메뉴 건너뛰기




Volumn 299, Issue , 2012, Pages 117-159

Effect of viral infection on the nuclear envelope and nuclear pore complex

Author keywords

Apoptosis; Mitosis; Nuclear envelope; Nuclear lamina; Nuclear pore complex; Nuclear transport; Nucleoporin; Virology; Virus

Indexed keywords

NUCLEOPORIN; NUCLEOPORIN 214; NUCLEOPORIN 358; NUCLEOPORIN 62; NUCLEOPORIN 98; UNCLASSIFIED DRUG;

EID: 84865983670     PISSN: 19376448     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-394310-1.00003-5     Document Type: Chapter
Times cited : (24)

References (179)
  • 1
    • 0025083331 scopus 로고
    • Nuclear protein import in permeabilized mammalian cells requires soluble cytoplasmic factors
    • Adam S.A., Marr R.S., Gerace L. Nuclear protein import in permeabilized mammalian cells requires soluble cytoplasmic factors. J. Cell Biol. 1990, 111:807-816.
    • (1990) J. Cell Biol. , vol.111 , pp. 807-816
    • Adam, S.A.1    Marr, R.S.2    Gerace, L.3
  • 3
    • 78349297963 scopus 로고    scopus 로고
    • Revisiting HIV-1 uncoating
    • Arhel N. Revisiting HIV-1 uncoating. Retrovirology 2010, 7:96.
    • (2010) Retrovirology , vol.7 , pp. 96
    • Arhel, N.1
  • 4
    • 84855858712 scopus 로고    scopus 로고
    • Nuclear transport of baculovirus: revealing the nuclear pore complex passage
    • Au S., Pante N. Nuclear transport of baculovirus: revealing the nuclear pore complex passage. J. Struct. Biol. 2012, 177:90-98.
    • (2012) J. Struct. Biol. , vol.177 , pp. 90-98
    • Au, S.1    Pante, N.2
  • 5
    • 0036168869 scopus 로고    scopus 로고
    • Translation of polioviral mRNA is inhibited by cleavage of polypyrimidine tract-binding proteins executed by polioviral 3C(pro)
    • Back S.H., Kim Y.K., Kim W.J., Cho S., Oh H.R., Kim J.E., Jang S.K. Translation of polioviral mRNA is inhibited by cleavage of polypyrimidine tract-binding proteins executed by polioviral 3C(pro). J. Virol. 2002, 76:2529-2542.
    • (2002) J. Virol. , vol.76 , pp. 2529-2542
    • Back, S.H.1    Kim, Y.K.2    Kim, W.J.3    Cho, S.4    Oh, H.R.5    Kim, J.E.6    Jang, S.K.7
  • 7
    • 0033998692 scopus 로고    scopus 로고
    • Infectious entry pathway of adeno-associated virus and adeno-associated virus vectors
    • Bartlett J.S., Wilcher R., Samulski R.J. Infectious entry pathway of adeno-associated virus and adeno-associated virus vectors. J. Virol. 2000, 74:2777-2785.
    • (2000) J. Virol. , vol.74 , pp. 2777-2785
    • Bartlett, J.S.1    Wilcher, R.2    Samulski, R.J.3
  • 8
    • 0037059611 scopus 로고    scopus 로고
    • Nuclear envelope breakdown proceeds by microtubule-induced tearing of the lamina
    • Beaudouin J., Gerlich D., Daigle N., Eils R., Ellenberg J. Nuclear envelope breakdown proceeds by microtubule-induced tearing of the lamina. Cell 2002, 108:83-96.
    • (2002) Cell , vol.108 , pp. 83-96
    • Beaudouin, J.1    Gerlich, D.2    Daigle, N.3    Eils, R.4    Ellenberg, J.5
  • 9
    • 34948891095 scopus 로고    scopus 로고
    • Snapshots of nuclear pore complexes in action captured by cryo-electron tomography
    • Beck M., Lucic V., Forster F., Baumeister W., Medalia O. Snapshots of nuclear pore complexes in action captured by cryo-electron tomography. Nature 2007, 449:611-615.
    • (2007) Nature , vol.449 , pp. 611-615
    • Beck, M.1    Lucic, V.2    Forster, F.3    Baumeister, W.4    Medalia, O.5
  • 11
    • 4444274231 scopus 로고    scopus 로고
    • Bidirectional increase in permeability of nuclear envelope upon poliovirus infection and accompanying alterations of nuclear pores
    • Belov G.A., Lidsky P.V., Mikitas O.V., Egger D., Lukyanov K.A., Bienz K., Agol V.I. Bidirectional increase in permeability of nuclear envelope upon poliovirus infection and accompanying alterations of nuclear pores. J. Virol. 2004, 78:10166-10177.
    • (2004) J. Virol. , vol.78 , pp. 10166-10177
    • Belov, G.A.1    Lidsky, P.V.2    Mikitas, O.V.3    Egger, D.4    Lukyanov, K.A.5    Bienz, K.6    Agol, V.I.7
  • 13
    • 34447539077 scopus 로고    scopus 로고
    • Adenoviridae: the viruses and their replication
    • Lippincott Williams & Wilkins, Philadelphia, D.M. Knipe (Ed.)
    • Berk A. Adenoviridae: the viruses and their replication. Fields Virology 2007, 2355-2394. Lippincott Williams & Wilkins, Philadelphia. fifth ed. D.M. Knipe (Ed.).
    • (2007) Fields Virology , pp. 2355-2394
    • Berk, A.1
  • 14
    • 36249027278 scopus 로고    scopus 로고
    • Parvoviridae
    • Lippincott Williams & Wilkins, Philadelphia, D.M. Knipe (Ed.)
    • Berns K., Parrish C.R. Parvoviridae. Fields Virology 2007, 2437-2477. Lippincott Williams & Wilkins, Philadelphia. fifth ed. D.M. Knipe (Ed.).
    • (2007) Fields Virology , pp. 2437-2477
    • Berns, K.1    Parrish, C.R.2
  • 15
    • 33646018621 scopus 로고    scopus 로고
    • Roles for herpes simplex virus type 1 UL34 and US3 proteins in disrupting the nuclear lamina during herpes simplex virus type 1 egress
    • Bjerke S.L., Roller R.J. Roles for herpes simplex virus type 1 UL34 and US3 proteins in disrupting the nuclear lamina during herpes simplex virus type 1 egress. Virology 2006, 347:261-276.
    • (2006) Virology , vol.347 , pp. 261-276
    • Bjerke, S.L.1    Roller, R.J.2
  • 16
    • 40349092941 scopus 로고    scopus 로고
    • Covalent capture of kinase-specific phosphopeptides reveals Cdk1-cyclin B substrates
    • Blethrow J.D., Glavy J.S., Morgan D.O., Shokat K.M. Covalent capture of kinase-specific phosphopeptides reveals Cdk1-cyclin B substrates. Proc. Natl Acad. Sci. USA 2008, 105:1442-1447.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 1442-1447
    • Blethrow, J.D.1    Glavy, J.S.2    Morgan, D.O.3    Shokat, K.M.4
  • 17
    • 0030612604 scopus 로고    scopus 로고
    • Karyopherin beta2 mediates nuclear import of a mRNA binding protein
    • Bonifaci N., Moroianu J., Radu A., Blobel G. Karyopherin beta2 mediates nuclear import of a mRNA binding protein. Proc. Natl Acad. Sci. USA 1997, 94:5055-5060.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 5055-5060
    • Bonifaci, N.1    Moroianu, J.2    Radu, A.3    Blobel, G.4
  • 18
    • 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. Cell. Mol. Life Sci. 2001, 58:1781-1789.
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 1781-1789
    • Buendia, B.1    Courvalin, J.C.2    Collas, P.3
  • 19
    • 0033020265 scopus 로고    scopus 로고
    • Caspase-dependent proteolysis of integral and peripheral proteins of nuclear membranes and nuclear pore complex proteins during apoptosis
    • Buendia B., Santa-Maria A., Courvalin J.C. Caspase-dependent proteolysis of integral and peripheral proteins of nuclear membranes and nuclear pore complex proteins during apoptosis. J. Cell Sci. 1999, 112(Pt 11):1743-1753.
    • (1999) J. Cell Sci. , vol.112 , Issue.PART 11 , pp. 1743-1753
    • Buendia, B.1    Santa-Maria, A.2    Courvalin, J.C.3
  • 20
    • 84861995457 scopus 로고    scopus 로고
    • Trafficking to uncharted territory of the nuclear envelope
    • Burns L.T., Wente S.R. Trafficking to uncharted territory of the nuclear envelope. Curr. Opin. Cell Biol 2012.
