메뉴 건너뛰기




Volumn 85, Issue 9, 2011, Pages 4271-4283

Uncoupling uncoating of herpes simplex virus genomes from their nuclear import and gene expression

Author keywords

[No Author keywords available]

Indexed keywords

CAPSID PROTEIN; PROTEIN GFPUL25; PROTEIN UL25; PROTEIN UL25GFP; PROTEIN UL6; UNCLASSIFIED DRUG;

EID: 79955419807     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02067-10     Document Type: Article
Times cited : (31)

References (98)
  • 1
    • 0021674340 scopus 로고
    • Characterisation of a herpes simplex virus type 1 mutant which has a temperature-sensitive defect in penetration of cells and assembly of capsids
    • Addison, C., F. J. Rixon, J. W. Palfreyman, M. O'Hara, and V. G. Preston. 1984. Characterisation of a herpes simplex virus type 1 mutant which has a temperature-sensitive defect in penetration of cells and assembly of capsids. Virology 138:246-259.
    • (1984) Virology , vol.138 , pp. 246-259
    • Addison, C.1    Rixon, F.J.2    Palfreyman, J.W.3    O'Hara, M.4    Preston, V.G.5
  • 2
    • 0029928134 scopus 로고    scopus 로고
    • Characterization of an essential HSV-1 protein encoded by the UL25 gene reported to be involved in virus penetration and capsid assembly
    • Ali, M. A., B. Forghani, and E. M. Cantin. 1996. Characterization of an essential HSV-1 protein encoded by the UL25 gene reported to be involved in virus penetration and capsid assembly. Virology 216:278-283.
    • (1996) Virology , vol.216 , pp. 278-283
    • Ali, M.A.1    Forghani, B.2    Cantin, E.M.3
  • 3
    • 27144510987 scopus 로고    scopus 로고
    • Cleavage and packaging of herpes simplex 1 viral DNA
    • C. E. Catalano (ed.), Landes Biosciences, Austin, TX
    • Baines, J. D., and S. K. Weller. 2005. Cleavage and packaging of herpes simplex 1 viral DNA, p. 135-150. In C. E. Catalano (ed.), Viral genome packaging machines: genetics, structures and mechanism. Landes Biosciences, Austin, TX.
    • (2005) Viral genome packaging machines: Genetics, structures and mechanism , pp. 135-150
    • Baines, J.D.1    Weller, S.K.2
  • 4
    • 27744487093 scopus 로고    scopus 로고
    • Common ancestry of herpesviruses and tailed DNA bacteriophages
    • Baker, M. L., W. Jiang, F. J. Rixon, and W. Chiu. 2005. Common ancestry of herpesviruses and tailed DNA bacteriophages. J. Virol. 79:14967-14970.
    • (2005) J. Virol. , vol.79 , pp. 14967-14970
    • Baker, M.L.1    Jiang, W.2    Rixon, F.J.3    Chiu, W.4
  • 5
    • 0020701819 scopus 로고
    • Molecular genetics of herpes simplex virus. VIII. further characterization of a temperature-sensitive mutant defective in release of viral DNA and in other stages of the viral reproductive cycle
    • Batterson, W., D. Furlong, and B. Roizman. 1983. Molecular genetics of herpes simplex virus. VIII. further characterization of a temperature-sensitive mutant defective in release of viral DNA and in other stages of the viral reproductive cycle. J. Virol. 45:397-407.
    • (1983) J. Virol. , vol.45 , pp. 397-407
    • Batterson, W.1    Furlong, D.2    Roizman, B.3
  • 6
    • 39749151703 scopus 로고    scopus 로고
    • The essential human cytomegalovirus gene UL52 is required for cleavage-packaging of the viral genome
    • Borst, E. M., K. Wagner, A. Binz, B. Sodeik, and M. Messerle. 2008. The essential human cytomegalovirus gene UL52 is required for cleavage-packaging of the viral genome. J. Virol. 82:2065-2078.
    • (2008) J. Virol. , vol.82 , pp. 2065-2078
    • Borst, E.M.1    Wagner, K.2    Binz, A.3    Sodeik, B.4    Messerle, M.5
  • 7
    • 33144488410 scopus 로고    scopus 로고
    • Structural characterization of the UL25 DNA-packaging protein from herpes simplex virus type 1
    • Bowman, B. R., et al. 2006. Structural characterization of the UL25 DNA-packaging protein from herpes simplex virus type 1. J. Virol. 80:2309-2317.
    • (2006) J. Virol. , vol.80 , pp. 2309-2317
    • Bowman, B.R.1
  • 8
    • 0005246168 scopus 로고    scopus 로고
    • Packaging DNA into herpesvirus capsids
    • A. Holzenburg and E. Bogner (ed.), Kluwer Academic/Plenum Publishers, New York, NY
    • Brown, J. C., M. A. McVoy, and F. L. Homa. 2002. Packaging DNA into herpesvirus capsids, p. 111-154. In A. Holzenburg and E. Bogner (ed.), Structure-function relationships of human pathogenic viruses. Kluwer Academic/Plenum Publishers, New York, NY.
    • (2002) Structure-function relationships of human pathogenic viruses , pp. 111-154
    • Brown, J.C.1    McVoy, M.A.2    Homa, F.L.3
  • 9
    • 0026744303 scopus 로고
    • The small GTPase rab5 functions as a regulatory factor in the early endocytic pathway
    • Bucci, C., et al. 1992. The small GTPase rab5 functions as a regulatory factor in the early endocytic pathway. Cell 70:715-728.
    • (1992) Cell , vol.70 , pp. 715-728
    • Bucci, C.1
  • 10
    • 58149384474 scopus 로고    scopus 로고
    • Role of the UL25 protein in herpes simplex virus DNA encapsidation
    • Cockrell, S. K., M. E. Sanchez, A. Erazo, and F. L. Homa. 2009. Role of the UL25 protein in herpes simplex virus DNA encapsidation. J. Virol. 83:47-57.
