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Volumn 15, Issue 12, 2015, Pages 1943-1956

Investigating the biology of alpha herpesviruses with MS-based proteomics

Author keywords

Alpha herpesvirus; Animal proteomics; BHV 1; HSV 1; PRV; VZV

Indexed keywords

PROTEOME; VIRUS DNA; VIRUS PROTEIN; VIRAL PROTEIN;

EID: 84931004252     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201400604     Document Type: Review
Times cited : (34)

References (107)
  • 3
    • 0035073814 scopus 로고    scopus 로고
    • The nine ages of herpes simplex virus
    • Roizman, B., Whitley, R. J., The nine ages of herpes simplex virus. Herpes 2001, 8, 23-27.
    • (2001) Herpes , vol.8 , pp. 23-27
    • Roizman, B.1    Whitley, R.J.2
  • 4
    • 0035849323 scopus 로고    scopus 로고
    • Herpes simplex virus infections
    • Whitley, R. J., Roizman, B., Herpes simplex virus infections. Lancet 2001, 357, 1513-1518.
    • (2001) Lancet , vol.357 , pp. 1513-1518
    • Whitley, R.J.1    Roizman, B.2
  • 5
    • 84904351424 scopus 로고    scopus 로고
    • The strategy of herpes simplex virus replication and takeover of the host cell
    • in: Arvin, A., Campadelli-Fiume, G., Mocarski, E., Moore, P. S. (Eds.), Cambridge University Press.
    • Roizman, B., Taddeo, B., The strategy of herpes simplex virus replication and takeover of the host cell, in: Arvin, A., Campadelli-Fiume, G., Mocarski, E., Moore, P. S. et al. (Eds.) Human Herpesviruses: Biology, Therapy, and Immunoprophylaxis, Cambridge University Press 2007.
    • (2007) Human Herpesviruses: Biology, Therapy, and Immunoprophylaxis
    • Roizman, B.1    Taddeo, B.2
  • 6
    • 84894039546 scopus 로고    scopus 로고
    • Molecular mechanisms of varicella zoster virus pathogenesis
    • Zerboni, L., Sen, N., Oliver, S. L., Arvin, A. M., Molecular mechanisms of varicella zoster virus pathogenesis. Nat. Rev. Microbiol. 2014, 12, 197-210.
    • (2014) Nat. Rev. Microbiol. , vol.12 , pp. 197-210
    • Zerboni, L.1    Sen, N.2    Oliver, S.L.3    Arvin, A.M.4
  • 7
    • 84867649395 scopus 로고    scopus 로고
    • Herpesvirus transport to the nervous system and back again
    • Smith, G., Herpesvirus transport to the nervous system and back again. Annu. Rev. Microbiol. 2012, 66, 153-176.
    • (2012) Annu. Rev. Microbiol. , vol.66 , pp. 153-176
    • Smith, G.1
  • 9
    • 84873735486 scopus 로고    scopus 로고
    • Directional spread of alphaherpesviruses in the nervous system
    • Kramer, T. and Enquist, L. W., Directional spread of alphaherpesviruses in the nervous system. Viruses 2013, 5, 678-707.
    • (2013) Viruses , vol.5 , pp. 678-707
    • Kramer, T.1    Enquist, L.W.2
  • 10
    • 85017004540 scopus 로고    scopus 로고
    • The impact of mass spectrometry-based proteomics on fundamental discoveries in virology
    • Greco, T. M., Diner, B. A., Cristea, I. M., The impact of mass spectrometry-based proteomics on fundamental discoveries in virology. Ann. Rev. Virol. 2014, 1, 581-604.
    • (2014) Ann. Rev. Virol. , vol.1 , pp. 581-604
    • Greco, T.M.1    Diner, B.A.2    Cristea, I.M.3
  • 11
    • 84919629153 scopus 로고    scopus 로고
    • Cellular mechanisms of alpha herpesvirus egress: live cell fluorescence microscopy of pseudorabies virus exocytosis
    • Hogue, I. B., Bosse, J. B., Hu, J. R., Thiberge, S. Y. et al., Cellular mechanisms of alpha herpesvirus egress: live cell fluorescence microscopy of pseudorabies virus exocytosis. PLoS Pathog., 2014, 10, e1004535.
    • (2014) PLoS Pathog. , vol.10 , pp. e1004535
    • Hogue, I.B.1    Bosse, J.B.2    Hu, J.R.3    Thiberge, S.Y.4
  • 12
    • 80052069079 scopus 로고    scopus 로고
    • Proteomic characterization of pseudorabies virus extracellular virions
    • Kramer, T., Greco, T. M., Enquist, L. W., Cristea, I. M., Proteomic characterization of pseudorabies virus extracellular virions. J. Virol., 2011, 85, 6427-6441.
    • (2011) J. Virol. , vol.85 , pp. 6427-6441
    • Kramer, T.1    Greco, T.M.2    Enquist, L.W.3    Cristea, I.M.4
  • 13
    • 84867231810 scopus 로고    scopus 로고
    • Deciphering novel host-herpesvirus interactions by virion proteomics
    • Lippe, R., Deciphering novel host-herpesvirus interactions by virion proteomics. Front. Microbiol. 2012, 3, 181.
    • (2012) Front. Microbiol. , vol.3 , pp. 181
    • Lippe, R.1
  • 14
    • 50149119228 scopus 로고    scopus 로고
    • Comprehensive characterization of extracellular herpes simplex virus type 1 virions
    • Loret, S., Guay, G., Lippe, R., Comprehensive characterization of extracellular herpes simplex virus type 1 virions. J. Virol. 2008, 82, 8605-8618.
    • (2008) J. Virol. , vol.82 , pp. 8605-8618
    • Loret, S.1    Guay, G.2    Lippe, R.3
  • 15
    • 84883272572 scopus 로고    scopus 로고
    • Structure of the pseudorabies virus capsid: comparison with herpes simplex virus type 1 and differential binding of essential minor proteins
    • Homa, F. L., Huffman, J. B., Toropova, K., Lopez, H. R. et al., Structure of the pseudorabies virus capsid: comparison with herpes simplex virus type 1 and differential binding of essential minor proteins. J. Mol. Biol. 2013, 425, 3415-3428.
    • (2013) J. Mol. Biol. , vol.425 , pp. 3415-3428
    • Homa, F.L.1    Huffman, J.B.2    Toropova, K.3    Lopez, H.R.4
  • 16
    • 33751414792 scopus 로고    scopus 로고
    • Properties of a herpes simplex virus multiple immediate-early gene-deleted recombinant as a vaccine vector
    • Watanabe, D., Brockman, M. A., Ndung'u, T., Mathews, L. et al., Properties of a herpes simplex virus multiple immediate-early gene-deleted recombinant as a vaccine vector. Virology 2007, 357, 186-198.
