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Volumn 454-455, Issue 1, 2014, Pages 311-327

Varicella-zoster virus induces the formation of dynamic nuclear capsid aggregates

Author keywords

Assembly; Capsid; Correlative microscopy; Fluorescent virus; Herpesvirus; ORF23; UL36; UL37; VP26; VZV

Indexed keywords

CAPSID PROTEIN; ENHANCED GREEN FLUORESCENT PROTEIN; SCAFFOLD PROTEIN;

EID: 84897079727     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2014.02.023     Document Type: Article
Times cited : (19)

References (55)
  • 1
    • 43949107502 scopus 로고    scopus 로고
    • Identification of a highly conserved, functional nuclear localization signal within the N-terminal region of herpes simplex virus type 1 VP1-2 tegument protein
    • Abaitua F., O'Hare P. Identification of a highly conserved, functional nuclear localization signal within the N-terminal region of herpes simplex virus type 1 VP1-2 tegument protein. J. Virol. 2008, 82:5234-5244.
    • (2008) J. Virol. , vol.82 , pp. 5234-5244
    • Abaitua, F.1    O'Hare, P.2
  • 2
    • 0030055588 scopus 로고    scopus 로고
    • Varicella-zoster virus
    • Arvin A.M. Varicella-zoster virus. Clin. Microbiol. Rev. 1996, 9:361-381.
    • (1996) Clin. Microbiol. Rev. , vol.9 , pp. 361-381
    • Arvin, A.M.1
  • 3
    • 34147100237 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 tegument proteins VP1/2 and UL37 are associated with intranuclear capsids
    • Bucks M.A., O'Regan K.J., Murphy M.A., Wills J.W., Courtney R.J. Herpes simplex virus type 1 tegument proteins VP1/2 and UL37 are associated with intranuclear capsids. Virology 2007, 361:316-324.
    • (2007) Virology , vol.361 , pp. 316-324
    • Bucks, M.A.1    O'Regan, K.J.2    Murphy, M.A.3    Wills, J.W.4    Courtney, R.J.5
  • 4
    • 0028237175 scopus 로고
    • Preexisting nuclear architecture defines the intranuclear location of herpesvirus DNA replication structures
    • de Bruyn Kops A., Knipe D.M. Preexisting nuclear architecture defines the intranuclear location of herpesvirus DNA replication structures. J. Virol. 1994, 68:3512-3526.
    • (1994) J. Virol. , vol.68 , pp. 3512-3526
    • de Bruyn Kops, A.1    Knipe, D.M.2
  • 5
    • 0032488265 scopus 로고    scopus 로고
    • Comparison of the intranuclear distributions of herpes simplex virus proteins involved in various viral functions
    • de Bruyn Kops A., Uprichard S.L., Chen M., Knipe D.M. Comparison of the intranuclear distributions of herpes simplex virus proteins involved in various viral functions. Virology 1998, 252:162-178.
    • (1998) Virology , vol.252 , pp. 162-178
    • de Bruyn Kops, A.1    Uprichard, S.L.2    Chen, M.3    Knipe, D.M.4
  • 6
    • 84858240360 scopus 로고    scopus 로고
    • Procapsid assembly, maturation, nuclear exit: dynamic steps in the production of infectious herpesvirions
    • Cardone G., Heymann J.B., Cheng N., Trus B.L., Steven A.C. Procapsid assembly, maturation, nuclear exit: dynamic steps in the production of infectious herpesvirions. Adv. Exp. Med. Biol. 2012, 726:423-439.
    • (2012) Adv. Exp. Med. Biol. , vol.726 , pp. 423-439
    • Cardone, G.1    Heymann, J.B.2    Cheng, N.3    Trus, B.L.4    Steven, A.C.5
  • 7
    • 53749105230 scopus 로고    scopus 로고
    • Functions of Varicella-zoster virus ORF23 capsid protein in viral replication and the pathogenesis of skin infection
    • Chaudhuri V., Sommer M., Rajamani J., Zerboni L., Arvin A.M. Functions of Varicella-zoster virus ORF23 capsid protein in viral replication and the pathogenesis of skin infection. J. Virol. 2008, 82:10231-10246.