    • (2012) Curr. Opin. Cell Biol
    • Burns, L.T.1    Wente, S.R.2
  • 22
    • 77949396630 scopus 로고    scopus 로고
    • Simian virus 40 infection triggers a balanced network that includes apoptotic, survival, and stress pathways
    • Butin-Israeli V., Drayman N., Oppenheim A. Simian virus 40 infection triggers a balanced network that includes apoptotic, survival, and stress pathways. J. Virol. 2010, 84:3431-3442.
    • (2010) J. Virol. , vol.84 , pp. 3431-3442
    • Butin-Israeli, V.1    Drayman, N.2    Oppenheim, A.3
  • 23
    • 0035834646 scopus 로고    scopus 로고
    • The docking of kinesins, KIF5B and KIF5C, to Ran-binding protein 2 (RanBP2) is mediated via a novel RanBP2 domain
    • Cai Y., Singh B.B., Aslanukov A., Zhao H., Ferreira P.A. The docking of kinesins, KIF5B and KIF5C, to Ran-binding protein 2 (RanBP2) is mediated via a novel RanBP2 domain. J. Biol. Chem. 2001, 276:41594-41602.
    • (2001) J. Biol. Chem. , vol.276 , pp. 41594-41602
    • Cai, Y.1    Singh, B.B.2    Aslanukov, A.3    Zhao, H.4    Ferreira, P.A.5
  • 24
    • 79959345921 scopus 로고    scopus 로고
    • The multifaceted poliovirus 2A protease: regulation of gene expression by picornavirus proteases
    • Castello A., Alvarez E., Carrasco L. The multifaceted poliovirus 2A protease: regulation of gene expression by picornavirus proteases. J. Biomed. Biotechnol. 2011, 2011:369648.
    • (2011) J. Biomed. Biotechnol. , vol.2011 , pp. 369648
    • Castello, A.1    Alvarez, E.2    Carrasco, L.3
  • 25
    • 70350367733 scopus 로고    scopus 로고
    • RNA nuclear export is blocked by poliovirus 2A protease and is concomitant with nucleoporin cleavage
    • Castello A., Izquierdo J.M., Welnowska E., Carrasco L. RNA nuclear export is blocked by poliovirus 2A protease and is concomitant with nucleoporin cleavage. J. Cell Sci. 2009, 122:3799-3809.
    • (2009) J. Cell Sci. , vol.122 , pp. 3799-3809
    • Castello, A.1    Izquierdo, J.M.2    Welnowska, E.3    Carrasco, L.4
  • 26
    • 0027340582 scopus 로고
    • The product of the UL31 gene of herpes simplex virus 1 is a nuclear phosphoprotein which partitions with the nuclear matrix
    • Chang Y.E., Roizman B. The product of the UL31 gene of herpes simplex virus 1 is a nuclear phosphoprotein which partitions with the nuclear matrix. J. Virol. 1993, 67:6348-6356.
    • (1993) J. Virol. , vol.67 , pp. 6348-6356
    • Chang, Y.E.1    Roizman, B.2
  • 27
    • 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. J. Virol. 1997, 71:8307-8315.
    • (1997) J. Virol. , vol.71 , pp. 8307-8315
    • Chang, Y.E.1    Van Sant, C.2    Krug, P.W.3    Sears, A.E.4    Roizman, B.5
  • 28
    • 0034087641 scopus 로고    scopus 로고
    • The polo-like kinase PLK-1 is required for nuclear envelope breakdown and the completion of meiosis in Caenorhabditis elegans
    • Chase D., Serafinas C., Ashcroft N., Kosinski M., Longo D., Ferris D.K., Golden A. The polo-like kinase PLK-1 is required for nuclear envelope breakdown and the completion of meiosis in Caenorhabditis elegans. Genesis 2000, 26:26-41.
    • (2000) Genesis , vol.26 , pp. 26-41
    • Chase, D.1    Serafinas, C.2    Ashcroft, N.3    Kosinski, M.4    Longo, D.5    Ferris, D.K.6    Golden, A.7
  • 29
    • 67349136342 scopus 로고    scopus 로고
    • RANBP2 is an allosteric activator of the conventional kinesin-1 motor protein, KIF5B, in a minimal cell-free system
    • Cho K.I., Yi H., Desai R., Hand A.R., Haas A.L., Ferreira P.A. RANBP2 is an allosteric activator of the conventional kinesin-1 motor protein, KIF5B, in a minimal cell-free system. EMBO Rep. 2009, 10:480-486.
    • (2009) EMBO Rep. , vol.10 , pp. 480-486
    • Cho, K.I.1    Yi, H.2    Desai, R.3    Hand, A.R.4    Haas, A.L.5    Ferreira, P.A.6
  • 30
    • 79960912049 scopus 로고    scopus 로고
    • Nuclear import by karyopherin-betas: recognition and inhibition
    • Chook Y.M., Suel K.E. Nuclear import by karyopherin-betas: recognition and inhibition. Biochim. Biophys. Acta 2011, 1813:1593-1606.
    • (2011) Biochim. Biophys. Acta , vol.1813 , pp. 1593-1606
    • Chook, Y.M.1    Suel, K.E.2
  • 32
    • 33750279611 scopus 로고    scopus 로고
    • Parvoviral nuclear import: bypassing the host nuclear-transport machinery
    • Cohen S., Behzad A.R., Carroll J.B., Pante N. Parvoviral nuclear import: bypassing the host nuclear-transport machinery. J. Gen. Virol. 2006, 87:3209-3213.
    • (2006) J. Gen. Virol. , vol.87 , pp. 3209-3213
    • Cohen, S.1    Behzad, A.R.2    Carroll, J.B.3    Pante, N.4
  • 33
    • 79955440194 scopus 로고    scopus 로고
    • Nuclear envelope disruption involving host caspases plays a role in the parvovirus replication cycle
    • Cohen S., Marr A.K., Garcin P., Pante N. Nuclear envelope disruption involving host caspases plays a role in the parvovirus replication cycle. J. Virol. 2011, 85:4863-4874.
    • (2011) J. Virol. , vol.85 , pp. 4863-4874
    • Cohen, S.1    Marr, A.K.2    Garcin, P.3    Pante, N.4
  • 34
    • 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., Pante N. Pushing the envelope: microinjection of Minute virus of mice into Xenopus oocytes causes damage to the nuclear envelope. J. Gen. Virol. 2005, 86:3243-3252.
    • (2005) J. Gen. Virol. , vol.86 , pp. 3243-3252
    • Cohen, S.1    Pante, N.2
  • 35
    • 85145128502 scopus 로고    scopus 로고
    • Structure and organization of the viral genome
    • Hodder Arnold, London, J.R. Kerr, S.F. Cotmore, M.E. Bloom, R.M. Linden, C.R. Parrish (Eds.)
    • Cotmore S.F., Tattersall P. Structure and organization of the viral genome. Parvoviruses 2006, 73-94. Hodder Arnold, London. J.R. Kerr, S.F. Cotmore, M.E. Bloom, R.M. Linden, C.R. Parrish (Eds.).
    • (2006) Parvoviruses , pp. 73-94
    • Cotmore, S.F.1    Tattersall, P.2
  • 36
    • 0026783801 scopus 로고
    • The lamin B receptor of the inner nuclear membrane undergoes mitosis-specific phosphorylation and is a substrate for p34cdc2-type protein kinase
    • Courvalin J.C., Segil N., Blobel G., Worman H.J. The lamin B receptor of the inner nuclear membrane undergoes mitosis-specific phosphorylation and is a substrate for p34cdc2-type protein kinase. J. Biol. Chem. 1992, 267:19035-19038.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19035-19038
    • Courvalin, J.C.1    Segil, N.2    Blobel, G.3    Worman, H.J.4
  • 40
  • 41
    • 70449701570 scopus 로고    scopus 로고
    • Double duty for nuclear proteins-the price of more open forms of mitosis
    • De Souza C.P., Osmani S.A. Double duty for nuclear proteins-the price of more open forms of mitosis. Trends Genet. 2009, 25:545-554.
    • (2009) Trends Genet. , vol.25 , pp. 545-554
    • De Souza, C.P.1    Osmani, S.A.2
  • 42
    • 0032541346 scopus 로고    scopus 로고
    • Detergent-salt resistance of LAP2alpha in interphase nuclei and phosphorylation-dependent association with chromosomes early in nuclear assembly implies functions in nuclear structure dynamics
    • Dechat T., Gotzmann J., Stockinger A., Harris C.A., Talle M.A., Siekierka J.J., Foisner R. Detergent-salt resistance of LAP2alpha in interphase nuclei and phosphorylation-dependent association with chromosomes early in nuclear assembly implies functions in nuclear structure dynamics. EMBO J. 1998, 17:4887-4902.