    • (2007) Virology , vol.357 , pp. 186-198
    • Watanabe, D.1    Brockman, M.A.2    Ndung'u, T.3    Mathews, L.4
  • 17
    • 0029846871 scopus 로고    scopus 로고
    • The general transcription factors of RNA polymerase II
    • Orphanides, G., Lagrange, T., Reinberg, D., The general transcription factors of RNA polymerase II. Genes Dev. 1996, 10, 2657-2683.
    • (1996) Genes Dev. , vol.10 , pp. 2657-2683
    • Orphanides, G.1    Lagrange, T.2    Reinberg, D.3
  • 18
    • 0029946735 scopus 로고    scopus 로고
    • Interaction of the viral activator protein ICP4 with TFIID through TAF250
    • Carrozza, M. J., DeLuca, N. A., Interaction of the viral activator protein ICP4 with TFIID through TAF250. Mol. Cell Biol. 1996, 16, 3085-3093.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 3085-3093
    • Carrozza, M.J.1    DeLuca, N.A.2
  • 19
    • 79958102996 scopus 로고    scopus 로고
    • Herpes simplex virus 1 ICP4 forms complexes with TFIID and mediator in virus-infected cells
    • Lester, J. T., DeLuca, N. A., Herpes simplex virus 1 ICP4 forms complexes with TFIID and mediator in virus-infected cells. J. Virol. 2011, 85, 5733-5744.
    • (2011) J. Virol. , vol.85 , pp. 5733-5744
    • Lester, J.T.1    DeLuca, N.A.2
  • 20
    • 84885393420 scopus 로고    scopus 로고
    • Temporal association of herpes simplex virus ICP4 with cellular complexes functioning at multiple steps in PolII transcription
    • Wagner, L. M., DeLuca, N. A., Temporal association of herpes simplex virus ICP4 with cellular complexes functioning at multiple steps in PolII transcription. PLoS One 2013, 8, e78242.
    • (2013) PLoS One , vol.8 , pp. e78242
    • Wagner, L.M.1    DeLuca, N.A.2
  • 21
    • 84920885194 scopus 로고    scopus 로고
    • Characterization of a replication-incompetent pseudorabies virus mutant lacking the sole immediate early gene IE180
    • Wu, B. W., Engel, E. A., Enquist, L. W., Characterization of a replication-incompetent pseudorabies virus mutant lacking the sole immediate early gene IE180. MBio 2014, 5(6), e01850.
    • (2014) MBio , vol.5 , Issue.6 , pp. e01850
    • Wu, B.W.1    Engel, E.A.2    Enquist, L.W.3
  • 22
    • 9644289432 scopus 로고    scopus 로고
    • Proteomics of herpes simplex virus infected cell protein 27: association with translation initiation factors
    • Fontaine-Rodriguez, E. C., Taylor, T. J., Olesky, M., Knipe, D. M., Proteomics of herpes simplex virus infected cell protein 27: association with translation initiation factors. Virology 2004, 330, 487-492.
    • (2004) Virology , vol.330 , pp. 487-492
    • Fontaine-Rodriguez, E.C.1    Taylor, T.J.2    Olesky, M.3    Knipe, D.M.4
  • 23
    • 84875938497 scopus 로고    scopus 로고
    • Proteomics analysis of herpes simplex virus type 1-infected cells reveals dynamic changes of viral protein expression, ubiquitylation, and phosphorylation
    • Bell, C., Desjardins, M., Thibault, P., Radtke, K., Proteomics analysis of herpes simplex virus type 1-infected cells reveals dynamic changes of viral protein expression, ubiquitylation, and phosphorylation. J. Proteome Res. 2013, 12, 1820-1829.
    • (2013) J. Proteome Res. , vol.12 , pp. 1820-1829
    • Bell, C.1    Desjardins, M.2    Thibault, P.3    Radtke, K.4
  • 24
    • 11144240022 scopus 로고    scopus 로고
    • Phosphorylation site mutations affect herpes simplex virus type 1 ICP0 function
    • Davido, D. J., von Zagorski, W. F., Lane, W. S., Schaffer, P. A., Phosphorylation site mutations affect herpes simplex virus type 1 ICP0 function. J. Virol. 2005, 79, 1232-1243.
    • (2005) J. Virol. , vol.79 , pp. 1232-1243
    • Davido, D.J.1    von Zagorski, W.F.2    Lane, W.S.3    Schaffer, P.A.4
  • 25
    • 2442653990 scopus 로고    scopus 로고
    • Proteomics of herpes simplex virus replication compartments: association of cellular DNA replication, repair, recombination, and chromatin remodeling proteins with ICP8
    • Taylor, T. J., Knipe, D. M., Proteomics of herpes simplex virus replication compartments: association of cellular DNA replication, repair, recombination, and chromatin remodeling proteins with ICP8. J. Virol. 2004, 78, 5856-5866.
    • (2004) J. Virol. , vol.78 , pp. 5856-5866
    • Taylor, T.J.1    Knipe, D.M.2
  • 26
    • 84903769923 scopus 로고    scopus 로고
    • Co-opting the Fanconi anemia genomic stability pathway enables herpesvirus DNA synthesis and productive growth
    • Karttunen, H., Savas, J. N., McKinney, C., Chen, Y. H. et al., Co-opting the Fanconi anemia genomic stability pathway enables herpesvirus DNA synthesis and productive growth. Mol. Cell 2014, 55, 111-122.
    • (2014) Mol. Cell , vol.55 , pp. 111-122
    • Karttunen, H.1    Savas, J.N.2    McKinney, C.3    Chen, Y.H.4
  • 27
    • 33846070634 scopus 로고    scopus 로고
    • Efficient incorporation of tegument proteins pUL46, pUL49, and pUS3 into pseudorabies virus particles depends on the presence of pUL21
    • Michael, K., Klupp, B. G., Karger, A., Mettenleiter, T. C., Efficient incorporation of tegument proteins pUL46, pUL49, and pUS3 into pseudorabies virus particles depends on the presence of pUL21. J. Virol. 2007, 81, 1048-1051.
    • (2007) J. Virol. , vol.81 , pp. 1048-1051
    • Michael, K.1    Klupp, B.G.2    Karger, A.3    Mettenleiter, T.C.4
  • 28
    • 31144433860 scopus 로고    scopus 로고
    • Composition of pseudorabies virus particles lacking tegument protein US3, UL47, or UL49 or envelope glycoprotein E
    • Michael, K., Klupp, B. G., Mettenleiter, T. C., Karger, A., Composition of pseudorabies virus particles lacking tegument protein US3, UL47, or UL49 or envelope glycoprotein E. J. Virol. 2006, 80, 1332-1339.