    • (2008) J. Virol. , vol.82 , pp. 10231-10246
    • Chaudhuri, V.1    Sommer, M.2    Rajamani, J.3    Zerboni, L.4    Arvin, A.M.5
  • 8
    • 0036635530 scopus 로고    scopus 로고
    • Characterization of varicella-zoster virus gene 21 and 29 proteins in infected cells
    • Cohrs R.J., Wischer J., Essman C., Gilden D.H. Characterization of varicella-zoster virus gene 21 and 29 proteins in infected cells. J. Virol. 2002, 76:7228-7238.
    • (2002) J. Virol. , vol.76 , pp. 7228-7238
    • Cohrs, R.J.1    Wischer, J.2    Essman, C.3    Gilden, D.H.4
  • 9
    • 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., Lee J.I., Ueda A., Smith G.A. The capsid and tegument of the alphaherpesviruses are linked by an interaction between the UL25 and VP1/2 proteins. J. Virol. 2007, 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
  • 10
    • 0037213596 scopus 로고    scopus 로고
    • Residues of VP26 of herpes simplex virus type 1 that are required for its interaction with capsids
    • Desai P., Akpa J.C., Person S. Residues of VP26 of herpes simplex virus type 1 that are required for its interaction with capsids. J. Virol. 2003, 77:391-404.
    • (2003) J. Virol. , vol.77 , pp. 391-404
    • Desai, P.1    Akpa, J.C.2    Person, S.3
  • 11
    • 0031846233 scopus 로고    scopus 로고
    • Incorporation of the green fluorescent protein into the herpes simplex virus type 1 capsid
    • Desai P., Person S. Incorporation of the green fluorescent protein into the herpes simplex virus type 1 capsid. J. Virol. 1998, 72:7563-7568.
    • (1998) J. Virol. , vol.72 , pp. 7563-7568
    • Desai, P.1    Person, S.2
  • 12
    • 55549112567 scopus 로고    scopus 로고
    • Localization of herpes simplex virus type 1 UL37 in the Golgi complex requires UL36 but not capsid structures
    • Desai P., Sexton G.L., Huang E., Person S. Localization of herpes simplex virus type 1 UL37 in the Golgi complex requires UL36 but not capsid structures. J. Virol. 2008, 82:11354-11361.
    • (2008) J. Virol. , vol.82 , pp. 11354-11361
    • Desai, P.1    Sexton, G.L.2    Huang, E.3    Person, S.4
  • 13
    • 0034785814 scopus 로고    scopus 로고
    • A null mutation in the gene encoding the herpes simplex virus type 1 UL37 polypeptide abrogates virus maturation
    • Desai P., Sexton G.L., McCaffery J.M., Person S. A null mutation in the gene encoding the herpes simplex virus type 1 UL37 polypeptide abrogates virus maturation. J. Virol. 2001, 75:10259-10271.
    • (2001) J. Virol. , vol.75 , pp. 10259-10271
    • Desai, P.1    Sexton, G.L.2    McCaffery, J.M.3    Person, S.4
  • 14
    • 0034466764 scopus 로고    scopus 로고
    • A null mutation in the UL36 gene of herpes simplex virus type 1 results in accumulation of unenveloped DNA-filled capsids in the cytoplasm of infected cells
    • Desai P.J. A null mutation in the UL36 gene of herpes simplex virus type 1 results in accumulation of unenveloped DNA-filled capsids in the cytoplasm of infected cells. J. Virol. 2000, 74:11608-11618.
    • (2000) J. Virol. , vol.74 , pp. 11608-11618
    • Desai, P.J.1
  • 16
    • 84876339135 scopus 로고    scopus 로고
    • Analysis of the early steps of herpes simplex virus 1 capsid tegumentation
    • Henaff D., Remillard-Labrosse G., Loret S., Lippe R. Analysis of the early steps of herpes simplex virus 1 capsid tegumentation. J. Virol. 2013, 87:4895-4906.