    • (1998) EMBO J. , vol.17 , pp. 4887-4902
    • Dechat, T.1    Gotzmann, J.2    Stockinger, A.3    Harris, C.A.4    Talle, M.A.5    Siekierka, J.J.6    Foisner, R.7
  • 43
    • 1842483901 scopus 로고    scopus 로고
    • The leader protein of Theiler's virus interferes with nucleocytoplasmic trafficking of cellular proteins
    • Delhaye S., van Pesch V., Michiels T. The leader protein of Theiler's virus interferes with nucleocytoplasmic trafficking of cellular proteins. J. Virol. 2004, 78:4357-4362.
    • (2004) J. Virol. , vol.78 , pp. 4357-4362
    • Delhaye, S.1    van Pesch, V.2    Michiels, T.3
  • 45
    • 0033587498 scopus 로고    scopus 로고
    • Identification of phosphorylation sites in native lamina-associated polypeptide 2 beta
    • Dreger M., Otto H., Neubauer G., Mann M., Hucho F. Identification of phosphorylation sites in native lamina-associated polypeptide 2 beta. Biochemistry 1999, 38:9426-9434.
    • (1999) Biochemistry , vol.38 , pp. 9426-9434
    • Dreger, M.1    Otto, H.2    Neubauer, G.3    Mann, M.4    Hucho, F.5
  • 46
    • 33749049426 scopus 로고    scopus 로고
    • The nuclear pore complex, nuclear transport, and apoptosis
    • Fahrenkrog B. The nuclear pore complex, nuclear transport, and apoptosis. Can. J. Physiol. Pharmacol. 2006, 84:279-286.
    • (2006) Can. J. Physiol. Pharmacol. , vol.84 , pp. 279-286
    • Fahrenkrog, B.1
  • 48
    • 28044448698 scopus 로고    scopus 로고
    • Parvoviral virions deploy a capsid-tethered lipolytic enzyme to breach the endosomal membrane during cell entry
    • Farr G.A., Zhang L.G., Tattersall P. Parvoviral virions deploy a capsid-tethered lipolytic enzyme to breach the endosomal membrane during cell entry. Proc. Natl. Acad. Sci. USA 2005, 102:17148-17153.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 17148-17153
    • Farr, G.A.1    Zhang, L.G.2    Tattersall, P.3
  • 49
    • 0029945130 scopus 로고    scopus 로고
    • Cell cycle-dependent phosphorylation of nucleoporins and nuclear pore membrane protein Gp210
    • Favreau C., Worman H.J., Wozniak R.W., Frappier T., Courvalin J.C. Cell cycle-dependent phosphorylation of nucleoporins and nuclear pore membrane protein Gp210. Biochemistry 1996, 35:8035-8044.
    • (1996) Biochemistry , vol.35 , pp. 8035-8044
    • Favreau, C.1    Worman, H.J.2    Wozniak, R.W.3    Frappier, T.4    Courvalin, J.C.5
  • 50
    • 27144464007 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport in apoptosis
    • Ferrando-May E. Nucleocytoplasmic transport in apoptosis. Cell Death Differ. 2005, 12:1263-1276.
    • (2005) Cell Death Differ. , vol.12 , pp. 1263-1276
    • Ferrando-May, E.1
  • 51
    • 0035007598 scopus 로고    scopus 로고
    • Caspases mediate nucleoporin cleavage, but not early redistribution of nuclear transport factors and modulation of nuclear permeability in apoptosis
    • Ferrando-May E., Cordes V., Biller-Ckovric I., Mirkovic J., Gorlich D., Nicotera P. Caspases mediate nucleoporin cleavage, but not early redistribution of nuclear transport factors and modulation of nuclear permeability in apoptosis. Cell Death Differ. 2001, 8:495-505.
    • (2001) Cell Death Differ. , vol.8 , pp. 495-505
    • Ferrando-May, E.1    Cordes, V.2    Biller-Ckovric, I.3    Mirkovic, J.4    Gorlich, D.5    Nicotera, P.6
  • 52
    • 0016426580 scopus 로고
    • Virus development in enucleate cells: echovirus, poliovirus, pseudorabies virus, reovirus, respiratory syncytial virus and Semliki Forest virus
    • Follett E.A., Pringle C.R., Pennington T.H. Virus development in enucleate cells: echovirus, poliovirus, pseudorabies virus, reovirus, respiratory syncytial virus and Semliki Forest virus. J. Gen. Virol. 1975, 26:183-196.
    • (1975) J. Gen. Virol. , vol.26 , pp. 183-196
    • Follett, E.A.1    Pringle, C.R.2    Pennington, T.H.3
  • 53
    • 34250372513 scopus 로고    scopus 로고
    • HIVs and their replication
    • Lippincott, Williams & Wilkins, Philadelphia, D.M. Knipe (Ed.)
    • Freed E.O., Martin M.A. HIVs and their replication. Fields Virology 2007, 2107-2186. Lippincott, Williams & Wilkins, Philadelphia. fifth ed. D.M. Knipe (Ed.).
    • (2007) Fields Virology , pp. 2107-2186
    • Freed, E.O.1    Martin, M.A.2
  • 54
    • 73249130542 scopus 로고    scopus 로고
    • Structural analysis of a metazoan nuclear pore complex reveals a fused concentric ring architecture
    • Frenkiel-Krispin D., Maco B., Aebi U., Medalia O. Structural analysis of a metazoan nuclear pore complex reveals a fused concentric ring architecture. J. Mol. Biol. 2010, 395:578-586.
    • (2010) J. Mol. Biol. , vol.395 , pp. 578-586
    • Frenkiel-Krispin, D.1    Maco, B.2    Aebi, U.3    Medalia, O.4
  • 55
    • 0042830859 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: taking an inventory
    • Fried H., Kutay U. Nucleocytoplasmic transport: taking an inventory. Cell Mol. Life Sci. 2003, 60:1659-1688.
    • (2003) Cell Mol. Life Sci. , vol.60 , pp. 1659-1688
    • Fried, H.1    Kutay, U.2
  • 57
    • 80051922904 scopus 로고    scopus 로고
    • Regulation of nucleocytoplasmic trafficking of viral proteins: an integral role in pathogenesis?
    • Fulcher A.J., Jans D.A. Regulation of nucleocytoplasmic trafficking of viral proteins: an integral role in pathogenesis?. Biochim. Biophys. Acta 2011, 1813:2176-2190.
    • (2011) Biochim. Biophys. Acta , vol.1813 , pp. 2176-2190
    • Fulcher, A.J.1    Jans, D.A.2
  • 58
    • 67650410025 scopus 로고    scopus 로고
    • Rhinovirus 3C protease can localize in the nucleus and alter active and passive nucleocytoplasmic transport
    • Ghildyal R., Jordan B., Li D., Dagher H., Bardin P.G., Gern J.E., Jans D.A. Rhinovirus 3C protease can localize in the nucleus and alter active and passive nucleocytoplasmic transport. J. Virol. 2009, 83:7349-7352.
    • (2009) J. Virol. , vol.83 , pp. 7349-7352
    • Ghildyal, R.1    Jordan, B.2    Li, D.3    Dagher, H.4    Bardin, P.G.5    Gern, J.E.6    Jans, D.A.7
  • 59
    • 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. J. Virol. 2012, 86:3180-3192.
    • (2012) J. Virol. , vol.86 , pp. 3180-3192
    • Giorda, K.M.1    Raghava, S.2    Hebert, D.N.3
  • 61
    • 0033708899 scopus 로고    scopus 로고
    • Caspase-mediated cleavage of the chromosome-binding domain of lamina-associated polypeptide 2 alpha
    • Gotzmann J., Vlcek S., Foisner R. Caspase-mediated cleavage of the chromosome-binding domain of lamina-associated polypeptide 2 alpha. J. Cell Sci. 2000, 113(Pt 21):3769-3780.
    • (2000) J. Cell Sci. , vol.113 , Issue.PART 21 , pp. 3769-3780
    • Gotzmann, J.1    Vlcek, S.2    Foisner, R.3
  • 64
    • 0029983628 scopus 로고    scopus 로고
    • The role of the adenovirus protease on virus entry into cells
    • Greber U.F., Webster P., Weber J., Helenius A. The role of the adenovirus protease on virus entry into cells. EMBO J. 1996, 15:1766-1777.
    • (1996) EMBO J. , vol.15 , pp. 1766-1777
    • Greber, U.F.1    Webster, P.2    Weber, J.3    Helenius, A.4
  • 65
    • 0027496645 scopus 로고
    • Stepwise dismantling of adenovirus 2 during entry into cells
    • Greber U.F., Willetts M., Webster P., Helenius A. Stepwise dismantling of adenovirus 2 during entry into cells. Cell 1993, 75:477-486.