    • (2009) J. Virol. , vol.83 , pp. 47-57
    • Cockrell, S.K.1    Sanchez, M.E.2    Erazo, A.3    Homa, F.L.4
  • 11
    • 0018860443 scopus 로고
    • Structural analysis of the capsid polypeptides of herpes simplex virus types 1 and 2
    • Cohen, G. H., et al. 1980. Structural analysis of the capsid polypeptides of herpes simplex virus types 1 and 2. J. Virol. 34:521-531.
    • (1980) J. Virol. , vol.34 , pp. 521-531
    • Cohen, G.H.1
  • 12
    • 35448946916 scopus 로고    scopus 로고
    • The capsid and tegument of the alphaherpesviruses are linked by an interaction between the UL25 and VP1/2 proteins
    • Coller, K. E., J. I. Lee, A. Ueda, and G. A. Smith. 2007. The capsid and tegument of the alphaherpesviruses are linked by an interaction between the UL25 and VP1/2 proteins. J. Virol. 81:11790-11797.
    • (2007) J. Virol. , vol.81 , pp. 11790-11797
    • Coller, K.E.1    Lee, J.I.2    Ueda, A.3    Smith, G.A.4
  • 13
    • 77349090419 scopus 로고    scopus 로고
    • Labeling and localization of the herpes simplex virus capsid protein UL25 and its interaction with the two triplexes closest to the penton
    • Conway, J. F., et al. 2010. Labeling and localization of the herpes simplex virus capsid protein UL25 and its interaction with the two triplexes closest to the penton. J. Mol. Biol. 397:575-586.
    • (2010) J. Mol. Biol. , vol.397 , pp. 575-586
    • Conway, J.F.1
  • 14
    • 59649092592 scopus 로고    scopus 로고
    • Herpes simplex virus replication: Roles of viral proteins and nucleoporins in capsid-nucleus attachment
    • Copeland, A. M., W. W. Newcomb, and J. C. Brown. 2009. Herpes simplex virus replication: roles of viral proteins and nucleoporins in capsid-nucleus attachment. J. Virol. 83:1660-1668.
    • (2009) J. Virol. , vol.83 , pp. 1660-1668
    • Copeland, A.M.1    Newcomb, W.W.2    Brown, J.C.3
  • 16
    • 0027514853 scopus 로고
    • A cosmid-based system for constructing mutants of herpes simplex virus type 1
    • Cunningham, C., and A. J. Davison. 1993. A cosmid-based system for constructing mutants of herpes simplex virus type 1. Virology 197:116-124.
    • (1993) Virology , vol.197 , pp. 116-124
    • Cunningham, C.1    Davison, A.J.2
  • 17
    • 52949107958 scopus 로고    scopus 로고
    • Structure, dynamics and function of nuclear pore complexes
    • D'Angelo, M. A., and M. W. Hetzer. 2008. Structure, dynamics and function of nuclear pore complexes. Trends Cell Biol. 18:456-466.
    • (2008) Trends Cell Biol , vol.18 , pp. 456-466
    • D'Angelo, M.A.1    Hetzer, M.W.2
  • 18
    • 0042854781 scopus 로고    scopus 로고
    • Implication of the product of the bovine herpesvirus type 1 UL25 gene in capsid assembly
    • Desloges, N., and C. Simard. 2003. Implication of the product of the bovine herpesvirus type 1 UL25 gene in capsid assembly. J. Gen. Virol. 84:2485-2490.
    • (2003) J. Gen. Virol. , vol.84 , pp. 2485-2490
    • Desloges, N.1    Simard, C.2
  • 19
    • 33746853425 scopus 로고    scopus 로고
    • Eclipse phase of herpes simplex virus type 1 infection: Efficient dynein-mediated capsid transport without the small capsid protein VP26
    • Döhner, K., K. Radtke, S. Schmidt, and B. Sodeik. 2006. Eclipse phase of herpes simplex virus type 1 infection: efficient capsid transport without the small capsid protein VP26. J. Virol. 80:8211-8224.
    • (2006) J. Virol. , vol.80 , pp. 8211-8224
    • Döhner, K.1    Radtke, K.2    Schmidt, S.3    Sodeik, B.4
  • 20
    • 0036678882 scopus 로고    scopus 로고
    • Function of dynein and dynactin in herpes simplex virus capsid transport
    • Döhner, K., et al. 2002. Function of dynein and dynactin in herpes simplex virus capsid transport. Mol. Biol. Cell 13:2795-2809.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2795-2809
    • Döhner, K.1
  • 21
    • 16244422998 scopus 로고    scopus 로고
    • ND10 components relocate to sites associated with herpes simplex virus type 1 nucleoprotein complexes during virus infection
    • Everett, R. D., and J. Murray. 2005. ND10 components relocate to sites associated with herpes simplex virus type 1 nucleoprotein complexes during virus infection. J. Virol. 79:5078-5089.
    • (2005) J. Virol. , vol.79 , pp. 5078-5089
    • Everett, R.D.1    Murray, J.2
  • 22
    • 0025946814 scopus 로고
    • High level expression and purification of herpes simplex virus type 1 immediate early polypeptide Vmw110
    • Everett, R. D., A. Orr, and M. Elliott. 1991. High level expression and purification of herpes simplex virus type 1 immediate early polypeptide Vmw110. Nucleic Acids Res. 19:6155-6161.
    • (1991) Nucleic Acids Res , vol.19 , pp. 6155-6161
    • Everett, R.D.1    Orr, A.2    Elliott, M.3
  • 23
    • 0031444202 scopus 로고    scopus 로고
    • An extended microtubule-binding structure within the dynein motor domain
    • Gee, M. A., J. E. Heuser, and R. B. Vallee. 1997. An extended microtubule-binding structure within the dynein motor domain. Nature 390:636-639.
    • (1997) Nature , vol.390 , pp. 636-639
    • Gee, M.A.1    Heuser, J.E.2    Vallee, R.B.3
  • 24
    • 68349116137 scopus 로고    scopus 로고
    • Conditional and reversible disruption of essential herpesvirus proteins
    • Glass, M., A. Busche, K. Wagner, M. Messerle, and E. M. Borst. 2009. Conditional and reversible disruption of essential herpesvirus proteins. Nat. Methods 6:577-579.