    • (2006) J. Virol. , vol.80 , pp. 1332-1339
    • Michael, K.1    Klupp, B.G.2    Mettenleiter, T.C.3    Karger, A.4
  • 29
    • 84887091401 scopus 로고    scopus 로고
    • A proteomic perspective of inbuilt viral protein regulation: pUL46 tegument protein is targeted for degradation by ICP0 during herpes simplex virus type 1 infection
    • Lin, A. E., Greco, T. M., Dohner, K., Sodeik, B. et al., A proteomic perspective of inbuilt viral protein regulation: pUL46 tegument protein is targeted for degradation by ICP0 during herpes simplex virus type 1 infection. Mol. Cell Proteomics 2013, 12, 3237-3252.
    • (2013) Mol. Cell Proteomics , vol.12 , pp. 3237-3252
    • Lin, A.E.1    Greco, T.M.2    Dohner, K.3    Sodeik, B.4
  • 30
    • 0142092454 scopus 로고    scopus 로고
    • Binding Partners for the UL11 tegument protein of herpes simplex virus type 1
    • Loomis, J. S., Courtney, R. J., Wills, J. W., Binding Partners for the UL11 tegument protein of herpes simplex virus type 1. J. Virol. 2003, 77, 11417-11424.
    • (2003) J. Virol. , vol.77 , pp. 11417-11424
    • Loomis, J.S.1    Courtney, R.J.2    Wills, J.W.3
  • 31
    • 55349107247 scopus 로고    scopus 로고
    • The product of the Herpes simplex virus 1 UL7 gene interacts with a mitochondrial protein, adenine nucleotide translocator 2
    • Tanaka, M., Sata, T., Kawaguchi, Y., The product of the Herpes simplex virus 1 UL7 gene interacts with a mitochondrial protein, adenine nucleotide translocator 2. Virol. J. 2008, 5, 125.
    • (2008) Virol. J. , vol.5 , pp. 125
    • Tanaka, M.1    Sata, T.2    Kawaguchi, Y.3
  • 32
    • 0033997929 scopus 로고    scopus 로고
    • Bovine herpesvirus 1 UL3.5 interacts with bovine herpesvirus 1 alpha -transinducing factor
    • Lam, N., Letchworth, G. J., Bovine herpesvirus 1 UL3.5 interacts with bovine herpesvirus 1 alpha -transinducing factor. J. Virol. 2000, 74, 2876-2884.
    • (2000) J. Virol. , vol.74 , pp. 2876-2884
    • Lam, N.1    Letchworth, G.J.2
  • 33
    • 70849129899 scopus 로고    scopus 로고
    • Major tegument protein VP8 of bovine herpesvirus 1 is phosphorylated by viral US3 and cellular CK2 protein kinases
    • Labiuk, S. L., Babiuk, L. A., van Drunen Littel-van den Hurk, S., Major tegument protein VP8 of bovine herpesvirus 1 is phosphorylated by viral US3 and cellular CK2 protein kinases. J. Gen. Virol. 2009, 90, 2829-2839.
    • (2009) J. Gen. Virol. , vol.90 , pp. 2829-2839
    • Labiuk, S.L.1    Babiuk, L.A.2    van Drunen Littel-van den Hurk, S.3
  • 34
    • 84890862425 scopus 로고    scopus 로고
    • Varicella-zoster virus ORF49 functions in the efficient production of progeny virus through its interaction with essential tegument protein ORF44
    • Sadaoka, T., Serada, S., Kato, J., Hayashi, M. et al., Varicella-zoster virus ORF49 functions in the efficient production of progeny virus through its interaction with essential tegument protein ORF44. J. Virol. 2014, 88, 188-201.
    • (2014) J. Virol. , vol.88 , pp. 188-201
    • Sadaoka, T.1    Serada, S.2    Kato, J.3    Hayashi, M.4
  • 35
    • 77952878717 scopus 로고    scopus 로고
    • Gene expression profiling of Pseudorabies virus (PrV) infected bovine cells by combination of transcript analysis and quantitative proteomic techniques
    • Skiba, M., Glowinski, F., Koczan, D., Mettenleiter, T. C. et al., Gene expression profiling of Pseudorabies virus (PrV) infected bovine cells by combination of transcript analysis and quantitative proteomic techniques. Vet. Microbiol. 2010, 143, 14-20.
    • (2010) Vet. Microbiol. , vol.143 , pp. 14-20
    • Skiba, M.1    Glowinski, F.2    Koczan, D.3    Mettenleiter, T.C.4
  • 36
    • 84875090034 scopus 로고    scopus 로고
    • Role of Us9 phosphorylation in axonal sorting and anterograde transport of pseudorabies virus
    • Kratchmarov, R., Taylor, M. P., Enquist, L. W., Role of Us9 phosphorylation in axonal sorting and anterograde transport of pseudorabies virus. PLoS One 2013, 8, e58776.
    • (2013) PLoS One , vol.8 , pp. e58776
    • Kratchmarov, R.1    Taylor, M.P.2    Enquist, L.W.3
  • 37
    • 84873152434 scopus 로고    scopus 로고
    • An immunoreceptor tyrosine-based inhibition motif in varicella-zoster virus glycoprotein B regulates cell fusion and skin pathogenesis
    • Oliver, S. L., Brady, J. J., Sommer, M. H., Reichelt, M. et al., An immunoreceptor tyrosine-based inhibition motif in varicella-zoster virus glycoprotein B regulates cell fusion and skin pathogenesis. Proc. Natl. Acad. Sci. USA 2013, 110, 1911-1916.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 1911-1916
    • Oliver, S.L.1    Brady, J.J.2    Sommer, M.H.3    Reichelt, M.4
  • 38
    • 77951039948 scopus 로고    scopus 로고
    • Identification of phosphorylated residues on varicella-zoster virus immediate-early protein ORF63
    • Mueller, N. H., Walters, M. S., Marcus, R. A., Graf, L. L. et al., Identification of phosphorylated residues on varicella-zoster virus immediate-early protein ORF63. J. Gen. Virol. 2010, 91, 1133-1137.
    • (2010) J. Gen. Virol. , vol.91 , pp. 1133-1137
    • Mueller, N.H.1    Walters, M.S.2    Marcus, R.A.3    Graf, L.L.4
  • 39
    • 84860907534 scopus 로고    scopus 로고
    • Five questions about viral trafficking in neurons
    • Enquist, L. W., Five questions about viral trafficking in neurons. PLoS Pathog. 2012, 8, e1002472.