    • (1993) Cell , vol.75 , pp. 477-486
    • Greber, U.F.1    Willetts, M.2    Webster, P.3    Helenius, A.4
  • 67
    • 0142091706 scopus 로고    scopus 로고
    • Inhibition of nucleo-cytoplasmic trafficking by RNA viruses: targeting the nuclear pore complex
    • Gustin K.E. Inhibition of nucleo-cytoplasmic trafficking by RNA viruses: targeting the nuclear pore complex. Virus Res. 2003, 95:35-44.
    • (2003) Virus Res. , vol.95 , pp. 35-44
    • Gustin, K.E.1
  • 68
    • 0035863125 scopus 로고    scopus 로고
    • Effects of poliovirus infection on nucleo-cytoplasmic trafficking and nuclear pore complex composition
    • Gustin K.E., Sarnow P. Effects of poliovirus infection on nucleo-cytoplasmic trafficking and nuclear pore complex composition. EMBO J. 2001, 20:240-249.
    • (2001) EMBO J. , vol.20 , pp. 240-249
    • Gustin, K.E.1    Sarnow, P.2
  • 69
    • 0036337963 scopus 로고    scopus 로고
    • Inhibition of nuclear import and alteration of nuclear pore complex composition by rhinovirus
    • Gustin K.E., Sarnow P. Inhibition of nuclear import and alteration of nuclear pore complex composition by rhinovirus. J. Virol. 2002, 76:8787-8796.
    • (2002) J. Virol. , vol.76 , pp. 8787-8796
    • Gustin, K.E.1    Sarnow, P.2
  • 70
    • 60749108426 scopus 로고    scopus 로고
    • Orchestrating nuclear envelope disassembly and reassembly during mitosis
    • Guttinger S., Laurell E., Kutay U. Orchestrating nuclear envelope disassembly and reassembly during mitosis. Nat. Rev. Mol. Cell Biol. 2009, 10:178-191.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 178-191
    • Guttinger, S.1    Laurell, E.2    Kutay, U.3
  • 71
    • 34047179437 scopus 로고    scopus 로고
    • Centrosomes promote timely mitotic entry in C. elegans embryos
    • Hachet V., Canard C., Gonczy P. Centrosomes promote timely mitotic entry in C. elegans embryos. Dev. Cell 2007, 12:531-541.
    • (2007) Dev. Cell , vol.12 , pp. 531-541
    • Hachet, V.1    Canard, C.2    Gonczy, P.3
  • 72
    • 0034759535 scopus 로고    scopus 로고
    • Infection of purified nuclei by adeno-associated virus 2
    • Hansen J., Qing K., Srivastava A. Infection of purified nuclei by adeno-associated virus 2. Mol. Ther. 2001, 4:289-296.
    • (2001) Mol. Ther. , vol.4 , pp. 289-296
    • Hansen, J.1    Qing, K.2    Srivastava, A.3
  • 73
    • 70549089770 scopus 로고    scopus 로고
    • Cellular and nuclear degradation during apoptosis
    • He B., Lu N., Zhou Z. Cellular and nuclear degradation during apoptosis. Curr. Opin. Cell Biol. 2009, 21:900-912.
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 900-912
    • He, B.1    Lu, N.2    Zhou, Z.3
  • 74
    • 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, 61:579-589.
    • (1990) Cell , vol.61 , pp. 579-589
    • Heald, R.1    McKeon, F.2
  • 75
    • 0027172207 scopus 로고
    • A cytoplasmic 57-kDa protein that is required for translation of picornavirus RNA by internal ribosomal entry is identical to the nuclear pyrimidine tract-binding protein
    • Hellen C.U., Witherell G.W., Schmid M., Shin S.H., Pestova T.V., Gil A., Wimmer E. A cytoplasmic 57-kDa protein that is required for translation of picornavirus RNA by internal ribosomal entry is identical to the nuclear pyrimidine tract-binding protein. Proc. Natl Acad. Sci. USA 1993, 90:7642-7646.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 7642-7646
    • Hellen, C.U.1    Witherell, G.W.2    Schmid, M.3    Shin, S.H.4    Pestova, T.V.5    Gil, A.6    Wimmer, E.7
  • 77
  • 78
    • 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. J. Virol. 2008, 82:8392-8399.
    • (2008) J. Virol. , vol.82 , pp. 8392-8399
    • Hofemeister, H.1    O'Hare, P.2
  • 79
    • 33745032590 scopus 로고    scopus 로고
    • Caspase 3, periodically expressed and activated at G2/M transition, is required for nocodazole-induced mitotic checkpoint
    • Hsu S.L., Yu C.T., Yin S.C., Tang M.J., Tien A.C., Wu Y.M., Huang C.Y. Caspase 3, periodically expressed and activated at G2/M transition, is required for nocodazole-induced mitotic checkpoint. Apoptosis 2006, 11:765-771.
    • (2006) Apoptosis , vol.11 , pp. 765-771
    • Hsu, S.L.1    Yu, C.T.2    Yin, S.C.3    Tang, M.J.4    Tien, A.C.5    Wu, Y.M.6    Huang, C.Y.7
  • 80
    • 76349121992 scopus 로고    scopus 로고
    • Minor capsid proteins of mouse polyomavirus are inducers of apoptosis when produced individually but are only moderate contributors to cell death during the late phase of viral infection
    • Huerfano S., Zila V., Boura E., Spanielova H., Stokrova J., Forstova J. Minor capsid proteins of mouse polyomavirus are inducers of apoptosis when produced individually but are only moderate contributors to cell death during the late phase of viral infection. FEBS J. 2010, 277:1270-1283.
    • (2010) FEBS J. , vol.277 , pp. 1270-1283
    • Huerfano, S.1    Zila, V.2    Boura, E.3    Spanielova, H.4    Stokrova, J.5    Forstova, J.6
  • 81
    • 36749064529 scopus 로고    scopus 로고
    • Polyomaviruses
    • Lippincott Williams & Wilkins, Philadelphia, D.M. Knipe (Ed.)
    • Imperiale M.J., Major E.O. Polyomaviruses. Fields Virology 2007, 2263-2394. Lippincott Williams & Wilkins, Philadelphia. fifth ed. D.M. Knipe (Ed.).
    • (2007) Fields Virology , pp. 2263-2394
    • Imperiale, M.J.1    Major, E.O.2
  • 82
    • 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. Nat. Rev. Microbiol. 2011, 9:382-394.
    • (2011) Nat. Rev. Microbiol. , vol.9 , pp. 382-394
    • Johnson, D.C.1    Baines, J.D.2
  • 84
    • 0034757949 scopus 로고    scopus 로고
    • Sequential degradation of proteins from the nuclear envelope during apoptosis
    • Kihlmark M., Imreh G., Hallberg E. Sequential degradation of proteins from the nuclear envelope during apoptosis. J. Cell Sci. 2001, 114:3643-3653.
    • (2001) J. Cell Sci. , vol.114 , pp. 3643-3653
    • Kihlmark, M.1    Imreh, G.2    Hallberg, E.3
  • 85
    • 0347722245 scopus 로고    scopus 로고
    • Correlation between nucleocytoplasmic transport and caspase-3-dependent dismantling of nuclear pores during apoptosis
    • Kihlmark M., Rustum C., Eriksson C., Beckman M., Iverfeldt K., Hallberg E. Correlation between nucleocytoplasmic transport and caspase-3-dependent dismantling of nuclear pores during apoptosis. Exp. Cell Res. 2004, 293:346-356.
    • (2004) Exp. Cell Res. , vol.293 , pp. 346-356
    • Kihlmark, M.1    Rustum, C.2    Eriksson, C.3    Beckman, M.4    Iverfeldt, K.5    Hallberg, E.6
  • 87
    • 79960454923 scopus 로고    scopus 로고
    • Dismantling the NPC permeability barrier at the onset of mitosis
    • Laurell E., Kutay U. Dismantling the NPC permeability barrier at the onset of mitosis. Cell Cycle 2011, 10:2243-2245.
    • (2011) Cell Cycle , vol.10 , pp. 2243-2245
    • Laurell, E.1    Kutay, U.2
  • 88
    • 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, 406:127-137.
    • (2010) Virology , vol.406 , pp. 127-137
    • Leach, N.R.1    Roller, R.J.2
  • 89
    • 77953302554 scopus 로고    scopus 로고
    • Escape of herpesviruses from the nucleus
    • Lee C.P., Chen M.R. Escape of herpesviruses from the nucleus. Rev. Med. Virol. 2010, 20:214-230.
    • (2010) Rev. Med. Virol. , vol.20 , pp. 214-230
    • Lee, C.P.1    Chen, M.R.2
  • 91
    • 34548236927 scopus 로고    scopus 로고
    • Intracellular trafficking of adenovirus: many means to many ends
    • Leopold P.L., Crystal R.G. Intracellular trafficking of adenovirus: many means to many ends. Adv. Drug Deliv. Rev. 2007, 59:810-821.