    • (2009) Nat. Methods , vol.6 , pp. 577-579
    • Glass, M.1    Busche, A.2    Wagner, K.3    Messerle, M.4    Borst, E.M.5
  • 25
    • 13944272582 scopus 로고    scopus 로고
    • Entry of pseudo-rabies virus: An immunogold-labeling study
    • Granzow, H., B. G. Klupp, and T. C. Mettenleiter. 2005. Entry of pseudo-rabies virus: an immunogold-labeling study. J. Virol. 79:3200-3205.
    • (2005) J. Virol. , vol.79 , pp. 3200-3205
    • Granzow, H.1    Klupp, B.G.2    Mettenleiter, T.C.3
  • 26
    • 0031048830 scopus 로고    scopus 로고
    • Ultrastructural analysis of the replication cycle of pseudorabies virus in cell culture: A reassessment
    • Granzow, H., et al. 1997. Ultrastructural analysis of the replication cycle of pseudorabies virus in cell culture: a reassessment. J. Virol. 71:2072-2082.
    • (1997) J. Virol. , vol.71 , pp. 2072-2082
    • Granzow, H.1
  • 27
    • 48249132077 scopus 로고    scopus 로고
    • Interactions of the HSV-1 UL25 capsid protein with cellular microtubule-associated protein
    • Guo, L., et al. 2008. Interactions of the HSV-1 UL25 capsid protein with cellular microtubule-associated protein. Virologica Sinica 23:211-217.
    • (2008) Virologica Sinica , vol.23 , pp. 211-217
    • Guo, L.1
  • 28
    • 0030871678 scopus 로고    scopus 로고
    • Capsid assembly and DNA packaging in herpes simplex virus
    • Homa, F. L., and J. C. Brown. 1997. Capsid assembly and DNA packaging in herpes simplex virus. Rev. Med. Virol. 7:107-122.
    • (1997) Rev. Med. Virol. , vol.7 , pp. 107-122
    • Homa, F.L.1    Brown, J.C.2
  • 29
    • 48249150289 scopus 로고    scopus 로고
    • The Nup358-RanGAP complex is required for efficient importin alpha/beta-dependent nuclear import
    • Hutten, S., A. Flotho, F. Melchior, and R. H. Kehlenbach. 2008. The Nup358-RanGAP complex is required for efficient importin alpha/beta-dependent nuclear import. Mol. Biol. Cell 19:2300-2310.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2300-2310
    • Hutten, S.1    Flotho, A.2    Melchior, F.3    Kehlenbach, R.H.4
  • 30
    • 33748657386 scopus 로고    scopus 로고
    • Nup214 is required for CRM1-dependent nuclear protein export in vivo
    • Hutten, S., and R. H. Kehlenbach. 2006. Nup214 is required for CRM1-dependent nuclear protein export in vivo. Mol. Cell. Biol. 26:6772-6785.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 6772-6785
    • Hutten, S.1    Kehlenbach, R.H.2
  • 31
    • 66849125858 scopus 로고    scopus 로고
    • The nuclear pore component Nup358 promotes transportin-dependent nuclear import
    • Hutten, S., S. Walde, C. Spillner, J. Hauber, and R. H. Kehlenbach. 2009. The nuclear pore component Nup358 promotes transportin-dependent nuclear import. J. Cell Sci. 122:1100-1110.
    • (2009) J. Cell Sci. , vol.122 , pp. 1100-1110
    • Hutten, S.1    Walde, S.2    Spillner, C.3    Hauber, J.4    Kehlenbach, R.H.5
  • 32
    • 33745714419 scopus 로고    scopus 로고
    • Dynamics of DNA ejection from bacteriophage
    • Inamdar, M. M., W. M. Gelbart, and R. Phillips. 2006. Dynamics of DNA ejection from bacteriophage. Biophys. J. 91:411-420.
    • (2006) Biophys. J. , vol.91 , pp. 411-420
    • Inamdar, M.M.1    Gelbart, W.M.2    Phillips, R.3
  • 33
    • 41149126620 scopus 로고    scopus 로고
    • Proteolytic cleavage of VP1-2 is required for release of herpes simplex virus 1 DNA into the nucleus
    • Jovasevic, V., L. Liang, and B. Roizman. 2008. Proteolytic cleavage of VP1-2 is required for release of herpes simplex virus 1 DNA into the nucleus. J. Virol. 82:3311-3319.
    • (2008) J. Virol. , vol.82 , pp. 3311-3319
    • Jovasevic, V.1    Liang, L.2    Roizman, B.3
  • 34
    • 0343503005 scopus 로고    scopus 로고
    • The UL25 protein of pseudorabies virus associates with capsids and localizes to the nucleus and to microtubules
    • Kaelin, K., S. Dezelee, M. J. Masse, F. Bras, and A. Flamand. 2000. The UL25 protein of pseudorabies virus associates with capsids and localizes to the nucleus and to microtubules. J. Virol. 74:474-482.
    • (2000) J. Virol. , vol.74 , pp. 474-482
    • Kaelin, K.1    Dezelee, S.2    Masse, M.J.3    Bras, F.4    Flamand, A.5
  • 35
    • 3042635320 scopus 로고    scopus 로고
    • CRM1-depen-dent, but not ARE-mediated, nuclear export of IFN-alpha1 mRNA
    • Kimura, T., I. Hashimoto, T. Nagase, and J. Fujisawa. 2004. CRM1-depen-dent, but not ARE-mediated, nuclear export of IFN-alpha1 mRNA. J. Cell Sci. 117:2259-2270.
    • (2004) J. Cell Sci. , vol.117 , pp. 2259-2270
    • Kimura, T.1    Hashimoto, I.2    Nagase, T.3    Fujisawa, J.4
  • 36
    • 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., H. Granzow, G. M. Keil, and T. C. Mettenleiter. 2006. 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. J. Virol. 80:6235-6246.
