediate interaction between pUL15 and pUL33. Journal of Virology 2006, 80(12):5733-5739. 10.1128/JVI.00125-06.
    • (2006) Journal of Virology , vol.80 , Issue.12 , pp. 5733-5739
    • Yang, K.1    Baines, J.D.2
  • 324
    • 80052149066 scopus 로고    scopus 로고
    • Selection of HSV capsids for envelopment involves interaction between capsid surface components pUL31, pUL17, and pUL25
    • Yang K., Baines J.D. Selection of HSV capsids for envelopment involves interaction between capsid surface components pUL31, pUL17, and pUL25. Proceedings of the National Academy of Sciences of the United States of America 2011, 108(34):14276-14281. 10.1073/pnas.1108564108.
    • (2011) Proceedings of the National Academy of Sciences of the United States of America , vol.108 , Issue.34 , pp. 14276-14281
    • Yang, K.1    Baines, J.D.2
  • 325
    • 37349102695 scopus 로고    scopus 로고
    • Temperature-sensitive mutations in the putative herpes simplex virus type 1 terminase subunits pUL15 and pUL33 preclude viral DNA cleavage/packaging and interaction with pUL28 at the nonpermissive temperature
    • Yang K., Poon A.P., Roizman B., Baines J.D. Temperature-sensitive mutations in the putative herpes simplex virus type 1 terminase subunits pUL15 and pUL33 preclude viral DNA cleavage/packaging and interaction with pUL28 at the nonpermissive temperature. Journal of Virology 2008, 82(1):487-494. 10.1128/JVI.01875-07.
    • (2008) Journal of Virology , vol.82 , Issue.1 , pp. 487-494
    • Yang, K.1    Poon, A.P.2    Roizman, B.3    Baines, J.D.4
  • 326
    • 84895427394 scopus 로고    scopus 로고
    • Association of herpes simplex virus pUL31 with capsid vertices and components of the capsid vertex-specific complex
    • Yang K., Wills E., Lim H.Y., Zhou Z.H., Baines J.D. Association of herpes simplex virus pUL31 with capsid vertices and components of the capsid vertex-specific complex. Journal of Virology 2014, 88(7):3815-3825. 10.1128/JVI.03175-13.
    • (2014) Journal of Virology , vol.88 , Issue.7 , pp. 3815-3825
    • Yang, K.1    Wills, E.2    Lim, H.Y.3    Zhou, Z.H.4    Baines, J.D.5
  • 327
    • 0028363978 scopus 로고
    • Primary structure analysis and lamin B and DNA binding of human LBR, an integral protein of the nuclear envelope inner membrane
    • Ye Q., Worman H.J. Primary structure analysis and lamin B and DNA binding of human LBR, an integral protein of the nuclear envelope inner membrane. The Journal of Biological Chemistry 1994, 269(15):11306-11311.
    • (1994) The Journal of Biological Chemistry , vol.269 , Issue.15 , pp. 11306-11311
    • Ye, Q.1    Worman, H.J.2
  • 328
    • 0032579608 scopus 로고    scopus 로고
    • Genetic analysis of the UL 15 gene locus for the putative terminase of herpes simplex virus type 1
    • Yu D., Weller S.K. Genetic analysis of the UL 15 gene locus for the putative terminase of herpes simplex virus type 1. Virology 1998, 243(1):32-44. 10.1006/viro.1998.9041.
    • (1998) Virology , vol.243 , Issue.1 , pp. 32-44
    • Yu, D.1    Weller, S.K.2
  • 329
    • 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
    • Yuan M., Huang Z., Wei D., Hu Z., Yang K., Pang Y. Identification of Autographa californica nucleopolyhedrovirus ac93 as a core gene and its requirement for intranuclear microvesicle formation and nuclear egress of nucleocapsids. Journal of Virology 2011, 85(22):11664-11674. 10.1128/JVI.05275-11.
    • (2011) Journal of Virology , vol.85 , Issue.22 , pp. 11664-11674
    • Yuan, M.1    Huang, Z.2    Wei, D.3    Hu, Z.4    Yang, K.5    Pang, Y.6
  • 330
    • 84950245174 scopus 로고    scopus 로고
    • Crystal structure of the herpesvirus nuclear egress complex provides insights into inner nuclear membrane remodelling
    • Zeev-Ben-Mordehai T., Weberruß M., Lorenz M., et al. Crystal structure of the herpesvirus nuclear egress complex provides insights into inner nuclear membrane remodelling. Cell Reports 2015, 13:2645-2652.
    • (2015) Cell Reports , vol.13 , pp. 2645-2652
    • Zeev-Ben-Mordehai, T.1    Weberruß, M.2    Lorenz, M.3
  • 332
    • 84863115605 scopus 로고    scopus 로고
    • Structure of Sad1-UNC84 homology (SUN) domain defines features of molecular bridge in nuclear envelope
    • Zhou Z., Du X., Cai Z., et al. Structure of Sad1-UNC84 homology (SUN) domain defines features of molecular bridge in nuclear envelope. The Journal of Biological Chemistry 2012, 287(8):5317-5326. 10.1074/jbc.M111.304543.
    • (2012) The Journal of Biological Chemistry , vol.287 , Issue.8 , pp. 5317-5326
    • Zhou, Z.1    Du, X.2    Cai, Z.3
  • 333
    • 78549234083 scopus 로고    scopus 로고
    • A unique redox-sensing sensor II motif in TorsinA plays a critical role in nucleotide and partner binding
    • Zhu L., Millen L., Mendoza J.L., Thomas P.J. A unique redox-sensing sensor II motif in TorsinA plays a critical role in nucleotide and partner binding. The Journal of Biological Chemistry 2010, 285(48):37271-37280. 10.1074/jbc.M110.123471.
    • (2010) The Journal of Biological Chemistry , vol.285 , Issue.48 , pp. 37271-37280
    • Zhu, L.1    Millen, L.2    Mendoza, J.L.3    Thomas, P.J.4
  • 334
    • 0032720875 scopus 로고    scopus 로고
    • Intracellular localization of the UL31 protein of herpes simplex virus type 2
    • Zhu H.Y., Yamada H., Jiang Y.M., Yamada M., Nishiyama Y. Intracellular localization of the UL31 protein of herpes simplex virus type 2. Archives of Virology 1999, 144(10):1923-1935.
    • (1999) Archives of Virology , vol.144 , Issue.10 , pp. 1923-1935
    • Zhu, H.Y.1    Yamada, H.2    Jiang, Y.M.3    Yamada, M.4    Nishiyama, Y.5
  • 335
    • 84938814797 scopus 로고    scopus 로고
    • Dimerization-induced allosteric changes of the oxyanion-hole loop activate the pseudorabies virus assemblin pUL26N, a herpesvirus serine protease
    • Zühlsdorf M., Werten S., Klupp B.G., Palm G.J., Mettenleiter T.C., Hinrichs W. Dimerization-induced allosteric changes of the oxyanion-hole loop activate the pseudorabies virus assemblin pUL26N, a herpesvirus serine protease. PLoS Pathogen 2015, 11(7):e1005045. 10.1371/journal.ppat.1005045.
    • (2015) PLoS Pathogen , vol.11 , Issue.7
    • Zühlsdorf, M.1    Werten, S.2    Klupp, B.G.3    Palm, G.J.4    Mettenleiter, T.C.5    Hinrichs, W.6


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