    • (2013) J. Virol. , vol.87 , pp. 4895-4906
    • Henaff, D.1    Remillard-Labrosse, G.2    Loret, S.3    Lippe, R.4
  • 18
    • 0030871678 scopus 로고    scopus 로고
    • Capsid assembly and DNA packaging in herpes simplex virus
    • Homa F.L., Brown J.C. Capsid assembly and DNA packaging in herpes simplex virus. Rev. Med. Virol. 1997, 7:107-122.
    • (1997) Rev. Med. Virol. , vol.7 , pp. 107-122
    • Homa, F.L.1    Brown, J.C.2
  • 19
    • 0036784583 scopus 로고    scopus 로고
    • Sequential localization of two herpes simplex virus tegument proteins to punctate nuclear dots adjacent to ICP0 domains
    • Hutchinson I., Whiteley A., Browne H., Elliott G. Sequential localization of two herpes simplex virus tegument proteins to punctate nuclear dots adjacent to ICP0 domains. J. Virol. 2002, 76:10365-10373.
    • (2002) J. Virol. , vol.76 , pp. 10365-10373
    • Hutchinson, I.1    Whiteley, A.2    Browne, H.3    Elliott, G.4
  • 20
    • 84855196271 scopus 로고    scopus 로고
    • Identification of a single amino acid residue which is critical for the interaction between HSV-1 inner tegument proteins pUL36 and pUL37
    • Kelly B.J., Mijatov B., Fraefel C., Cunningham A.L., Diefenbach R.J. Identification of a single amino acid residue which is critical for the interaction between HSV-1 inner tegument proteins pUL36 and pUL37. Virology 2012, 422:308-316.
    • (2012) Virology , vol.422 , pp. 308-316
    • Kelly, B.J.1    Mijatov, B.2    Fraefel, C.3    Cunningham, A.L.4    Diefenbach, R.J.5
  • 21
    • 0029052417 scopus 로고
    • The transcriptional regulatory proteins encoded by varicella-zoster virus open reading frames (ORFs) 4 and 63, but not ORF 61, are associated with purified virus particles
    • Kinchington P.R., Bookey D., Turse S.E. The transcriptional regulatory proteins encoded by varicella-zoster virus open reading frames (ORFs) 4 and 63, but not ORF 61, are associated with purified virus particles. J. Virol. 1995, 69:4274-4282.
    • (1995) J. Virol. , vol.69 , pp. 4274-4282
    • Kinchington, P.R.1    Bookey, D.2    Turse, S.E.3
  • 22
    • 0036191216 scopus 로고    scopus 로고
    • Pseudorabies virus UL36 tegument protein physically interacts with the UL37 protein
    • Klupp B.G., Fuchs W., Granzow H., Nixdorf R., Mettenleiter T.C. Pseudorabies virus UL36 tegument protein physically interacts with the UL37 protein. J. Virol. 2002, 76:3065-3071.
    • (2002) J. Virol. , vol.76 , pp. 3065-3071
    • Klupp, B.G.1    Fuchs, W.2    Granzow, H.3    Nixdorf, R.4    Mettenleiter, T.C.5
  • 23
    • 0034849764 scopus 로고    scopus 로고
    • Pseudorabies virus UL37 gene product is involved in secondary envelopment
    • Klupp B.G., Granzow H., Mundt E., Mettenleiter T.C. Pseudorabies virus UL37 gene product is involved in secondary envelopment. J. Virol. 2001, 75:8927-8936.
    • (2001) J. Virol. , vol.75 , pp. 8927-8936
    • Klupp, B.G.1    Granzow, H.2    Mundt, E.3    Mettenleiter, T.C.4
  • 24
    • 84855247959 scopus 로고    scopus 로고
    • Herpesvirus replication compartments originate with single incoming viral genomes
    • e00278-11
    • Kobiler O., Brodersen P., Taylor M.P., Ludmir E.B., Enquist L.W. Herpesvirus replication compartments originate with single incoming viral genomes. mBio 2011, 2:e00278-11.
    • (2011) mBio , vol.2
    • Kobiler, O.1    Brodersen, P.2    Taylor, M.P.3    Ludmir, E.B.4    Enquist, L.W.5
  • 25
    • 70349756954 scopus 로고    scopus 로고
    • Complementation of a herpes simplex virus ICP0 null mutant by varicella-zoster virus ORF61p
    • Kyratsous C.A., Walters M.S., Panagiotidis C.A., Silverstein S.J. Complementation of a herpes simplex virus ICP0 null mutant by varicella-zoster virus ORF61p. J. Virol. 2009, 83:10637-10643.