    • (2006) J. Virol. , vol.80 , pp. 6235-6246
    • Klupp, B.G.1    Granzow, H.2    Keil, G.M.3    Mettenleiter, T.C.4
  • 38
    • 0030731408 scopus 로고    scopus 로고
    • The pseudorabies virus UL28 protein enters the nucleus after coexpression with the herpes simplex virus UL15 protein
    • Koslowski, K. M., P. R. Shaver, X. Y. Wang, D. J. Tenney, and N. E. Pederson. 1997. The pseudorabies virus UL28 protein enters the nucleus after coexpression with the herpes simplex virus UL15 protein. J. Virol. 71:9118-9123.
    • (1997) J. Virol. , vol.71 , pp. 9118-9123
    • Koslowski, K.M.1    Shaver, P.R.2    Wang, X.Y.3    Tenney, D.J.4    Pederson, N.E.5
  • 39
    • 0027715992 scopus 로고
    • Transient arrest of 3T3 cells in mitosis and inhibition of nuclear lamin reassembly around chromatin induced by anti-vimentin antibodies
    • Kouklis, P. D., A. Merdes, T. Papamarcaki, and S. D. Georgatos. 1993. Transient arrest of 3T3 cells in mitosis and inhibition of nuclear lamin reassembly around chromatin induced by anti-vimentin antibodies. Eur. J. Cell Biol. 62:224-236.
    • (1993) Eur. J. Cell Biol. , vol.62 , pp. 224-236
    • Kouklis, P.D.1    Merdes, A.2    Papamarcaki, T.3    Georgatos, S.D.4
  • 40
    • 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., et al. 2008. Partial functional complementation of a pseudorabies virus UL25 deletion mutant by herpes simplex virus type 1 pUL25 indicates overlapping functions of alphaherpesvirus pUL25 proteins. J. Virol. 82: 5725-5734.
    • (2008) J. Virol. , vol.82 , pp. 5725-5734
    • Kuhn, J.1
  • 41
    • 70350397021 scopus 로고    scopus 로고
    • Transportin mediates nuclear entry of DNA in vertebrate systems
    • Lachish-Zalait, A., et al. 2009. Transportin mediates nuclear entry of DNA in vertebrate systems. Traffic 10:1414-1428.
    • (2009) Traffic , vol.10 , pp. 1414-1428
    • Lachish-Zalait, A.1
  • 42
    • 39149125768 scopus 로고    scopus 로고
    • Towards reconciling structure and function in the nuclear pore complex
    • Lim, R. Y., U. Aebi, and B. Fahrenkrog. 2008. Towards reconciling structure and function in the nuclear pore complex. Histochem. Cell Biol. 129:105-116.
    • (2008) Histochem. Cell Biol. , vol.129 , pp. 105-116
    • Lim, R.Y.1    Aebi, U.2    Fahrenkrog, B.3
  • 43
    • 50149119228 scopus 로고    scopus 로고
    • Comprehensive characterization of extracellular herpes simplex virus type 1 virions
    • Loret, S., G. Guay, and R. Lippe. 2008. Comprehensive characterization of extracellular herpes simplex virus type 1 virions. J. Virol. 82:8605-8618.
    • (2008) J. Virol. , vol.82 , pp. 8605-8618
    • Loret, S.1    Guay, G.2    Lippe, R.3
  • 44
    • 77949266043 scopus 로고    scopus 로고
    • Chromatin assembly on herpes simplex virus genomes during lytic infection. Biochim. Biophys
    • Lu, X., and S. J. Triezenberg. 2010. Chromatin assembly on herpes simplex virus genomes during lytic infection. Biochim. Biophys. Acta 1799:217-222.
    • (2010) Acta , vol.1799 , pp. 217-222
    • Lu, X.1    Triezenberg, S.J.2
  • 45
    • 77950515413 scopus 로고    scopus 로고
    • Regulation of ICP0-null mutant herpes simplex virus type 1 infection by ND10 components ATRX and hDaxx
    • Lukashchuk, V., and R. D. Everett. 2010. Regulation of ICP0-null mutant herpes simplex virus type 1 infection by ND10 components ATRX and hDaxx. J. Virol. 84:4026-4040.
    • (2010) J. Virol. , vol.84 , pp. 4026-4040
    • Lukashchuk, V.1    Everett, R.D.2
  • 46
    • 17644404401 scopus 로고    scopus 로고
    • Targeting of herpesvirus capsid transport in axons is coupled to association with specific sets of tegument proteins
    • Luxton, G. W., et al. 2005. Targeting of herpesvirus capsid transport in axons is coupled to association with specific sets of tegument proteins. Proc. Natl. Acad. Sci. U. S. A. 102:5832-5837.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 5832-5837
    • Luxton, G.W.1
  • 47
    • 0036776337 scopus 로고    scopus 로고
    • Intact microtubules support adenovirus and herpes simplex virus infections
    • Mabit, H., et al. 2002. Intact microtubules support adenovirus and herpes simplex virus infections. J. Virol. 76:9962-9971.
    • (2002) J. Virol. , vol.76 , pp. 9962-9971
    • Mabit, H.1
  • 48
    • 1842843639 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 infection of polarized epithelial cells requires microtubules and access to receptors present at cell-cell contact sites
    • Marozin, S., U. Prank, and B. Sodeik. 2004. Herpes simplex virus type 1 infection of polarized epithelial cells requires microtubules and access to receptors present at cell-cell contact sites. J. Gen. Virol. 85:775-786.
    • (2004) J. Gen. Virol. , vol.85 , pp. 775-786
    • Marozin, S.1    Prank, U.2    Sodeik, B.3
  • 49
    • 48749114826 scopus 로고    scopus 로고
    • Native 3D intermediates of membrane fusion in herpes simplex virus 1 entry
    • Maurer, U. E., B. Sodeik, and K. Grünewald. 2008. Native 3D intermediates of membrane fusion in herpes simplex virus 1 entry. Proc. Natl. Acad. Sci. U. S. A. 105:10559-10564.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 10559-10564
    • Maurer, U.E.1    Sodeik, B.2    Grünewald, K.3
  • 50
    • 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., et al. 1998. The product of the herpes simplex virus type 1 UL25 gene is required for encapsidation but not for cleavage of replicated viral DNA. J. Virol. 72:1060-1070.