    • (2012) PLoS Pathog. , vol.8 , pp. e1002472
    • Enquist, L.W.1
  • 40
    • 84894470670 scopus 로고    scopus 로고
    • The neuroinvasive profiles of H129 (herpes simplex virus type 1) recombinants with putative anterograde-only transneuronal spread properties
    • Wojaczynski, G. J., Engel, E. A., Steren, K. E., Enquist, L. W. et al., The neuroinvasive profiles of H129 (herpes simplex virus type 1) recombinants with putative anterograde-only transneuronal spread properties. Brain Struct. Funct. 2015, 220, 1395-1420.
    • (2015) Brain Struct. Funct. , vol.220 , pp. 1395-1420
    • Wojaczynski, G.J.1    Engel, E.A.2    Steren, K.E.3    Enquist, L.W.4
  • 41
    • 24944433231 scopus 로고    scopus 로고
    • Molecular biology of pseudorabies virus: impact on neurovirology and veterinary medicine
    • Pomeranz, L. E., Reynolds, A. E., Hengartner, C. J., Molecular biology of pseudorabies virus: impact on neurovirology and veterinary medicine. Microbiol. Mol. Biol. Rev. 2005, 69, 462-500.
    • (2005) Microbiol. Mol. Biol. Rev. , vol.69 , pp. 462-500
    • Pomeranz, L.E.1    Reynolds, A.E.2    Hengartner, C.J.3
  • 42
    • 84872576880 scopus 로고    scopus 로고
    • Efficient retrograde transport of pseudorabies virus within neurons requires local protein synthesis in axons
    • Koyuncu, O. O., Perlman, D. H., Enquist, L. W., Efficient retrograde transport of pseudorabies virus within neurons requires local protein synthesis in axons. Cell Host Microbe 2013, 13, 54-66.
    • (2013) Cell Host Microbe , vol.13 , pp. 54-66
    • Koyuncu, O.O.1    Perlman, D.H.2    Enquist, L.W.3
  • 43
    • 0034608952 scopus 로고    scopus 로고
    • Retrograde axonal transport of herpes simplex virus: evidence for a single mechanism and a role for tegument
    • Bearer, E. L., Breakefield, X. O., Schuback, D., Reese, T. S. et al., Retrograde axonal transport of herpes simplex virus: evidence for a single mechanism and a role for tegument. Proc. Natl. Acad. Sci. USA 2000, 97, 8146-8150.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8146-8150
    • Bearer, E.L.1    Breakefield, X.O.2    Schuback, D.3    Reese, T.S.4
  • 44
    • 77957652501 scopus 로고    scopus 로고
    • Plus- and minus-end directed microtubule motors bind simultaneously to herpes simplex virus capsids using different inner tegument structures
    • Radtke, K., Kieneke, D., Wolfstein, A., Michael, K. et al., Plus- and minus-end directed microtubule motors bind simultaneously to herpes simplex virus capsids using different inner tegument structures. PLoS Pathog. 2010, 6, e1000991.
    • (2010) PLoS Pathog. , vol.6 , pp. e1000991
    • Radtke, K.1    Kieneke, D.2    Wolfstein, A.3    Michael, K.4
  • 45
    • 84871022299 scopus 로고    scopus 로고
    • Kinesin-3 mediates axonal sorting and directional transport of alphaherpesvirus particles in neurons
    • Kramer, T., Greco, T. M., Taylor, M. P., Ambrosini, A. E. et al., Kinesin-3 mediates axonal sorting and directional transport of alphaherpesvirus particles in neurons. Cell Host Microbe 2012, 12, 806-814.
    • (2012) Cell Host Microbe , vol.12 , pp. 806-814
    • Kramer, T.1    Greco, T.M.2    Taylor, M.P.3    Ambrosini, A.E.4
  • 46
    • 0033989063 scopus 로고    scopus 로고
    • Role of pseudorabies virus Us9, a type II membrane protein, in infection of tissue culture cells and the rat nervous system
    • Brideau, A. D., Card, J. P., Enquist, L. W., Role of pseudorabies virus Us9, a type II membrane protein, in infection of tissue culture cells and the rat nervous system. J. Virol. 2000, 74, 834-845.
    • (2000) J. Virol. , vol.74 , pp. 834-845
    • Brideau, A.D.1    Card, J.P.2    Enquist, L.W.3
  • 47
    • 34548653451 scopus 로고    scopus 로고
    • Envelope protein Us9 is required for the anterograde transport of bovine herpesvirus type 1 from trigeminal ganglia to nose and eye upon reactivation
    • Butchi, N. B., Jones, C., Perez, S., Doster, A. et al., Envelope protein Us9 is required for the anterograde transport of bovine herpesvirus type 1 from trigeminal ganglia to nose and eye upon reactivation. J. Neurovirol. 2007, 13, 384-388.
    • (2007) J. Neurovirol. , vol.13 , pp. 384-388
    • Butchi, N.B.1    Jones, C.2    Perez, S.3    Doster, A.4
  • 48
    • 84883269126 scopus 로고    scopus 로고
    • Glycoproteins gE and gI are required for efficient KIF1A-dependent anterograde axonal transport of alphaherpesvirus particles in neurons
    • Kratchmarov, R., Kramer, T., Greco, T. M., Taylor, M. P. et al., Glycoproteins gE and gI are required for efficient KIF1A-dependent anterograde axonal transport of alphaherpesvirus particles in neurons. J. Virol. 2013, 87, 9431-9440.
    • (2013) J. Virol. , vol.87 , pp. 9431-9440
    • Kratchmarov, R.1    Kramer, T.2    Greco, T.M.3    Taylor, M.P.4
  • 49
    • 84871997521 scopus 로고    scopus 로고
    • Herpes simplex virus membrane proteins gE/gI and US9 act cooperatively to promote transport of capsids and glycoproteins from neuron cell bodies into initial axon segments
    • Howard, P. W., Howard, T. L., Johnson, D. C., Herpes simplex virus membrane proteins gE/gI and US9 act cooperatively to promote transport of capsids and glycoproteins from neuron cell bodies into initial axon segments. J. Virol. 2013, 87, 403-414.
    • (2013) J. Virol. , vol.87 , pp. 403-414
    • Howard, P.W.1    Howard, T.L.2    Johnson, D.C.3
  • 50
    • 69249219334 scopus 로고    scopus 로고
    • Anterograde spread of herpes simplex virus type 1 requires glycoprotein E and glycoprotein I but not Us9
    • McGraw, H. M., Awasthi, S., Wojcechowskyj, J. A., Friedman, H. M., Anterograde spread of herpes simplex virus type 1 requires glycoprotein E and glycoprotein I but not Us9. J. Virol. 2009, 83, 8315-8326.