    • (2007) Adv. Drug Deliv. Rev. , vol.59 , pp. 810-821
    • Leopold, P.L.1    Crystal, R.G.2
  • 92
    • 79851486019 scopus 로고    scopus 로고
    • Insights into cellular factors that regulate HIV-1 replication in human cells
    • Lever A.M., Jeang K.T. Insights into cellular factors that regulate HIV-1 replication in human cells. Biochemistry 2011, 50:920-931.
    • (2011) Biochemistry , vol.50 , pp. 920-931
    • Lever, A.M.1    Jeang, K.T.2
  • 94
    • 0042196107 scopus 로고    scopus 로고
    • The COPI complex functions in nuclear envelope breakdown and is recruited by the nucleoporin Nup153
    • Liu J., Prunuske A.J., Fager A.M., Ullman K.S. The COPI complex functions in nuclear envelope breakdown and is recruited by the nucleoporin Nup153. Dev. Cell 2003, 5:487-498.
    • (2003) Dev. Cell , vol.5 , pp. 487-498
    • Liu, J.1    Prunuske, A.J.2    Fager, A.M.3    Ullman, K.S.4
  • 95
    • 44449129923 scopus 로고    scopus 로고
    • Nuclear pore composition regulates neural stem/progenitor cell differentiation in the mouse embryo
    • Lupu F., Alves A., Anderson K., Doye V., Lacy E. Nuclear pore composition regulates neural stem/progenitor cell differentiation in the mouse embryo. Dev. Cell 2008, 14:831-842.
    • (2008) Dev. Cell , vol.14 , pp. 831-842
    • Lupu, F.1    Alves, A.2    Anderson, K.3    Doye, V.4    Lacy, E.5
  • 97
    • 0028853451 scopus 로고
    • Differential mitotic phosphorylation of proteins of the nuclear pore complex
    • Macaulay C., Meier E., Forbes D.J. Differential mitotic phosphorylation of proteins of the nuclear pore complex. J. Biol. Chem. 1995, 270:254-262.
    • (1995) J. Biol. Chem. , vol.270 , pp. 254-262
    • Macaulay, C.1    Meier, E.2    Forbes, D.J.3
  • 98
    • 26944450514 scopus 로고    scopus 로고
    • ERp29 triggers a conformational change in polyomavirus to stimulate membrane binding
    • Magnuson B., Rainey E.K., Benjamin T., Baryshev M., Mkrtchian S., Tsai B. ERp29 triggers a conformational change in polyomavirus to stimulate membrane binding. Mol. Cell 2005, 20:289-300.
    • (2005) Mol. Cell , vol.20 , pp. 289-300
    • Magnuson, B.1    Rainey, E.K.2    Benjamin, T.3    Baryshev, M.4    Mkrtchian, S.5    Tsai, B.6
  • 99
    • 30344459715 scopus 로고    scopus 로고
    • Low pH-dependent endosomal processing of the incoming parvovirus minute virus of mice virion leads to externalization of the VP1 N-terminal sequence (N-VP1), N-VP2 cleavage, and uncoating of the full-length genome
    • Mani B., Baltzer C., Valle N., Almendral J.M., Kempf C., Ros C. Low pH-dependent endosomal processing of the incoming parvovirus minute virus of mice virion leads to externalization of the VP1 N-terminal sequence (N-VP1), N-VP2 cleavage, and uncoating of the full-length genome. J. Virol. 2006, 80:1015-1024.
    • (2006) J. Virol. , vol.80 , pp. 1015-1024
    • Mani, B.1    Baltzer, C.2    Valle, N.3    Almendral, J.M.4    Kempf, C.5    Ros, C.6
  • 101
    • 0029911783 scopus 로고    scopus 로고
    • Human protein Sam68 relocalization and interaction with poliovirus RNA polymerase in infected cells
    • McBride A.E., Schlegel A., Kirkegaard K. Human protein Sam68 relocalization and interaction with poliovirus RNA polymerase in infected cells. Proc. Natl Acad. Sci. USA 1996, 93:2296-2301.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 2296-2301
    • McBride, A.E.1    Schlegel, A.2    Kirkegaard, K.3
  • 103
    • 0036148284 scopus 로고    scopus 로고
    • Herpesvirus assembly and egress
    • Mettenleiter T.C. Herpesvirus assembly and egress. J. Virol. 2002, 76:1537-1547.
    • (2002) J. Virol. , vol.76 , pp. 1537-1547
    • Mettenleiter, T.C.1
  • 104
    • 0026325508 scopus 로고
    • Cell-free, de novo synthesis of poliovirus
    • Molla A., Paul A.V., Wimmer E. Cell-free, de novo synthesis of poliovirus. Science 1991, 254:1647-1651.
    • (1991) Science , vol.254 , pp. 1647-1651
    • Molla, A.1    Paul, A.V.2    Wimmer, E.3
  • 105
    • 71449106849 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 (HIV-1) induces the cytoplasmic retention of heterogeneous nuclear ribonucleoprotein A1 by disrupting nuclear import: implications for HIV-1 gene expression
    • Monette A., Ajamian L., Lopez-Lastra M., Mouland A.J. Human immunodeficiency virus type 1 (HIV-1) induces the cytoplasmic retention of heterogeneous nuclear ribonucleoprotein A1 by disrupting nuclear import: implications for HIV-1 gene expression. J. Biol. Chem. 2009, 284:31350-31362.
    • (2009) J. Biol. Chem. , vol.284 , pp. 31350-31362
    • Monette, A.1    Ajamian, L.2    Lopez-Lastra, M.3    Mouland, A.J.4
  • 106
    • 79958238205 scopus 로고    scopus 로고
    • HIV-1 remodels the nuclear pore complex
    • Monette A., Pante N., Mouland A.J. HIV-1 remodels the nuclear pore complex. J. Cell Biol. 2011, 193:619-631.
    • (2011) J. Cell Biol. , vol.193 , pp. 619-631
    • Monette, A.1    Pante, N.2    Mouland, A.J.3
  • 107
    • 34247642597 scopus 로고    scopus 로고
    • Herpes simplex virus infection induces phosphorylation and delocalization of emerin, a key inner nuclear membrane protein
    • Morris J.B., Hofemeister H., O'Hare P. Herpes simplex virus infection induces phosphorylation and delocalization of emerin, a key inner nuclear membrane protein. J. Virol. 2007, 81:4429-4437.
    • (2007) J. Virol. , vol.81 , pp. 4429-4437
    • Morris, J.B.1    Hofemeister, H.2    O'Hare, P.3
  • 108
    • 83455228341 scopus 로고    scopus 로고
    • Breach of the nuclear lamina during assembly of herpes simplex viruses
    • Morrison L.A., Delassus G.S. Breach of the nuclear lamina during assembly of herpes simplex viruses. Nucleus 2011, 2.
    • (2011) Nucleus , vol.2
    • Morrison, L.A.1    Delassus, G.S.2
  • 109
    • 34249939914 scopus 로고    scopus 로고
    • US3 of herpes simplex virus type 1 encodes a promiscuous protein kinase that phosphorylates and alters localization of lamin A/C in infected cells
    • Mou F., Forest T., Baines J.D. US3 of herpes simplex virus type 1 encodes a promiscuous protein kinase that phosphorylates and alters localization of lamin A/C in infected cells. J. Virol. 2007, 81:6459-6470.
    • (2007) J. Virol. , vol.81 , pp. 6459-6470
    • Mou, F.1    Forest, T.2    Baines, J.D.3
  • 110
    • 34547959246 scopus 로고    scopus 로고
    • An in vitro nuclear disassembly system reveals a role for the RanGTPase system and microtubule-dependent steps in nuclear envelope breakdown
    • Muhlhausser P., Kutay U. An in vitro nuclear disassembly system reveals a role for the RanGTPase system and microtubule-dependent steps in nuclear envelope breakdown. J. Cell Biol. 2007, 178:595-610.
    • (2007) J. Cell Biol. , vol.178 , pp. 595-610
    • Muhlhausser, P.1    Kutay, U.2
  • 111
    • 0033942486 scopus 로고    scopus 로고
    • The first step of adenovirus type 2 disassembly occurs at the cell surface, independently of endocytosis and escape to the cytosol
    • Nakano M.Y., Boucke K., Suomalainen M., Stidwill R.P., Greber U.F. The first step of adenovirus type 2 disassembly occurs at the cell surface, independently of endocytosis and escape to the cytosol. J. Virol. 2000, 74:7085-7095.
    • (2000) J. Virol. , vol.74 , pp. 7085-7095
    • Nakano, M.Y.1    Boucke, K.2    Suomalainen, M.3    Stidwill, R.P.4    Greber, U.F.5
  • 112
    • 19944423114 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 enters human epidermal keratinocytes, but not neurons, via a pH-dependent endocytic pathway
    • Nicola A.V., Hou J., Major E.O., Straus S.E. Herpes simplex virus type 1 enters human epidermal keratinocytes, but not neurons, via a pH-dependent endocytic pathway. J. Virol. 2005, 79:7609-7616.