    • (1998) J. Virol. , vol.72 , pp. 1060-1070
    • McNab, A.R.1
  • 52
    • 40149086016 scopus 로고    scopus 로고
    • Nuclear egress and envelopment of herpes simplex virus capsids analyzed with dual-color fluorescence HSV-1(17+)
    • Nagel, C. H., et al. 2008. Nuclear egress and envelopment of herpes simplex virus capsids analyzed with dual-color fluorescence HSV-1(17+). J. Virol. 82:3109-3124.
    • (2008) J. Virol. , vol.82 , pp. 3109-3124
    • Nagel, C.H.1
  • 53
    • 34249930876 scopus 로고    scopus 로고
    • Uncoating the herpes simplex virus genome
    • Newcomb, W. W., F. P. Booy, and J. C. Brown. 2007. Uncoating the herpes simplex virus genome. J. Mol. Biol. 370:633-642.
    • (2007) J. Mol. Biol. , vol.370 , pp. 633-642
    • Newcomb, W.W.1    Booy, F.P.2    Brown, J.C.3
  • 54
    • 0028091060 scopus 로고
    • Induced extrusion of DNA from the capsid of herpes simplex virus type 1
    • Newcomb, W. W., and J. C. Brown. 1994. Induced extrusion of DNA from the capsid of herpes simplex virus type 1. J. Virol. 68:433-440.
    • (1994) J. Virol. , vol.68 , pp. 433-440
    • Newcomb, W.W.1    Brown, J.C.2
  • 55
  • 56
    • 33745244290 scopus 로고    scopus 로고
    • Herpes simplex virus capsid structure: DNA packaging protein UL25 is located on the external surface of the capsid near the vertices
    • Newcomb, W. W., F. L. Homa, and J. C. Brown. 2006. Herpes simplex virus capsid structure: DNA packaging protein UL25 is located on the external surface of the capsid near the vertices. J. Virol. 80:6286-6294.
    • (2006) J. Virol. , vol.80 , pp. 6286-6294
    • Newcomb, W.W.1    Homa, F.L.2    Brown, J.C.3
  • 57
    • 23244438898 scopus 로고    scopus 로고
    • Involvement of the portal at an early step in herpes simplex virus capsid assembly
    • Newcomb, W. W., F. L. Homa, and J. C. Brown. 2005. Involvement of the portal at an early step in herpes simplex virus capsid assembly. J. Virol. 79:10540-10546.
    • (2005) J. Virol. , vol.79 , pp. 10540-10546
    • Newcomb, W.W.1    Homa, F.L.2    Brown, J.C.3
  • 58
    • 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., D. R. Thomsen, F. L. Homa, and J. C. Brown. 2003. Assembly of the herpes simplex virus capsid: identification of soluble scaffold-portal complexes and their role in formation of portal-containing capsids. J. Virol. 77:9862-9871.
    • (2003) J. Virol. , vol.77 , pp. 9862-9871
    • Newcomb, W.W.1    Thomsen, D.R.2    Homa, F.L.3    Brown, J.C.4
  • 59
    • 0035152181 scopus 로고    scopus 로고
    • Role of the UL25 gene product in packaging DNA into the herpes simplex virus capsid: Location of UL25 product in the capsid and demonstration that it binds DNA
    • Ogasawara, M., T. Suzutani, I. Yoshida, and M. Azuma. 2001. Role of the UL25 gene product in packaging DNA into the herpes simplex virus capsid: location of UL25 product in the capsid and demonstration that it binds DNA. J. Virol. 75:1427-1436.
    • (2001) J. Virol. , vol.75 , pp. 1427-1436
    • Ogasawara, M.1    Suzutani, T.2    Yoshida, I.3    Azuma, M.4
  • 60
    • 41149097014 scopus 로고    scopus 로고
    • Temporal association of the herpes simplex virus genome with histone proteins during a lytic infection
    • Oh, J., and N. W. Fraser. 2008. Temporal association of the herpes simplex virus genome with histone proteins during a lytic infection. J. Virol. 82:3530-3537.
    • (2008) J. Virol. , vol.82 , pp. 3530-3537
    • Oh, J.1    Fraser, N.W.2
  • 61
    • 77950838826 scopus 로고    scopus 로고
    • Mutational analysis of the herpes simplex virus type 1 UL25 DNA packaging protein reveals regions that are important after the viral DNA has been packaged
    • O'Hara, M., et al. 2010. Mutational analysis of the herpes simplex virus type 1 UL25 DNA packaging protein reveals regions that are important after the viral DNA has been packaged. J. Virol. 84:4252-4263.
    • (2010) J. Virol. , vol.84 , pp. 4252-4263
    • O'Hara, M.1
  • 62
    • 0034091334 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 entry into host cells: Reconstitution of capsid binding and uncoating at the nuclear pore complex in vitro
    • Ojala, P. M., B. Sodeik, M. W. Ebersold, U. Kutay, and A. Helenius. 2000. Herpes simplex virus type 1 entry into host cells: reconstitution of capsid binding and uncoating at the nuclear pore complex in vitro. Mol. Cell. Biol. 20:4922-4931.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 4922-4931
    • Ojala, P.M.1    Sodeik, B.2    Ebersold, M.W.3    Kutay, U.4    Helenius, A.5
  • 63
    • 67449089967 scopus 로고    scopus 로고
    • Herpesvirus capsid association with the nuclear pore complex and viral DNA release involve the nucleoporin CAN/Nup214 and the capsid protein pUL25
    • Pasdeloup, D., D. Blondel, A. L. Isidro, and F. J. Rixon. 2009. Herpesvirus capsid association with the nuclear pore complex and viral DNA release involve the nucleoporin CAN/Nup214 and the capsid protein pUL25. J. Virol. 83:6610-6623.