    • (2009) J. Virol. , vol.83 , pp. 10637-10643
    • Kyratsous, C.A.1    Walters, M.S.2    Panagiotidis, C.A.3    Silverstein, S.J.4
  • 26
    • 49049113021 scopus 로고    scopus 로고
    • Identification of structural protein-protein interactions of herpes simplex virus type 1
    • Lee J.H., Vittone V., Diefenbach E., Cunningham A.L., Diefenbach R.J. Identification of structural protein-protein interactions of herpes simplex virus type 1. Virology 2008, 378:347-354.
    • (2008) Virology , vol.378 , pp. 347-354
    • Lee, J.H.1    Vittone, V.2    Diefenbach, E.3    Cunningham, A.L.4    Diefenbach, R.J.5
  • 27
    • 33845421600 scopus 로고    scopus 로고
    • Identification of an essential domain in the herpesvirus VP1/2 tegument protein: the carboxy terminus directs incorporation into capsid assemblons
    • Lee J.I., Luxton G.W., Smith G.A. Identification of an essential domain in the herpesvirus VP1/2 tegument protein: the carboxy terminus directs incorporation into capsid assemblons. J. Virol. 2006, 80:12086-12094.
    • (2006) J. Virol. , vol.80 , pp. 12086-12094
    • Lee, J.I.1    Luxton, G.W.2    Smith, G.A.3
  • 29
    • 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., Haverlock S., Coller K.E., Antinone S.E., Pincetic A., Smith G.A. Targeting of herpesvirus capsid transport in axons is coupled to association with specific sets of tegument proteins. Proc. Natl. Acad. Sci. U.S.A. 2005, 102:5832-5837.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 5832-5837
    • Luxton, G.W.1    Haverlock, S.2    Coller, K.E.3    Antinone, S.E.4    Pincetic, A.5    Smith, G.A.6
  • 30
    • 32944480977 scopus 로고    scopus 로고
    • The pseudorabies virus VP1/2 tegument protein is required for intracellular capsid transport
    • Luxton G.W., Lee J.I., Haverlock-Moyns S., Schober J.M., Smith G.A. The pseudorabies virus VP1/2 tegument protein is required for intracellular capsid transport. J. Virol. 2006, 80:201-209.
    • (2006) J. Virol. , vol.80 , pp. 201-209
    • Luxton, G.W.1    Lee, J.I.2    Haverlock-Moyns, S.3    Schober, J.M.4    Smith, G.A.5
  • 31
    • 0033989722 scopus 로고    scopus 로고
    • Small dense nuclear bodies are the site of localization of herpes simplex virus 1 U(L)3 and U(L)4 proteins and of ICP22 only when the latter protein is present
    • Markovitz N.S., Roizman B. Small dense nuclear bodies are the site of localization of herpes simplex virus 1 U(L)3 and U(L)4 proteins and of ICP22 only when the latter protein is present. J. Virol. 2000, 74:523-528.
    • (2000) J. Virol. , vol.74 , pp. 523-528
    • Markovitz, N.S.1    Roizman, B.2
  • 32
    • 0026787060 scopus 로고
    • Characterization of the large tegument protein (ICP1/2) of herpes simplex virus type 1
    • McNabb D.S., Courtney R.J. Characterization of the large tegument protein (ICP1/2) of herpes simplex virus type 1. Virology 1992, 190:221-232.
    • (1992) Virology , vol.190 , pp. 221-232
    • McNabb, D.S.1    Courtney, R.J.2
  • 33
    • 70349286031 scopus 로고    scopus 로고
    • Intracellular localization of the pseudorabies virus large tegument protein pUL36
    • Mohl B.S., Bottcher S., Granzow H., Kuhn J., Klupp B.G., Mettenleiter T.C. Intracellular localization of the pseudorabies virus large tegument protein pUL36. J. Virol. 2009, 83:9641-9651.