    • (2005) J. Virol. , vol.79 , pp. 7609-7616
    • Nicola, A.V.1    Hou, J.2    Major, E.O.3    Straus, S.E.4
  • 113
    • 0346992146 scopus 로고    scopus 로고
    • Limited expression of nuclear pore membrane glycoprotein 210 in cell lines and tissues suggests cell-type specific nuclear pores in metazoans
    • Olsson M., Scheele S., Ekblom P. Limited expression of nuclear pore membrane glycoprotein 210 in cell lines and tissues suggests cell-type specific nuclear pores in metazoans. Exp. Cell Res. 2004, 292:359-370.
    • (2004) Exp. Cell Res. , vol.292 , pp. 359-370
    • Olsson, M.1    Scheele, S.2    Ekblom, P.3
  • 114
    • 27644495950 scopus 로고    scopus 로고
    • Cdk1 and okadaic acid-sensitive phosphatases control assembly of nuclear pore complexes in Drosophila embryos
    • Onischenko E.A., Gubanova N.V., Kiseleva E.V., Hallberg E. Cdk1 and okadaic acid-sensitive phosphatases control assembly of nuclear pore complexes in Drosophila embryos. Mol. Biol. Cell 2005, 16:5152-5162.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5152-5162
    • Onischenko, E.A.1    Gubanova, N.V.2    Kiseleva, E.V.3    Hallberg, E.4
  • 115
  • 116
    • 0036175701 scopus 로고    scopus 로고
    • Nuclear pore complex is able to transport macromolecules with diameters of about 39 nm
    • Pante N., Kann M. Nuclear pore complex is able to transport macromolecules with diameters of about 39 nm. Mol. Biol. Cell 2002, 13:425-434.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 425-434
    • Pante, N.1    Kann, M.2
  • 117
    • 38849138626 scopus 로고    scopus 로고
    • Differential targeting of nuclear pore complex proteins in poliovirus-infected cells
    • Park N., Katikaneni P., Skern T., Gustin K.E. Differential targeting of nuclear pore complex proteins in poliovirus-infected cells. J. Virol. 2008, 82:1647-1655.
    • (2008) J. Virol. , vol.82 , pp. 1647-1655
    • Park, N.1    Katikaneni, P.2    Skern, T.3    Gustin, K.E.4
  • 118
    • 77956511212 scopus 로고    scopus 로고
    • Specific cleavage of the nuclear pore complex protein Nup62 by a viral protease
    • Park N., Skern T., Gustin K.E. Specific cleavage of the nuclear pore complex protein Nup62 by a viral protease. J. Biol. Chem. 2010, 285:28796-28805.
    • (2010) J. Biol. Chem. , vol.285 , pp. 28796-28805
    • Park, N.1    Skern, T.2    Gustin, K.E.3
  • 119
    • 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. J. Virol. 2006, 80:494-504.
    • (2006) J. Virol. , vol.80 , pp. 494-504
    • Park, R.1    Baines, J.D.2
  • 120
    • 0033937284 scopus 로고    scopus 로고
    • Cellular uptake and infection by canine parvovirus involves rapid dynamin-regulated clathrin-mediated endocytosis, followed by slower intracellular trafficking
    • Parker J.S., Parrish C.R. Cellular uptake and infection by canine parvovirus involves rapid dynamin-regulated clathrin-mediated endocytosis, followed by slower intracellular trafficking. J. Virol. 2000, 74:1919-1930.
    • (2000) J. Virol. , vol.74 , pp. 1919-1930
    • Parker, J.S.1    Parrish, C.R.2
  • 122
    • 0035017308 scopus 로고    scopus 로고
    • Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER
    • Pelkmans L., Kartenbeck J., Helenius A. Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER. Nat. Cell Biol. 2001, 3:473-483.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 473-483
    • Pelkmans, L.1    Kartenbeck, J.2    Helenius, A.3
  • 123
    • 0031557389 scopus 로고    scopus 로고
    • Molecular interactions between the importin alpha/beta heterodimer and proteins involved in vertebrate nuclear protein import
    • Percipalle P., Clarkson W.D., Kent H.M., Rhodes D., Stewart M. Molecular interactions between the importin alpha/beta heterodimer and proteins involved in vertebrate nuclear protein import. J. Mol. Biol. 1997, 266:722-732.
    • (1997) J. Mol. Biol. , vol.266 , pp. 722-732
    • Percipalle, P.1    Clarkson, W.D.2    Kent, H.M.3    Rhodes, D.4    Stewart, M.5
  • 124
    • 0025370462 scopus 로고
    • In vitro disassembly of the nuclear lamina and M phase-specific phosphorylation of lamins by cdc2 kinase
    • Peter M., Nakagawa J., Doree M., Labbe J.C., Nigg E.A. In vitro disassembly of the nuclear lamina and M phase-specific phosphorylation of lamins by cdc2 kinase. Cell 1990, 61:591-602.
    • (1990) Cell , vol.61 , pp. 591-602
    • Peter, M.1    Nakagawa, J.2    Doree, M.3    Labbe, J.C.4    Nigg, E.A.5
  • 125
    • 34347243476 scopus 로고    scopus 로고
    • Single-molecule fluorescence analysis of cellular nanomachinery components
    • Peters R. Single-molecule fluorescence analysis of cellular nanomachinery components. Annu. Rev. Biophys. Biomol. Struct. 2007, 36:371-394.
    • (2007) Annu. Rev. Biophys. Biomol. Struct. , vol.36 , pp. 371-394
    • Peters, R.1
  • 126
    • 0026527447 scopus 로고
    • Shuttling of pre-mRNA binding proteins between nucleus and cytoplasm
    • Pinol-Roma S., Dreyfuss G. Shuttling of pre-mRNA binding proteins between nucleus and cytoplasm. Nature 1992, 355:730-732.
    • (1992) Nature , vol.355 , pp. 730-732
    • Pinol-Roma, S.1    Dreyfuss, G.2
  • 128
    • 69249100500 scopus 로고    scopus 로고
    • Human caspases: activation, specificity, and regulation
    • Pop C., Salvesen G.S. Human caspases: activation, specificity, and regulation. J. Biol. Chem. 2009, 284:21777-21781.
    • (2009) J. Biol. Chem. , vol.284 , pp. 21777-21781
    • Pop, C.1    Salvesen, G.S.2
  • 129
    • 33747625216 scopus 로고    scopus 로고
    • A picornavirus protein interacts with Ran-GTPase and disrupts nucleocytoplasmic transport
    • Porter F.W., Bochkov Y.A., Albee A.J., Wiese C., Palmenberg A.C. A picornavirus protein interacts with Ran-GTPase and disrupts nucleocytoplasmic transport. Proc. Natl Acad. Sci. USA 2006, 103:12417-12422.
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 12417-12422
    • Porter, F.W.1    Bochkov, Y.A.2    Albee, A.J.3    Wiese, C.4    Palmenberg, A.C.5
  • 130
    • 78649423065 scopus 로고    scopus 로고
    • Nucleoporin phosphorylation triggered by the encephalomyocarditis virus leader protein is mediated by mitogen-activated protein kinases
    • Porter F.W., Brown B., Palmenberg A.C. Nucleoporin phosphorylation triggered by the encephalomyocarditis virus leader protein is mediated by mitogen-activated protein kinases. J. Virol. 2010, 84:12538-12548.
    • (2010) J. Virol. , vol.84 , pp. 12538-12548
    • Porter, F.W.1    Brown, B.2    Palmenberg, A.C.3
  • 131
    • 59649088827 scopus 로고    scopus 로고
    • Leader-induced phosphorylation of nucleoporins correlates with nuclear trafficking inhibition by cardioviruses
    • Porter F.W., Palmenberg A.C. Leader-induced phosphorylation of nucleoporins correlates with nuclear trafficking inhibition by cardioviruses. J. Virol. 2009, 83:1941-1951.
    • (2009) J. Virol. , vol.83 , pp. 1941-1951
    • Porter, F.W.1    Palmenberg, A.C.2
  • 132
  • 133
    • 0028906840 scopus 로고
    • Reconstituted nuclei depleted of a vertebrate GLFG nuclear pore protein, p97, import but are defective in nuclear growth and replication
    • Powers M.A., Macaulay C., Masiarz F.R., Forbes D.J. Reconstituted nuclei depleted of a vertebrate GLFG nuclear pore protein, p97, import but are defective in nuclear growth and replication. J. Cell Biol. 1995, 128:721-736.