    • (2009) J. Virol. , vol.83 , pp. 6610-6623
    • Pasdeloup, D.1    Blondel, D.2    Isidro, A.L.3    Rixon, F.J.4
  • 64
    • 73449134082 scopus 로고    scopus 로고
    • Three-dimensional visualization of gammaherpesvirus life cycle in host cells by electron tomography
    • Peng, L., S. Ryazantsev, R. Sun, and Z. H. Zhou. 2010. Three-dimensional visualization of gammaherpesvirus life cycle in host cells by electron tomography. Structure 18:47-58.
    • (2010) Structure , vol.18 , pp. 47-58
    • Peng, L.1    Ryazantsev, S.2    Sun, R.3    Zhou, Z.H.4
  • 65
    • 65449152302 scopus 로고    scopus 로고
    • Translocation through the nuclear pore: Kaps pave the way
    • Peters, R. 2009. Translocation through the nuclear pore: Kaps pave the way. Bioessays 31:466-477.
    • (2009) Bioessays , vol.31 , pp. 466-477
    • Peters, R.1
  • 66
    • 0031032666 scopus 로고    scopus 로고
    • Nuclear sites of herpes simplex virus type 1 DNA replication and transcription colocalize at early times postinfection and are largely distinct from RNA processing factors
    • Phelan, A., J. Dunlop, A. H. Patel, N. D. Stow, and J. B. Clements. 1997. Nuclear sites of herpes simplex virus type 1 DNA replication and transcription colocalize at early times postinfection and are largely distinct from RNA processing factors. J. Virol. 71:1124-1132.
    • (1997) J. Virol. , vol.71 , pp. 1124-1132
    • Phelan, A.1    Dunlop, J.2    Patel, A.H.3    Stow, N.D.4    Clements, J.B.5
  • 67
    • 45749098219 scopus 로고    scopus 로고
    • The UL25 gene product of herpes simplex virus type 1 is involved in uncoating of the viral genome
    • Preston, V. G., J. Murray, C. M. Preston, I. M. McDougall, and N. D. Stow. 2008. The UL25 gene product of herpes simplex virus type 1 is involved in uncoating of the viral genome. J. Virol. 82:6654-6666.
    • (2008) J. Virol. , vol.82 , pp. 6654-6666
    • Preston, V.G.1    Murray, J.2    Preston, C.M.3    McDougall, I.M.4    Stow, N.D.5
  • 68
    • 77957652501 scopus 로고    scopus 로고
    • Plus- and minus-end directed microtubule motors bind simultaneously to herpes simplex virus capsids using different inner tegument structures
    • doi10.1371/journal.ppat.1000991
    • Radtke, K., et al. 2010. Plus- and minus-end directed microtubule motors bind simultaneously to herpes simplex virus capsids using different inner tegument structures. PLoS Pathog. 6:e1000991. doi10.1371/journal.ppat.1000991.
    • (2010) PLoS Pathog , vol.6
    • Radtke, K.1
  • 69
    • 3542999281 scopus 로고    scopus 로고
    • Peculiarities of herpes simplex virus (HSV) transcription: An overview
    • Rajcáni, J., V. Andrea, and R. Ingeborg. 2004. Peculiarities of herpes simplex virus (HSV) transcription: an overview. Virus Genes 28:293-310.
    • (2004) Virus Genes , vol.28 , pp. 293-310
    • Rajcáni, J.1    Andrea, V.2    Ingeborg, R.3
  • 70
    • 57649226492 scopus 로고    scopus 로고
    • The bacteriophage DNA packaging motor
    • Rao, V. B., and M. Feiss. 2008. The bacteriophage DNA packaging motor. Annu. Rev. Genet. 42:647-681.
    • (2008) Annu. Rev. Genet. , vol.42 , pp. 647-681
    • Rao, V.B.1    Feiss, M.2
  • 71
    • 52649114611 scopus 로고
    • The use of lead citrate at high pH as an electron-opaque stain in electron microscopy
    • Reynolds, E. S. 1963. The use of lead citrate at high pH as an electron-opaque stain in electron microscopy. J. Cell Biol. 17:208-212.
    • (1963) J. Cell Biol. , vol.17 , pp. 208-212
    • Reynolds, E.S.1
  • 72
    • 58149393193 scopus 로고    scopus 로고
    • Differing roles of inner tegument proteins pUL36 and pUL37 during entry of herpes simplex virus type 1
    • Roberts, A. P., et al. 2009. Differing roles of inner tegument proteins pUL36 and pUL37 during entry of herpes simplex virus type 1. J. Virol. 83:105-116.
    • (2009) J. Virol. , vol.83 , pp. 105-116
    • Roberts, A.P.1
  • 73
    • 34249950342 scopus 로고    scopus 로고
    • Herpes simplex viruses
    • D. M. Knipe and P. M. Howley (ed.), 5th ed. Lippincott Williams & Wilkins, Philadelphia, PA
    • Roizman, B., D. M. Knipe, and R. J. Whitley. 2007. Herpes simplex viruses, p. 2502-2601. In D. M. Knipe and P. M. Howley (ed.), Fundamental virology, 5th ed. Lippincott Williams & Wilkins, Philadelphia, PA.
    • (2007) Fundamental virology , pp. 2502-2601
    • Roizman, B.1    Knipe, D.M.2    Whitley, R.J.3
  • 74
    • 34250734534 scopus 로고    scopus 로고
    • Viral capsids: Mechanical characteristics, genome packaging and delivery mechanisms
    • Roos, W. H., I. L. Ivanovska, A. Evilevitch, and G. J. Wuite. 2007. Viral capsids: mechanical characteristics, genome packaging and delivery mechanisms. Cell. Mol. Life Sci. 64:1484-1497.