    • (2009) J. Virol. , vol.83 , pp. 9641-9651
    • Mohl, B.S.1    Bottcher, S.2    Granzow, H.3    Kuhn, J.4    Klupp, B.G.5    Mettenleiter, T.C.6
  • 34
    • 0031693694 scopus 로고    scopus 로고
    • Differences in the intracellular localization and fate of herpes simplex virus tegument proteins early in the infection of Vero cells
    • Morrison E.E., Stevenson A.J., Wang Y.F., Meredith D.M. Differences in the intracellular localization and fate of herpes simplex virus tegument proteins early in the infection of Vero cells. J. Gen. Virol. 1998, 79(Pt 10):2517-2528.
    • (1998) J. Gen. Virol. , vol.79 , Issue.PART 10 , pp. 2517-2528
    • Morrison, E.E.1    Stevenson, A.J.2    Wang, Y.F.3    Meredith, D.M.4
  • 35
    • 84865635245 scopus 로고    scopus 로고
    • Improper tagging of the non-essential small capsid protein VP26 impairs nuclear capsid egress of herpes simplex virus
    • Nagel C.H., Dohner K., Binz A., Bauerfeind R., Sodeik B. Improper tagging of the non-essential small capsid protein VP26 impairs nuclear capsid egress of herpes simplex virus. PloS One 2012, 7:e44177.
    • (2012) PloS One , vol.7
    • Nagel, C.H.1    Dohner, K.2    Binz, A.3    Bauerfeind, R.4    Sodeik, B.5
  • 36
    • 0030298322 scopus 로고    scopus 로고
    • Assembly of the herpes simplex virus capsid: characterization of intermediates observed during cell-free capsid formation
    • Newcomb W.W., Homa F.L., Thomsen D.R., Booy F.P., Trus B.L., Steven A.C., Spencer J.V., Brown J.C. Assembly of the herpes simplex virus capsid: characterization of intermediates observed during cell-free capsid formation. J. Mol. Biol. 1996, 263:432-446.
    • (1996) J. Mol. Biol. , vol.263 , pp. 432-446
    • Newcomb, W.W.1    Homa, F.L.2    Thomsen, D.R.3    Booy, F.P.4    Trus, B.L.5    Steven, A.C.6    Spencer, J.V.7    Brown, J.C.8
  • 37
    • 0032899606 scopus 로고    scopus 로고
    • Assembly of the herpes simplex virus procapsid from purified components and identification of small complexes containing the major capsid and scaffolding proteins
    • Newcomb W.W., Homa F.L., Thomsen D.R., Trus B.L., Cheng N., Steven A., Booy F., Brown J.C. Assembly of the herpes simplex virus procapsid from purified components and identification of small complexes containing the major capsid and scaffolding proteins. J. Virol. 1999, 73:4239-4250.
    • (1999) J. Virol. , vol.73 , pp. 4239-4250
    • Newcomb, W.W.1    Homa, F.L.2    Thomsen, D.R.3    Trus, B.L.4    Cheng, N.5    Steven, A.6    Booy, F.7    Brown, J.C.8
  • 40
    • 47049094548 scopus 로고    scopus 로고
    • Small capsid protein pORF65 is essential for assembly of Kaposi's sarcoma-associated herpesvirus capsids
    • Perkins E.M., Anacker D., Davis A., Sankar V., Ambinder R.F., Desai P. Small capsid protein pORF65 is essential for assembly of Kaposi's sarcoma-associated herpesvirus capsids. J. Virol. 2008, 82:7201-7211.
    • (2008) J. Virol. , vol.82 , pp. 7201-7211
    • Perkins, E.M.1    Anacker, D.2    Davis, A.3    Sankar, V.4    Ambinder, R.F.5    Desai, P.6
  • 41
    • 0021233256 scopus 로고
    • The intranuclear location of a herpes simplex virus DNA-binding protein is determined by the status of viral DNA replication
    • Quinlan M.P., Chen L.B., Knipe D.M. The intranuclear location of a herpes simplex virus DNA-binding protein is determined by the status of viral DNA replication. Cell 1984, 36:857-868.