    • (1995) J. Cell Biol. , vol.128 , pp. 721-736
    • Powers, M.A.1    Macaulay, C.2    Masiarz, F.R.3    Forbes, D.J.4
  • 134
    • 0042692926 scopus 로고    scopus 로고
    • Nuclear import of hepatitis B virus capsids and release of the viral genome
    • Rabe B., Vlachou A., Pante N., Helenius A., Kann M. Nuclear import of hepatitis B virus capsids and release of the viral genome. Proc. Natl Acad. Sci. USA 2003, 100:9849-9854.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 9849-9854
    • Rabe, B.1    Vlachou, A.2    Pante, N.3    Helenius, A.4    Kann, M.5
  • 135
    • 7944236264 scopus 로고    scopus 로고
    • Mapping the dynamic organization of the nuclear pore complex inside single living cells
    • Rabut G., Doye V., Ellenberg J. Mapping the dynamic organization of the nuclear pore complex inside single living cells. Nat. Cell Biol. 2004, 6:1114-1121.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 1114-1121
    • Rabut, G.1    Doye, V.2    Ellenberg, J.3
  • 136
    • 79959832190 scopus 로고    scopus 로고
    • The SV40 late protein VP4 is a viroporin that forms pores to disrupt membranes for viral release
    • Raghava S., Giorda K.M., Romano F.B., Heuck A.P., Hebert D.N. The SV40 late protein VP4 is a viroporin that forms pores to disrupt membranes for viral release. PLoS Pathog. 2011, 7:e1002116.
    • (2011) PLoS Pathog. , vol.7
    • Raghava, S.1    Giorda, K.M.2    Romano, F.B.3    Heuck, A.P.4    Hebert, D.N.5
  • 137
    • 36348964305 scopus 로고    scopus 로고
    • A chaperone-activated nonenveloped virus perforates the physiologically relevant endoplasmic reticulum membrane
    • Rainey-Barger E.K., Magnuson B., Tsai B. A chaperone-activated nonenveloped virus perforates the physiologically relevant endoplasmic reticulum membrane. J. Virol. 2007, 81:12996-13004.
    • (2007) J. Virol. , vol.81 , pp. 12996-13004
    • Rainey-Barger, E.K.1    Magnuson, B.2    Tsai, B.3
  • 138
    • 0025247954 scopus 로고
    • Correlation between structure and mass distribution of the nuclear pore complex and of distinct pore complex components
    • Reichelt R., Holzenburg A., Buhle E.L., Jarnik M., Engel A., Aebi U. Correlation between structure and mass distribution of the nuclear pore complex and of distinct pore complex components. J. Cell Biol. 1990, 110:883-894.
    • (1990) J. Cell Biol. , vol.110 , pp. 883-894
    • Reichelt, R.1    Holzenburg, A.2    Buhle, E.L.3    Jarnik, M.4    Engel, A.5    Aebi, U.6
  • 140
    • 33748948262 scopus 로고    scopus 로고
    • Reconstitution of herpes simplex virus type 1 nuclear capsid egress in vitro
    • Remillard-Labrosse G., Guay G., Lippe R. Reconstitution of herpes simplex virus type 1 nuclear capsid egress in vitro. J. Virol. 2006, 80:9741-9753.
    • (2006) J. Virol. , vol.80 , pp. 9741-9753
    • Remillard-Labrosse, G.1    Guay, G.2    Lippe, R.3
  • 141
    • 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. J. Virol. 2004, 78:5564-5575.
    • (2004) J. Virol. , vol.78 , pp. 5564-5575
    • Reynolds, A.E.1    Liang, L.2    Baines, J.D.3
  • 142
    • 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. J. Virol. 2001, 75:8803-8817.
    • (2001) J. Virol. , vol.75 , pp. 8803-8817
    • Reynolds, A.E.1    Ryckman, B.J.2    Baines, J.D.3    Zhou, Y.4    Liang, L.5    Roller, R.J.6
  • 143
    • 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. J. Virol. 2002, 76:8939-8952.
    • (2002) J. Virol. , vol.76 , pp. 8939-8952
    • Reynolds, A.E.1    Wills, E.G.2    Roller, R.J.3    Ryckman, B.J.4    Baines, J.D.5
  • 145
    • 34249950342 scopus 로고    scopus 로고
    • Herpes simplex viruses
    • Lippincott Williams & Wilkins, Philadelphia, D.M. Knipe, P.M. Howley (Eds.)
    • Roizman B., Knipe D.M., Whitley R.J. Herpes simplex viruses. Fields Virology 2007, 2501-2601. Lippincott Williams & Wilkins, Philadelphia. fifth ed. D.M. Knipe, P.M. Howley (Eds.).
    • (2007) Fields Virology , pp. 2501-2601
    • Roizman, B.1    Knipe, D.M.2    Whitley, R.J.3
  • 146
    • 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. J. Virol. 2000, 74:117-129.
    • (2000) J. Virol. , vol.74 , pp. 117-129
    • Roller, R.J.1    Zhou, Y.2    Schnetzer, R.3    Ferguson, J.4    DeSalvo, D.5
  • 147
  • 148
    • 0027366167 scopus 로고
    • Isolation of the yeast nuclear pore complex
    • Rout M.P., Blobel G. Isolation of the yeast nuclear pore complex. J. Cell Biol. 1993, 123:771-783.
    • (1993) J. Cell Biol. , vol.123 , pp. 771-783
    • Rout, M.P.1    Blobel, G.2
  • 150
    • 0029973561 scopus 로고    scopus 로고
    • A yeast acetyl coenzyme A carboxylase mutant links very-long-chain fatty acid synthesis to the structure and function of the nuclear membrane-pore complex
    • Schneiter R., Hitomi M., Ivessa A.S., Fasch E.V., Kohlwein S.D., Tartakoff A.M. A yeast acetyl coenzyme A carboxylase mutant links very-long-chain fatty acid synthesis to the structure and function of the nuclear membrane-pore complex. Mol. Cell Biol. 1996, 16:7161-7172.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 7161-7172
    • Schneiter, R.1    Hitomi, M.2    Ivessa, A.S.3    Fasch, E.V.4    Kohlwein, S.D.5    Tartakoff, A.M.6
  • 151
    • 0035976603 scopus 로고    scopus 로고
    • Real-time single-molecule imaging of the infection pathway of an adeno-associated virus
    • Seisenberger G., Ried M.U., Endress T., Buning H., Hallek M., Brauchle C. Real-time single-molecule imaging of the infection pathway of an adeno-associated virus. Science 2001, 294:1929-1932.
    • (2001) Science , vol.294 , pp. 1929-1932
    • Seisenberger, G.1    Ried, M.U.2    Endress, T.3    Buning, H.4    Hallek, M.5    Brauchle, C.6
  • 152
    • 0033789521 scopus 로고    scopus 로고
    • The UL34 gene product of herpes simplex virus type 2 is a tail-anchored type II membrane protein that is significant for virus envelopment
    • Shiba C., Daikoku T., Goshima F., Takakuwa H., Yamauchi Y., Koiwai O., Nishiyama Y. The UL34 gene product of herpes simplex virus type 2 is a tail-anchored type II membrane protein that is significant for virus envelopment. J. Gen. Virol. 2000, 81:2397-2405.
    • (2000) J. Gen. Virol. , vol.81 , pp. 2397-2405
    • Shiba, C.1    Daikoku, T.2    Goshima, F.3    Takakuwa, H.4    Yamauchi, Y.5    Koiwai, O.6    Nishiyama, Y.7
  • 153
  • 154
    • 2442719000 scopus 로고    scopus 로고
    • Herpes simplex virus 1 U(L)31 and U(L)34 gene products promote the late maturation of viral replication compartments to the nuclear periphery
    • Simpson-Holley M., Baines J., Roller R., Knipe D.M. Herpes simplex virus 1 U(L)31 and U(L)34 gene products promote the late maturation of viral replication compartments to the nuclear periphery. J. Virol. 2004, 78:5591-5600.
    • (2004) J. Virol. , vol.78 , pp. 5591-5600
    • Simpson-Holley, M.1    Baines, J.2    Roller, R.3    Knipe, D.M.4
  • 155
    • 0035024157 scopus 로고    scopus 로고
    • Herpes simplex virus nucleocapsids mature to progeny virions by an envelopment --> deenvelopment --> reenvelopment pathway
    • Skepper J.N., Whiteley A., Browne H., Minson A. Herpes simplex virus nucleocapsids mature to progeny virions by an envelopment --> deenvelopment --> reenvelopment pathway. J. Virol. 2001, 75:5697-5702.