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 1484-1497
    • Roos, W.H.1    Ivanovska, I.L.2    Evilevitch, A.3    Wuite, G.J.4
  • 75
    • 67649852610 scopus 로고    scopus 로고
    • Scaffold expulsion and genome packaging trigger stabilization of herpes simplex virus capsids
    • Roos, W. H., et al. 2009. Scaffold expulsion and genome packaging trigger stabilization of herpes simplex virus capsids. Proc. Natl. Acad. Sci. U. S. A. 106:9673-9678.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 9673-9678
    • Roos, W.H.1
  • 76
    • 0030806017 scopus 로고    scopus 로고
    • Vaccinia virus membrane proteins p8 and p16 are cotranslationally inserted into the rough endoplasmic reticulum and retained in the intermediate compartment
    • Salmons, T., et al. 1997. Vaccinia virus membrane proteins p8 and p16 are cotranslationally inserted into the rough endoplasmic reticulum and retained in the intermediate compartment. J. Virol. 71:7404-7420.
    • (1997) J. Virol. , vol.71 , pp. 7404-7420
    • Salmons, T.1
  • 77
    • 0000936237 scopus 로고
    • Expression of cloned genes in cultured mammalian cells
    • In J. Sambrook, E. F. Fritsch, and T. Maniatis (ed.), 2nd ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Expression of cloned genes in cultured mammalian cells, p. 16.14-16.16. In J. Sambrook, E. F. Fritsch, and T. Maniatis (ed.), Molecular cloning: a laboratory manual, 2nd ed., vol. 3. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1989) Molecular cloning: A laboratory manual , vol.3
    • Sambrook, J.1    Fritsch, E.F.2    Maniatis, T.3
  • 78
    • 33644651719 scopus 로고    scopus 로고
    • Vaccinia virus-induced microtubule-dependent cellular rearrangements
    • Schepis, A., B. Schramm, C. A. de Haan, and J. Krijnse-Locker. 2006. Vaccinia virus-induced microtubule-dependent cellular rearrangements. Traffic 7:308-323.
    • (2006) Traffic , vol.7 , pp. 308-323
    • Schepis, A.1    Schramm, B.2    de Haan, C.A.3    Krijnse-Locker, J.4
  • 79
    • 0034633740 scopus 로고    scopus 로고
    • Efficient transformation of primary human amniocytes by E1 functions of Ad5: Generation of new cell lines for adenoviral vector production
    • Schiedner, G., S. Hertel, and S. Kochanek. 2000. Efficient transformation of primary human amniocytes by E1 functions of Ad5: generation of new cell lines for adenoviral vector production. Hum. Gene Ther. 11:2105-2116.
    • (2000) Hum. Gene Ther. , vol.11 , pp. 2105-2116
    • Schiedner, G.1    Hertel, S.2    Kochanek, S.3
  • 80
    • 72849144977 scopus 로고    scopus 로고
    • Effects of major capsid proteins, capsid assembly, and DNA cleavage/packaging on the pUL17/pUL25 complex of herpes simplex virus 1
    • Scholtes, L., and J. D. Baines. 2009. Effects of major capsid proteins, capsid assembly, and DNA cleavage/packaging on the pUL17/pUL25 complex of herpes simplex virus 1. J. Virol. 83:12725-12737.
    • (2009) J. Virol. , vol.83 , pp. 12725-12737
    • Scholtes, L.1    Baines, J.D.2
  • 81
    • 24944532259 scopus 로고    scopus 로고
    • Cytoplasmic organization of Poxvirus DNA replication
    • Schramm, B., and J. K. Krijnse-Locker. 2005. Cytoplasmic organization of Poxvirus DNA replication. Traffic 6:839-846.
    • (2005) Traffic , vol.6 , pp. 839-846
    • Schramm, B.1    Krijnse-Locker, J.K.2
  • 82
    • 0014095550 scopus 로고
    • The infection of Escherichia coli by T2 and T4 bacteriophages as seen in the electron microscope. I. Attachment and penetration
    • Simon, L. D., and T. F. Anderson. 1967. The infection of Escherichia coli by T2 and T4 bacteriophages as seen in the electron microscope. I. Attachment and penetration. Virology 32:279-297.
    • (1967) Virology , vol.32 , pp. 279-297
    • Simon, L.D.1    Anderson, T.F.2
  • 83
    • 33646733648 scopus 로고    scopus 로고
    • Role of the herpes simplex virus helicase-primase complex during adeno-associated virus DNA replication
    • Slanina, H., S. Weger, N. D. Stow, A. Kuhrs, and R. Heilbronn. 2006. Role of the herpes simplex virus helicase-primase complex during adeno-associated virus DNA replication. J. Virol. 80:5241-5250.
    • (2006) J. Virol. , vol.80 , pp. 5241-5250
    • Slanina, H.1    Weger, S.2    Stow, N.D.3    Kuhrs, A.4    Heilbronn, R.5
  • 84
    • 0030896925 scopus 로고    scopus 로고
    • Microtubule-mediated transport of incoming herpes simplex virus 1 capsids to the nucleus
    • Sodeik, B., M. W. Ebersold, and A. Helenius. 1997. Microtubule-mediated transport of incoming herpes simplex virus 1 capsids to the nucleus. J. Cell Biol. 136:1007-1021.
    • (1997) J. Cell Biol. , vol.136 , pp. 1007-1021
    • Sodeik, B.1    Ebersold, M.W.2    Helenius, A.3
  • 85
    • 17044440108 scopus 로고    scopus 로고
    • Virus maturation: Dynamics and mechanism of a stabilizing structural transition that leads to infectivity
    • Steven, A. C., J. B. Heymann, N. Cheng, B. L. Trus, and J. F. Conway. 2005. Virus maturation: dynamics and mechanism of a stabilizing structural transition that leads to infectivity. Curr. Opin. Struct. Biol. 15:227-236.
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 227-236
    • Steven, A.C.1    Heymann, J.B.2    Cheng, N.3    Trus, B.L.4    Conway, J.F.5
  • 86
    • 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. 2001. Packaging of genomic and amplicon DNA by the herpes simplex virus type 1 UL25-null mutant KUL25NS. J. Virol. 75:10755-10765.