    • (1984) Cell , vol.36 , pp. 857-868
    • Quinlan, M.P.1    Chen, L.B.2    Knipe, D.M.3
  • 42
    • 84864044838 scopus 로고    scopus 로고
    • 3D reconstruction of VZV infected cell nuclei and PML nuclear cages by serial section array scanning electron microscopy and electron tomography
    • Reichelt M., Joubert L., Perrino J., Koh A.L., Phanwar I., Arvin A.M. 3D reconstruction of VZV infected cell nuclei and PML nuclear cages by serial section array scanning electron microscopy and electron tomography. PLoS Pathog. 2012, 8:e1002740.
    • (2012) PLoS Pathog. , vol.8
    • Reichelt, M.1    Joubert, L.2    Perrino, J.3    Koh, A.L.4    Phanwar, I.5    Arvin, A.M.6
  • 43
  • 44
    • 84874746658 scopus 로고    scopus 로고
    • ORF9p phosphorylation by ORF47p is crucial for the formation and egress of varicella-zoster virus viral particles
    • Riva L., Thiry M., Bontems S., Joris A., Piette J., Lebrun M., Sadzot-Delvaux C. ORF9p phosphorylation by ORF47p is crucial for the formation and egress of varicella-zoster virus viral particles. J. Virol. 2013, 87:2868-2881.
    • (2013) J. Virol. , vol.87 , pp. 2868-2881
    • Riva, L.1    Thiry, M.2    Bontems, S.3    Joris, A.4    Piette, J.5    Lebrun, M.6    Sadzot-Delvaux, C.7
  • 45
    • 0031967148 scopus 로고    scopus 로고
    • The herpes simplex virus type 1 U(L)17 gene encodes virion tegument proteins that are required for cleavage and packaging of viral DNA
    • Salmon B., Cunningham C., Davison A.J., Harris W.J., Baines J.D. The herpes simplex virus type 1 U(L)17 gene encodes virion tegument proteins that are required for cleavage and packaging of viral DNA. J. Virol. 1998, 72:3779-3788.
    • (1998) J. Virol. , vol.72 , pp. 3779-3788
    • Salmon, B.1    Cunningham, C.2    Davison, A.J.3    Harris, W.J.4    Baines, J.D.5
  • 46
    • 8644272418 scopus 로고    scopus 로고
    • Local modulation of plus-end transport targets herpesvirus entry and egress in sensory axons
    • Smith G.A., Pomeranz L., Gross S.P., Enquist L.W. Local modulation of plus-end transport targets herpesvirus entry and egress in sensory axons. Proc. Natl. Acad. Sci. U.S.A. 2004, 101:16034-16039.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 16034-16039
    • Smith, G.A.1    Pomeranz, L.2    Gross, S.P.3    Enquist, L.W.4
  • 47
    • 0031980307 scopus 로고    scopus 로고
    • Assembly of the herpes simplex virus capsid: preformed triplexes bind to the nascent capsid
    • Spencer J.V., Newcomb W.W., Thomsen D.R., Homa F.L., Brown J.C. Assembly of the herpes simplex virus capsid: preformed triplexes bind to the nascent capsid. J. Virol. 1998, 72:3944-3951.
    • (1998) J. Virol. , vol.72 , pp. 3944-3951
    • Spencer, J.V.1    Newcomb, W.W.2    Thomsen, D.R.3    Homa, F.L.4    Brown, J.C.5
  • 48
    • 77949440090 scopus 로고    scopus 로고
    • Improving the yeast two-hybrid system with permutated fusions proteins: the Varicella Zoster Virus interactome
    • Stellberger T., Hauser R., Baiker A., Pothineni V.R., Haas J., Uetz P. Improving the yeast two-hybrid system with permutated fusions proteins: the Varicella Zoster Virus interactome. Prot. Sci. 2010, 8:8.