    • (2009) J. Virol. , vol.83 , pp. 8315-8326
    • McGraw, H.M.1    Awasthi, S.2    Wojcechowskyj, J.A.3    Friedman, H.M.4
  • 51
    • 0033913386 scopus 로고    scopus 로고
    • Characterization by two-dimensional gel electrophoresis of host proteins whose synthesis is sustained or stimulated during the course of herpes simplex virus type 1 infection
    • Greco, A., Bausch, N., Coute, Y., Diaz, J. J., Characterization by two-dimensional gel electrophoresis of host proteins whose synthesis is sustained or stimulated during the course of herpes simplex virus type 1 infection. Electrophoresis 2000, 21, 2522-2530.
    • (2000) Electrophoresis , vol.21 , pp. 2522-2530
    • Greco, A.1    Bausch, N.2    Coute, Y.3    Diaz, J.J.4
  • 52
    • 68549125523 scopus 로고    scopus 로고
    • Proteomic analysis of cells in the early stages of herpes simplex virus type-1 infection reveals widespread changes in the host cell proteome
    • Antrobus, R., Grant, K., Gangadharan, B., Chittenden, D. et al., Proteomic analysis of cells in the early stages of herpes simplex virus type-1 infection reveals widespread changes in the host cell proteome. Proteomics 2009, 9, 3913-3927.
    • (2009) Proteomics , vol.9 , pp. 3913-3927
    • Antrobus, R.1    Grant, K.2    Gangadharan, B.3    Chittenden, D.4
  • 53
    • 52649090784 scopus 로고    scopus 로고
    • Quantitative whole-cell proteome analysis of pseudorabies virus-infected cells
    • Skiba, M., Mettenleiter, T. C., Karger, A., Quantitative whole-cell proteome analysis of pseudorabies virus-infected cells. J. Virol. 2008, 82, 9689-9699.
    • (2008) J. Virol. , vol.82 , pp. 9689-9699
    • Skiba, M.1    Mettenleiter, T.C.2    Karger, A.3
  • 54
    • 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
  • 55
    • 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
  • 56
    • 49149090155 scopus 로고    scopus 로고
    • Effects of lamin A/C, lamin B1, and viral US3 kinase activity on viral infectivity, virion egress, and the targeting of herpes simplex virus U(L)34-encoded protein to the inner nuclear membrane
    • Mou, F., Wills, E. G., Park, R., Baines, J. D., Effects of lamin A/C, lamin B1, and viral US3 kinase activity on viral infectivity, virion egress, and the targeting of herpes simplex virus U(L)34-encoded protein to the inner nuclear membrane. J. Virol. 2008, 82, 8094-8104.
    • (2008) J. Virol. , vol.82 , pp. 8094-8104
    • Mou, F.1    Wills, E.G.2    Park, R.3    Baines, J.D.4
  • 57
    • 69249222501 scopus 로고    scopus 로고
    • Herpes simplex virus 2 UL13 protein kinase disrupts nuclear lamins
    • Cano-Monreal, G. L., Wylie, K. M., Cao, F., Tavis, J. E. et al., Herpes simplex virus 2 UL13 protein kinase disrupts nuclear lamins. Virology 2009, 392, 137-147.
    • (2009) Virology , vol.392 , pp. 137-147
    • Cano-Monreal, G.L.1    Wylie, K.M.2    Cao, F.3    Tavis, J.E.4
  • 58
    • 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
  • 59
    • 44949265263 scopus 로고    scopus 로고
    • Role for A-type lamins in herpesviral DNA targeting and heterochromatin modulation
    • Silva, L., Cliffe, A., Chang, L., Knipe, D. M., Role for A-type lamins in herpesviral DNA targeting and heterochromatin modulation. PLoS Pathog. 2008, 4, e1000071.
    • (2008) PLoS Pathog. , vol.4 , pp. e1000071
    • Silva, L.1    Cliffe, A.2    Chang, L.3    Knipe, D.M.4
  • 60
    • 0034467101 scopus 로고    scopus 로고
    • Interaction between herpes simplex virus type 1 IE63 protein and cellular protein p32
    • Bryant, H. E., Matthews, D. A., Wadd, S., Scott, J. E. et al., Interaction between herpes simplex virus type 1 IE63 protein and cellular protein p32. J. Virol. 2000, 74, 11322-11328.
    • (2000) J. Virol. , vol.74 , pp. 11322-11328
    • Bryant, H.E.1    Matthews, D.A.2    Wadd, S.3    Scott, J.E.4
  • 61
    • 0037378607 scopus 로고    scopus 로고
    • CK2 protein kinase is stimulated and redistributed by functional herpes simplex virus ICP27 protein
    • Koffa, M. D., Kean, J., Zachos, G., Rice, S. A. et al., CK2 protein kinase is stimulated and redistributed by functional herpes simplex virus ICP27 protein. J. Virol. 2003, 77, 4315-4325.
    • (2003) J. Virol. , vol.77 , pp. 4315-4325
    • Koffa, M.D.1    Kean, J.2    Zachos, G.3    Rice, S.A.4
  • 62
    • 0032878244 scopus 로고    scopus 로고
    • The multifunctional herpes simplex virus IE63 protein interacts with heterogeneous ribonucleoprotein K and with casein kinase 2
    • Wadd, S., Bryant, H., Filhol, O., Scott, J. E. et al., The multifunctional herpes simplex virus IE63 protein interacts with heterogeneous ribonucleoprotein K and with casein kinase 2. J. Biol. Chem. 1999, 274, 28991-28998.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28991-28998
    • Wadd, S.1    Bryant, H.2    Filhol, O.3    Scott, J.E.4
  • 63
    • 77957818530 scopus 로고    scopus 로고
    • The heterogeneous nuclear ribonucleoprotein K is important for Herpes simplex virus-1 propagation
    • Schmidt, T., Striebinger, H., Haas, J., Bailer, S. M., The heterogeneous nuclear ribonucleoprotein K is important for Herpes simplex virus-1 propagation. FEBS Lett. 2010, 584, 4361-4365.
    • (2010) FEBS Lett. , vol.584 , pp. 4361-4365
    • Schmidt, T.1    Striebinger, H.2    Haas, J.3    Bailer, S.M.4
  • 64
    • 66149091612 scopus 로고    scopus 로고
    • Identification of replication-competent HSV-1 Cgal+ strain signaling targets in human hepatoma cells by functional organelle proteomics
    • Santamaria, E., Mora, M. I., Potel, C., Fernandez-Irigoyen, J. et al., Identification of replication-competent HSV-1 Cgal+ strain signaling targets in human hepatoma cells by functional organelle proteomics. Mol. Cell Proteomics 2009, 8, 805-815.