    • (2001) J. Virol. , vol.75 , pp. 10755-10765
    • Stow, N.D.1
  • 87
    • 33144469676 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 DNA-packaging protein UL17 is required for efficient binding of UL25 to capsids
    • Thurlow, J. K., M. Murphy, N. D. Stow, and V. G. Preston. 2006. Herpes simplex virus type 1 DNA-packaging protein UL17 is required for efficient binding of UL25 to capsids. J. Virol. 80:2118-2126.
    • (2006) J. Virol. , vol.80 , pp. 2118-2126
    • Thurlow, J.K.1    Murphy, M.2    Stow, N.D.3    Preston, V.G.4
  • 88
    • 10644290789 scopus 로고    scopus 로고
    • The herpes simplex virus type 1 DNA packaging protein UL17 is a virion protein that is present in both the capsid and the tegument compartments
    • Thurlow, J. K., et al. 2005. The herpes simplex virus type 1 DNA packaging protein UL17 is a virion protein that is present in both the capsid and the tegument compartments. J. Virol. 79:150-158.
    • (2005) J. Virol. , vol.79 , pp. 150-158
    • Thurlow, J.K.1
  • 89
    • 0035195085 scopus 로고    scopus 로고
    • Import of adenovirus DNA involves the nuclear pore complex receptor CAN/Nup214 and histone H1
    • Trotman, L. C., N. Mosberger, M. Fornerod, R. P. Stidwill, and U. F. Greber. 2001. Import of adenovirus DNA involves the nuclear pore complex receptor CAN/Nup214 and histone H1. Nat. Cell Biol. 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
  • 90
    • 7644228864 scopus 로고    scopus 로고
    • Structure and polymorphism of the UL6 portal protein of herpes simplex virus type 1
    • Trus, B. L., et al. 2004. Structure and polymorphism of the UL6 portal protein of herpes simplex virus type 1. J. Virol. 78:12668-12671.
    • (2004) J. Virol. , vol.78 , pp. 12668-12671
    • Trus, B.L.1
  • 91
    • 0026490068 scopus 로고
    • Distinct monoclonal antibodies separately label the hexons or the pentons of herpes simplex virus capsid
    • Trus, B. L., W. W. Newcomb, F. P. Booy, J. C. Brown, and A. C. Steven. 1992. Distinct monoclonal antibodies separately label the hexons or the pentons of herpes simplex virus capsid. Proc. Natl. Acad. Sci. U. S. A. 89:11508-11512.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 11508-11512
    • Trus, B.L.1    Newcomb, W.W.2    Booy, F.P.3    Brown, J.C.4    Steven, A.C.5
  • 92
    • 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., et al. 2007. Allosteric signaling and a nuclear exit strategy: binding of UL25/UL17 heterodimers to DNA-filled HSV-1 capsids. Mol. Cell 26:479-489.
    • (2007) Mol. Cell , vol.26 , pp. 479-489
    • Trus, B.L.1
  • 93
    • 21644443202 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 capsids transit by the trans-Golgi network, where viral glycoproteins accumulate independently of capsid egress
    • Turcotte, S., J. Letellier, and R. Lipṕe. 2005. Herpes simplex virus type 1 capsids transit by the trans-Golgi network, where viral glycoproteins accumulate independently of capsid egress. J. Virol. 79:8847-8860.
    • (2005) J. Virol. , vol.79 , pp. 8847-8860
    • Turcotte, S.1    Letellier, J.2    Lipṕe, R.3
  • 94
    • 4644312884 scopus 로고    scopus 로고
    • Identification of proteins in human cytomeg-alovirus (HCMV) particles: The HCMV proteome
    • Varnum, S. M., et al. 2004. Identification of proteins in human cytomeg-alovirus (HCMV) particles: the HCMV proteome. J. Virol. 78:10960- 10966.
    • (2004) J. Virol. , vol.78
    • Varnum, S.M.1
  • 95
    • 33750352438 scopus 로고    scopus 로고
    • Herpes simplex virus 1 DNA packaging proteins encoded by UL6, UL15, UL17, UL28, and UL33 are located on the external surface of the viral capsid
    • Wills, E., L. Scholtes, and J. D. Baines. 2006. Herpes simplex virus 1 DNA packaging proteins encoded by UL6, UL15, UL17, UL28, and UL33 are located on the external surface of the viral capsid. J. Virol. 80:10894-10899.
    • (2006) J. Virol. , vol.80 , pp. 10894-10899
    • Wills, E.1    Scholtes, L.2    Baines, J.D.3
  • 96
    • 32944467134 scopus 로고    scopus 로고
    • The inner tegument promotes herpes simplex virus capsid motility along microtubules in vitro
    • Wolfstein, A., et al. 2006. The inner tegument promotes herpes simplex virus capsid motility along microtubules in vitro. Traffic 7:227-237.
    • (2006) Traffic , vol.7 , pp. 227-237
    • Wolfstein, A.1
  • 97
    • 0036109089 scopus 로고    scopus 로고
    • Efficient infection by a recombinant Kaposi's sarcoma-associated herpesvirus cloned in a bacterial artificial chromosome: Application for genetic analysis
    • Zhou, F. C., et al. 2002. Efficient infection by a recombinant Kaposi's sarcoma-associated herpesvirus cloned in a bacterial artificial chromosome: application for genetic analysis. J. Virol. 76:6185-6196.
    • (2002) J. Virol. , vol.76 , pp. 6185-6196
    • Zhou, F.C.1
  • 98
    • 33845422049 scopus 로고    scopus 로고
    • Functional characterization of Kaposi's sarcoma-associated herpesvirus ORF45 by bacterial artificial chromosome-based mutagenesis
    • Zhu, F. X., X. Li, F. Zhou, S. J. Gao, and Y. Yuan. 2006. Functional characterization of Kaposi's sarcoma-associated herpesvirus ORF45 by bacterial artificial chromosome-based mutagenesis. J. Virol. 80:12187-12196.
    • (2006) J. Virol. , vol.80 , pp. 12187-12196
    • Zhu, F.X.1    Li, X.2    Zhou, F.3    Gao, S.J.4    Yuan, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.