    • (2010) Prot. Sci. , vol.8 , pp. 8
    • Stellberger, T.1    Hauser, R.2    Baiker, A.3    Pothineni, V.R.4    Haas, J.5    Uetz, P.6
  • 49
    • 43949089146 scopus 로고    scopus 로고
    • Simultaneous tracking of capsid, tegument, and envelope protein localization in living cells infected with triply fluorescent herpes simplex virus 1
    • Sugimoto K., Uema M., Sagara H., Tanaka M., Sata T., Hashimoto Y., Kawaguchi Y. Simultaneous tracking of capsid, tegument, and envelope protein localization in living cells infected with triply fluorescent herpes simplex virus 1. J. Virol. 2008, 82:5198-5211.
    • (2008) J. Virol. , vol.82 , pp. 5198-5211
    • Sugimoto, K.1    Uema, M.2    Sagara, H.3    Tanaka, M.4    Sata, T.5    Hashimoto, Y.6    Kawaguchi, Y.7
  • 50
    • 0032488237 scopus 로고    scopus 로고
    • The herpes simplex virus 1 UL 17 gene is required for localization of capsids and major and minor capsid proteins to intranuclear sites where viral DNA is cleaved and packaged
    • Taus N.S., Salmon B., Baines J.D. The herpes simplex virus 1 UL 17 gene is required for localization of capsids and major and minor capsid proteins to intranuclear sites where viral DNA is cleaved and packaged. Virology 1998, 252:115-125.
    • (1998) Virology , vol.252 , pp. 115-125
    • Taus, N.S.1    Salmon, B.2    Baines, J.D.3
  • 51
    • 0029019922 scopus 로고
    • Assembly of the herpes simplex virus capsid: requirement for the carboxyl-terminal twenty-five amino acids of the proteins encoded by the UL26 and UL26.5 genes
    • Thomsen D.R., Newcomb W.W., Brown J.C., Homa F.L. Assembly of the herpes simplex virus capsid: requirement for the carboxyl-terminal twenty-five amino acids of the proteins encoded by the UL26 and UL26.5 genes. J. Virol. 1995, 69:3690-3703.
    • (1995) J. Virol. , vol.69 , pp. 3690-3703
    • Thomsen, D.R.1    Newcomb, W.W.2    Brown, J.C.3    Homa, F.L.4
  • 52
    • 0029908793 scopus 로고    scopus 로고
    • The herpes simplex virus procapsid: structure, conformational changes upon maturation, and roles of the triplex proteins VP19c and VP23 in assembly
    • Trus B.L., Booy F.P., Newcomb W.W., Brown J.C., Homa F.L., Thomsen D.R., Steven A.C. The herpes simplex virus procapsid: structure, conformational changes upon maturation, and roles of the triplex proteins VP19c and VP23 in assembly. J. Mol. Biol. 1996, 263:447-462.
    • (1996) J. Mol. Biol. , vol.263 , pp. 447-462
    • Trus, B.L.1    Booy, F.P.2    Newcomb, W.W.3    Brown, J.C.4    Homa, F.L.5    Thomsen, D.R.6    Steven, A.C.7
  • 53
    • 34248583632 scopus 로고    scopus 로고
    • Allosteric signaling and a nuclear exit strategy: binding of UL25/UL17 heterodimers to DNA-Filled HSV-1 capsids
    • Trus B.L., Newcomb W.W., Cheng N., Cardone G., Marekov L., Homa F.L., Brown J.C., Steven A.C. Allosteric signaling and a nuclear exit strategy: binding of UL25/UL17 heterodimers to DNA-Filled HSV-1 capsids. Mol. Cell 2007, 26:479-489.
    • (2007) Mol. Cell , vol.26 , pp. 479-489
    • Trus, B.L.1    Newcomb, W.W.2    Cheng, N.3    Cardone, G.4    Marekov, L.5    Homa, F.L.6    Brown, J.C.7    Steven, A.C.8
  • 54
    • 0029942272 scopus 로고    scopus 로고
    • Assemblons: nuclear structures defined by aggregation of immature capsids and some tegument proteins of herpes simplex virus 1
    • Ward P.L., Ogle W.O., Roizman B. Assemblons: nuclear structures defined by aggregation of immature capsids and some tegument proteins of herpes simplex virus 1. J. Virol. 1996, 70:4623-4631.
    • (1996) J. Virol. , vol.70 , pp. 4623-4631
    • Ward, P.L.1    Ogle, W.O.2    Roizman, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.