    • (2009) Mol. Cell Proteomics , vol.8 , pp. 805-815
    • Santamaria, E.1    Mora, M.I.2    Potel, C.3    Fernandez-Irigoyen, J.4
  • 65
    • 79957980688 scopus 로고    scopus 로고
    • HSV-1 Cgal+ infection promotes quaking RNA binding protein production and induces nuclear-cytoplasmic shuttling of quaking I-5 isoform in human hepatoma cells
    • M111 009126
    • Sanchez-Quiles, V., Mora, M. I., Segura, V., Greco, A. et al., HSV-1 Cgal+ infection promotes quaking RNA binding protein production and induces nuclear-cytoplasmic shuttling of quaking I-5 isoform in human hepatoma cells. Mol. Cell Proteomics 2011, 10, M111 009126.
    • (2011) Mol. Cell Proteomics , vol.10
    • Sanchez-Quiles, V.1    Mora, M.I.2    Segura, V.3    Greco, A.4
  • 66
    • 36349007701 scopus 로고    scopus 로고
    • Overexpression and role of the ATPase and putative DNA helicase RuvB-like 2 in human hepatocellular carcinoma
    • Rousseau, B., Menard, L., Haurie, V., Taras, D. et al., Overexpression and role of the ATPase and putative DNA helicase RuvB-like 2 in human hepatocellular carcinoma. Hepatology 2007, 46, 1108-1118.
    • (2007) Hepatology , vol.46 , pp. 1108-1118
    • Rousseau, B.1    Menard, L.2    Haurie, V.3    Taras, D.4
  • 67
    • 84910144160 scopus 로고    scopus 로고
    • Identification of putative biomarkers for HIV-associated neurocognitive impairment in the CSF of HIV-infected patients under cART therapy determined by mass spectrometry
    • Bora, A., Mohien, C. U., Chaerkady, R., Chang, L. et al., Identification of putative biomarkers for HIV-associated neurocognitive impairment in the CSF of HIV-infected patients under cART therapy determined by mass spectrometry. J. Neurovirol. 2014, 20, 457-465.
    • (2014) J. Neurovirol. , vol.20 , pp. 457-465
    • Bora, A.1    Mohien, C.U.2    Chaerkady, R.3    Chang, L.4
  • 68
    • 67449100986 scopus 로고    scopus 로고
    • RuvB-like protein 2 is a suppressor of influenza A virus polymerases
    • Kakugawa, S., Shimojima, M., Neumann, G., Goto, H. et al., RuvB-like protein 2 is a suppressor of influenza A virus polymerases. J. Virol. 2009, 83, 6429-6434.
    • (2009) J. Virol. , vol.83 , pp. 6429-6434
    • Kakugawa, S.1    Shimojima, M.2    Neumann, G.3    Goto, H.4
  • 69
    • 0035321969 scopus 로고    scopus 로고
    • Identification of ribosome-associated viral and cellular basic proteins during the course of infection with herpes simplex virus type 1
    • Greco, A., Bienvenut, W., Sanchez, J. C., Kindbeiter, K. et al., Identification of ribosome-associated viral and cellular basic proteins during the course of infection with herpes simplex virus type 1. Proteomics 2001, 1, 545-549.
    • (2001) Proteomics , vol.1 , pp. 545-549
    • Greco, A.1    Bienvenut, W.2    Sanchez, J.C.3    Kindbeiter, K.4
  • 71
    • 84859954603 scopus 로고    scopus 로고
    • Axonal mRNA localization and local protein synthesis in nervous system assembly, maintenance and repair
    • Jung, H., Yoon, B. C., Holt, C. E., Axonal mRNA localization and local protein synthesis in nervous system assembly, maintenance and repair. Nat. Rev. Neurosci. 2012, 13, 308-324.
    • (2012) Nat. Rev. Neurosci. , vol.13 , pp. 308-324
    • Jung, H.1    Yoon, B.C.2    Holt, C.E.3
  • 72
    • 84858799332 scopus 로고    scopus 로고
    • Axonal transcription factors signal retrogradely in lesioned peripheral nerve
    • Ben-Yaakov, K., Dagan, S. Y., Segal-Ruder, Y., Shalem, O. et al., Axonal transcription factors signal retrogradely in lesioned peripheral nerve. EMBO J. 2012, 31, 1350-1363.
    • (2012) EMBO J. , vol.31 , pp. 1350-1363
    • Ben-Yaakov, K.1    Dagan, S.Y.2    Segal-Ruder, Y.3    Shalem, O.4
  • 73
    • 38849124121 scopus 로고    scopus 로고
    • Intra-axonal translation and retrograde trafficking of CREB promotes neuronal survival
    • Cox, L. J., Hengst, U., Gurskaya, N. G., Lukyanov, K. A. et al., Intra-axonal translation and retrograde trafficking of CREB promotes neuronal survival. Nat. Cell Biol. 2008, 10, 149-159.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 149-159
    • Cox, L.J.1    Hengst, U.2    Gurskaya, N.G.3    Lukyanov, K.A.4
  • 74
    • 9144273965 scopus 로고    scopus 로고
    • Axoplasmic importins enable retrograde injury signaling in lesioned nerve
    • Hanz, S., Perlson, E., Willis, D., Zheng, J. Q. et al., Axoplasmic importins enable retrograde injury signaling in lesioned nerve. Neuron 2003, 40, 1095-1104.
    • (2003) Neuron , vol.40 , pp. 1095-1104
    • Hanz, S.1    Perlson, E.2    Willis, D.3    Zheng, J.Q.4
  • 75
    • 46549085203 scopus 로고    scopus 로고
    • Function and regulation of local axonal translation
    • Lin, A. C., Holt, C. E., Function and regulation of local axonal translation. Curr. Opin. Neurobiol. 2008, 18, 60-68.
    • (2008) Curr. Opin. Neurobiol. , vol.18 , pp. 60-68
    • Lin, A.C.1    Holt, C.E.2
  • 76
    • 84887013185 scopus 로고    scopus 로고
    • The central dogma decentralized: new perspectives on RNA function and local translation in neurons
    • Holt, C., Schuman, E., The central dogma decentralized: new perspectives on RNA function and local translation in neurons. Neuron 2013, 80, 648-657.
    • (2013) Neuron , vol.80 , pp. 648-657
    • Holt, C.1    Schuman, E.2
  • 78
    • 77958140656 scopus 로고    scopus 로고
    • IFI16 is an innate immune sensor for intracellular DNA
    • Unterholzner, L., Keating, S. E., Baran, M., Horan, K. A. et al., IFI16 is an innate immune sensor for intracellular DNA. Nat. Immunol. 2010, 11, 997-1004.