    • (2001) J. Virol. , vol.75 , pp. 5697-5702
    • Skepper, J.N.1    Whiteley, A.2    Browne, H.3    Minson, A.4
  • 156
    • 0035831473 scopus 로고    scopus 로고
    • Executioner caspase-3, -6, and -7 perform distinct, non-redundant roles during the demolition phase of apoptosis
    • Slee E.A., Adrain C., Martin S.J. Executioner caspase-3, -6, and -7 perform distinct, non-redundant roles during the demolition phase of apoptosis. J. Biol. Chem. 2001, 276:7320-7326.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7320-7326
    • Slee, E.A.1    Adrain, C.2    Martin, S.J.3
  • 157
    • 0030896925 scopus 로고    scopus 로고
    • Microtubule-mediated transport of incoming herpes simplex virus 1 capsids to the nucleus
    • Sodeik B., Ebersold M.W., Helenius A. Microtubule-mediated transport of incoming herpes simplex virus 1 capsids to the nucleus. J. Cell Biol. 1997, 136:1007-1021.
    • (1997) J. Cell Biol. , vol.136 , pp. 1007-1021
    • Sodeik, B.1    Ebersold, M.W.2    Helenius, A.3
  • 158
    • 80155205513 scopus 로고    scopus 로고
    • Molecular architecture of the transport channel of the nuclear pore complex
    • Solmaz S.R., Chauhan R., Blobel G., Melcak I. Molecular architecture of the transport channel of the nuclear pore complex. Cell 2011, 147:590-602.
    • (2011) Cell , vol.147 , pp. 590-602
    • Solmaz, S.R.1    Chauhan, R.2    Blobel, G.3    Melcak, I.4
  • 159
    • 33750712806 scopus 로고    scopus 로고
    • Adeno-associated virus type 2 capsids with externalized VP1/VP2 trafficking domains are generated prior to passage through the cytoplasm and are maintained until uncoating occurs in the nucleus
    • Sonntag F., Bleker S., Leuchs B., Fischer R., Kleinschmidt J.A. Adeno-associated virus type 2 capsids with externalized VP1/VP2 trafficking domains are generated prior to passage through the cytoplasm and are maintained until uncoating occurs in the nucleus. J. Virol. 2006, 80:11040-11054.
    • (2006) J. Virol. , vol.80 , pp. 11040-11054
    • Sonntag, F.1    Bleker, S.2    Leuchs, B.3    Fischer, R.4    Kleinschmidt, J.A.5
  • 160
    • 33646808579 scopus 로고    scopus 로고
    • Nuclear pore complex assembly and maintenance in POM121- and gp210-deficient cells
    • Stavru F., Nautrup-Pedersen G., Cordes V.C., Gorlich D. Nuclear pore complex assembly and maintenance in POM121- and gp210-deficient cells. J. Cell Biol. 2006, 173:477-483.
    • (2006) J. Cell Biol. , vol.173 , pp. 477-483
    • Stavru, F.1    Nautrup-Pedersen, G.2    Cordes, V.C.3    Gorlich, D.4
  • 161
  • 164
    • 33847139800 scopus 로고    scopus 로고
    • The road to chromatin-nuclear entry of retroviruses
    • Suzuki Y., Craigie R. The road to chromatin-nuclear entry of retroviruses. Nat. Rev. Microbiol. 2007, 5:187-196.
    • (2007) Nat. Rev. Microbiol. , vol.5 , pp. 187-196
    • Suzuki, Y.1    Craigie, R.2
  • 165
    • 0038702518 scopus 로고    scopus 로고
    • Cell-free synthesis of encephalomyocarditis virus
    • Svitkin Y.V., Sonenberg N. Cell-free synthesis of encephalomyocarditis virus. J. Virol. 2003, 77:6551-6555.
    • (2003) J. Virol. , vol.77 , pp. 6551-6555
    • Svitkin, Y.V.1    Sonenberg, N.2
  • 166
    • 0029666264 scopus 로고    scopus 로고
    • BetaII protein kinase C is required for the G2/M phase transition of cell cycle
    • Thompson L.J., Fields A.P. betaII protein kinase C is required for the G2/M phase transition of cell cycle. J. Biol. Chem. 1996, 271:15045-15053.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15045-15053
    • Thompson, L.J.1    Fields, A.P.2
  • 167
    • 0035195085 scopus 로고    scopus 로고
    • Import of adenovirus DNA involves the nuclear pore complex receptor CAN/Nup214 and histone H1
    • Trotman L.C., Mosberger N., Fornerod M., Stidwill R.P., Greber U.F. Import of adenovirus DNA involves the nuclear pore complex receptor CAN/Nup214 and histone H1. Nat. Cell Biol. 2001, 3:1092-1100.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 1092-1100
    • Trotman, L.C.1    Mosberger, N.2    Fornerod, M.3    Stidwill, R.P.4    Greber, U.F.5
  • 169
    • 0036149891 scopus 로고    scopus 로고
    • The VP1 N-terminal sequence of canine parvovirus affects nuclear transport of capsids and efficient cell infection
    • Vihinen-Ranta M., Wang D., Weichert W.S., Parrish C.R. The VP1 N-terminal sequence of canine parvovirus affects nuclear transport of capsids and efficient cell infection. J. Virol. 2002, 76:1884-1891.
    • (2002) J. Virol. , vol.76 , pp. 1884-1891
    • Vihinen-Ranta, M.1    Wang, D.2    Weichert, W.S.3    Parrish, C.R.4
  • 170
    • 0034000922 scopus 로고    scopus 로고
    • Cytoplasmic trafficking of the canine parvovirus capsid and its role in infection and nuclear transport
    • Vihinen-Ranta M., Yuan W., Parrish C.R. Cytoplasmic trafficking of the canine parvovirus capsid and its role in infection and nuclear transport. J. Virol. 2000, 74:4853-4859.
    • (2000) J. Virol. , vol.74 , pp. 4853-4859
    • Vihinen-Ranta, M.1    Yuan, W.2    Parrish, C.R.3
  • 171
    • 0031927035 scopus 로고    scopus 로고
    • Viral ribonucleoprotein complex formation and nucleolar-cytoplasmic relocalization of nucleolin in poliovirus-infected cells
    • Waggoner S., Sarnow P. Viral ribonucleoprotein complex formation and nucleolar-cytoplasmic relocalization of nucleolin in poliovirus-infected cells. J. Virol. 1998, 72:6699-6709.
    • (1998) J. Virol. , vol.72 , pp. 6699-6709
    • Waggoner, S.1    Sarnow, P.2
  • 173
    • 80055009976 scopus 로고    scopus 로고
    • Differential processing of nuclear pore complex proteins by rhinovirus 2A proteases from different species and serotypes
    • Watters K., Palmenberg A.C. Differential processing of nuclear pore complex proteins by rhinovirus 2A proteases from different species and serotypes. J. Virol. 2011, 85:10874-10883.
    • (2011) J. Virol. , vol.85 , pp. 10874-10883
    • Watters, K.1    Palmenberg, A.C.2
  • 175
    • 69849086706 scopus 로고    scopus 로고
    • Architectural nucleoporins Nup157/170 and Nup133 are structurally related and descend from a second ancestral element
    • Whittle J.R., Schwartz T.U. Architectural nucleoporins Nup157/170 and Nup133 are structurally related and descend from a second ancestral element. J. Biol. Chem. 2009, 284:28442-28452.
    • (2009) J. Biol. Chem. , vol.284 , pp. 28442-28452
    • Whittle, J.R.1    Schwartz, T.U.2
  • 176
    • 13444311651 scopus 로고    scopus 로고
    • Adenovirus protein VI mediates membrane disruption following capsid disassembly
    • Wiethoff C.M., Wodrich H., Gerace L., Nemerow G.R. Adenovirus protein VI mediates membrane disruption following capsid disassembly. J. Virol. 2005, 79:1992-2000.
    • (2005) J. Virol. , vol.79 , pp. 1992-2000
    • Wiethoff, C.M.1    Wodrich, H.2    Gerace, L.3    Nemerow, G.R.4
  • 177
    • 84855833888 scopus 로고    scopus 로고
    • Modulation of host cell nucleocytoplasmic trafficking during picornavirus infection
    • Younessi P., Jans D.A., Ghildyal R. Modulation of host cell nucleocytoplasmic trafficking during picornavirus infection. Infect. Disord. Drug Targets 2012, 12:59-67.
    • (2012) Infect. Disord. Drug Targets , vol.12 , pp. 59-67
    • Younessi, P.1    Jans, D.A.2    Ghildyal, R.3
  • 179
    • 77954176607 scopus 로고    scopus 로고
    • The nucleoporin Nup153 maintains nuclear envelope architecture and is required for cell migration in tumor cells
    • Zhou L., Pante N. The nucleoporin Nup153 maintains nuclear envelope architecture and is required for cell migration in tumor cells. FEBS Lett. 2010, 584:3013-3020.
    • (2010) FEBS Lett. , vol.584 , pp. 3013-3020
    • Zhou, L.1    Pante, N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.