    • (2010) Nat. Immunol. , vol.11 , pp. 997-1004
    • Unterholzner, L.1    Keating, S.E.2    Baran, M.3    Horan, K.A.4
  • 79
    • 84862976171 scopus 로고    scopus 로고
    • Acetylation modulates cellular distribution and DNA sensing ability of interferon-inducible protein IFI16
    • Li, T., Diner, B. A., Chen, J., Cristea, I. M., Acetylation modulates cellular distribution and DNA sensing ability of interferon-inducible protein IFI16. Proc. Natl. Acad. Sci. USA 2012, 109, 10558-10563.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 10558-10563
    • Li, T.1    Diner, B.A.2    Chen, J.3    Cristea, I.M.4
  • 81
    • 0035210423 scopus 로고    scopus 로고
    • Gene expression analyzed by microarrays in HSV-1 latent mouse trigeminal ganglion following heat stress
    • Hill, J.M., Lukiw, W. J., Gebhardt, B. M., Higaki, S. et al., Gene expression analyzed by microarrays in HSV-1 latent mouse trigeminal ganglion following heat stress. Virus Genes 2001, 23, 273-280.
    • (2001) Virus Genes , vol.23 , pp. 273-280
    • Hill, J.M.1    Lukiw, W.J.2    Gebhardt, B.M.3    Higaki, S.4
  • 82
    • 33847095829 scopus 로고    scopus 로고
    • Proteome analysis of human macrophages reveals the upregulation of manganese-containing superoxide dismutase after toll-like receptor activation
    • Rakkola, R., Matikainen, S., Nyman, T. A., Proteome analysis of human macrophages reveals the upregulation of manganese-containing superoxide dismutase after toll-like receptor activation. Proteomics 2007, 7, 378-384.
    • (2007) Proteomics , vol.7 , pp. 378-384
    • Rakkola, R.1    Matikainen, S.2    Nyman, T.A.3
  • 83
    • 15844375853 scopus 로고    scopus 로고
    • Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death
    • Baines, C. P., Kaiser, R. A., Purcell, N. H., Blair, N. S. et al., Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death. Nature 2005, 434, 658-662.
    • (2005) Nature , vol.434 , pp. 658-662
    • Baines, C.P.1    Kaiser, R.A.2    Purcell, N.H.3    Blair, N.S.4
  • 84
    • 53549129483 scopus 로고    scopus 로고
    • Cyclophilin D deficiency attenuates mitochondrial and neuronal perturbation and ameliorates learning and memory in Alzheimer's disease
    • Du, H., Guo, L., Fang, F., Chen, D. et al., Cyclophilin D deficiency attenuates mitochondrial and neuronal perturbation and ameliorates learning and memory in Alzheimer's disease. Nat. Med. 2008, 14, 1097-1105.
    • (2008) Nat. Med. , vol.14 , pp. 1097-1105
    • Du, H.1    Guo, L.2    Fang, F.3    Chen, D.4
  • 85
    • 67649785237 scopus 로고    scopus 로고
    • Role of cyclophilin D-dependent mitochondrial permeability transition in glutamate-induced calcium deregulation and excitotoxic neuronal death
    • Li, V., Brustovetsky, T., Brustovetsky, N., Role of cyclophilin D-dependent mitochondrial permeability transition in glutamate-induced calcium deregulation and excitotoxic neuronal death. Exp. Neurol. 2009, 218, 171-182.
    • (2009) Exp. Neurol. , vol.218 , pp. 171-182
    • Li, V.1    Brustovetsky, T.2    Brustovetsky, N.3
  • 86
    • 84875736640 scopus 로고    scopus 로고
    • The proteome of Toll-like receptor 3-stimulated human immortalized fibroblasts: implications for susceptibility to herpes simplex virus encephalitis
    • Perez de Diego, R., Mulvey, C., Crawford, M., Trotter, M. W. et al., The proteome of Toll-like receptor 3-stimulated human immortalized fibroblasts: implications for susceptibility to herpes simplex virus encephalitis. J. Allergy Clin. Immunol. 2013, 131, 1157-1166.
    • (2013) J. Allergy Clin. Immunol. , vol.131 , pp. 1157-1166
    • Perez de Diego, R.1    Mulvey, C.2    Crawford, M.3    Trotter, M.W.4
  • 87
    • 84869232621 scopus 로고    scopus 로고
    • Global secretome characterization of herpes simplex virus 1-infected human primary macrophages
    • Miettinen, J. J., Matikainen, S., Nyman, T. A., Global secretome characterization of herpes simplex virus 1-infected human primary macrophages. J. Virol. 2012, 86, 12770-12778.
    • (2012) J. Virol. , vol.86 , pp. 12770-12778
    • Miettinen, J.J.1    Matikainen, S.2    Nyman, T.A.3
  • 88
    • 34247553696 scopus 로고    scopus 로고
    • Investigating the human immunodeficiency virus type 1-infected monocyte-derived macrophage secretome
    • Ciborowski, P., Kadiu, I., Rozek, W., Smith, L. et al., Investigating the human immunodeficiency virus type 1-infected monocyte-derived macrophage secretome. Virology 2007, 363, 198-209.
    • (2007) Virology , vol.363 , pp. 198-209
    • Ciborowski, P.1    Kadiu, I.2    Rozek, W.3    Smith, L.4
  • 89
    • 79958048266 scopus 로고    scopus 로고
    • Quantitative subcellular proteome and secretome profiling of influenza A virus-infected human primary macrophages
    • Lietzen, N., Ohman, T., Rintahaka, J., Julkunen, I. et al., Quantitative subcellular proteome and secretome profiling of influenza A virus-infected human primary macrophages. PLoS Pathog. 2011, 7, e1001340.
    • (2011) PLoS Pathog. , vol.7 , pp. e1001340
    • Lietzen, N.1    Ohman, T.2    Rintahaka, J.3    Julkunen, I.4
  • 90
    • 77954904912 scopus 로고    scopus 로고
    • Innate and adaptive immune responses to herpes simplex virus
    • Chew, T., Taylor, K. E., Mossman, K. L., Innate and adaptive immune responses to herpes simplex virus. Viruses 2009, 1, 979-1002.
    • (2009) Viruses , vol.1 , pp. 979-1002
    • Chew, T.1    Taylor, K.E.2    Mossman, K.L.3
  • 91
    • 84872000832 scopus 로고    scopus 로고
    • Human anti-varicella-zoster virus (VZV) recombinant monoclonal antibody produced after Zostavax immunization recognizes the gH/gL complex and neutralizes VZV infection
    • Birlea, M., Owens, G. P., Eshleman, E. M., Ritchie, A. et al., Human anti-varicella-zoster virus (VZV) recombinant monoclonal antibody produced after Zostavax immunization recognizes the gH/gL complex and neutralizes VZV infection. J. Virol. 2013, 87, 415-421.
    • (2013) J. Virol. , vol.87 , pp. 415-421
    • Birlea, M.1    Owens, G.P.2    Eshleman, E.M.3    Ritchie, A.4
  • 92
    • 84864540907 scopus 로고    scopus 로고
    • Enhanced bovine herpesvirus type 1 neutralization by multimerized single-chain variable antibody fragments regardless of differential glycosylation
    • Pasman, Y., Nagy, E., Kaushik, A. K., Enhanced bovine herpesvirus type 1 neutralization by multimerized single-chain variable antibody fragments regardless of differential glycosylation. Clin. Vaccine Immunol. 2012, 19, 1150-1157.
    • (2012) Clin. Vaccine Immunol. , vol.19 , pp. 1150-1157
    • Pasman, Y.1    Nagy, E.2    Kaushik, A.K.3
  • 93
    • 84862131829 scopus 로고    scopus 로고
    • Varicella-zoster virus glycoproteins B and E are major targets of CD4+ and CD8+ T cells reconstituting during zoster after allogeneic transplantation
    • Kleemann, P., Distler, E., Wagner, E. M., Thomas, S. et al., Varicella-zoster virus glycoproteins B and E are major targets of CD4+ and CD8+ T cells reconstituting during zoster after allogeneic transplantation. Haematologica 2012, 97, 874-882.
    • (2012) Haematologica , vol.97 , pp. 874-882
    • Kleemann, P.1    Distler, E.2    Wagner, E.M.3    Thomas, S.4
  • 94
    • 84884138622 scopus 로고    scopus 로고
    • Single-cell mass cytometry for analysis of immune system functional states
    • Bjornson, Z. B., Nolan, G. P., Fantl, W. J., Single-cell mass cytometry for analysis of immune system functional states. Curr. Opin. Immunol. 2013, 25, 484-494.
    • (2013) Curr. Opin. Immunol. , vol.25 , pp. 484-494
    • Bjornson, Z.B.1    Nolan, G.P.2    Fantl, W.J.3
  • 95
    • 84904789189 scopus 로고    scopus 로고
    • Single-cell mass cytometry analysis of human tonsil T cell remodeling by varicella zoster virus
    • Sen, N., Mukherjee, G., Sen, A., Bendall, S. C. et al., Single-cell mass cytometry analysis of human tonsil T cell remodeling by varicella zoster virus. Cell Rep. 2014, 8, 633-645.
    • (2014) Cell Rep. , vol.8 , pp. 633-645
    • Sen, N.1    Mukherjee, G.2    Sen, A.3    Bendall, S.C.4
  • 96
    • 59949085582 scopus 로고    scopus 로고
    • Spectroscopic detection and identification of infected cells with herpes viruses
    • Erukhimovitch, V., Karpasasa, M., Huleihel, M., Spectroscopic detection and identification of infected cells with herpes viruses. Biopolymers 2009, 91, 61-67.
    • (2009) Biopolymers , vol.91 , pp. 61-67
    • Erukhimovitch, V.1    Karpasasa, M.2    Huleihel, M.3
  • 97
    • 84891426819 scopus 로고    scopus 로고
    • Virological diagnosis of central nervous system infections by use of PCR coupled with mass spectrometry analysis of cerebrospinal fluid samples
    • Leveque, N., Legoff, J., Mengelle, C., Mercier-Delarue, S. et al., Virological diagnosis of central nervous system infections by use of PCR coupled with mass spectrometry analysis of cerebrospinal fluid samples. J. Clin. Microbiol. 2014, 52, 212-217.
    • (2014) J. Clin. Microbiol. , vol.52 , pp. 212-217
    • Leveque, N.1    Legoff, J.2    Mengelle, C.3    Mercier-Delarue, S.4
  • 98
    • 84908083526 scopus 로고    scopus 로고
    • Non-cytotoxic Thymus capitata extracts prevent Bovine herpesvirus-1 infection in cell cultures
    • Boubaker Elandalousi, R., Mekni Toujani, M., Kaabi, B., Larbi, I. et al., Non-cytotoxic Thymus capitata extracts prevent Bovine herpesvirus-1 infection in cell cultures. BMC Vet. Res. 2014, 10, 231.
    • (2014) BMC Vet. Res. , vol.10 , pp. 231
    • Boubaker Elandalousi, R.1    Mekni Toujani, M.2    Kaabi, B.3    Larbi, I.4
  • 99
    • 79960958455 scopus 로고    scopus 로고
    • Divergent effects of human cytomegalovirus and herpes simplex virus-1 on cellular metabolism
    • Vastag, L., Koyuncu, E., Grady, S. L., Shenk, T. E. et al., Divergent effects of human cytomegalovirus and herpes simplex virus-1 on cellular metabolism. PLoS Pathog. 2011, 7, e1002124.
    • (2011) PLoS Pathog. , vol.7 , pp. e1002124
    • Vastag, L.1    Koyuncu, E.2    Grady, S.L.3    Shenk, T.E.4
  • 100
    • 0037031877 scopus 로고    scopus 로고
    • Characterization of a heparan sulfate octasaccharide that binds to herpes simplex virus type 1 glycoprotein D
    • Liu, J., Shriver, Z., Pope, R. M., Thorp, S. C. et al., Characterization of a heparan sulfate octasaccharide that binds to herpes simplex virus type 1 glycoprotein D. J. Biol. Chem. 2002, 277, 33456-33467.
    • (2002) J. Biol. Chem. , vol.277 , pp. 33456-33467
    • Liu, J.1    Shriver, Z.2    Pope, R.M.3    Thorp, S.C.4
  • 102
    • 73249116388 scopus 로고    scopus 로고
    • LuMPIS-a modified luminescence-based mammalian interactome mapping pull-down assay for the investigation of protein-protein interactions encoded by GC-low ORFs
    • Vizoso Pinto, M. G., Villegas, J. M., Peter, J., Haase, R. et al., LuMPIS-a modified luminescence-based mammalian interactome mapping pull-down assay for the investigation of protein-protein interactions encoded by GC-low ORFs. Proteomics 2009, 9, 5303-5308.
    • (2009) Proteomics , vol.9 , pp. 5303-5308
    • Vizoso Pinto, M.G.1    Villegas, J.M.2    Peter, J.3    Haase, R.4
  • 103
    • 41249086507 scopus 로고    scopus 로고
    • A review of the biology of bovine herpesvirus type 1 (BHV-1), its role as a cofactor in the bovine respiratory disease complex and development of improved vaccines
    • Jones, C., Chowdhury, S., A review of the biology of bovine herpesvirus type 1 (BHV-1), its role as a cofactor in the bovine respiratory disease complex and development of improved vaccines. Anim. Health Res. Rev. 2007, 8, 187-205.
    • (2007) Anim. Health Res. Rev. , vol.8 , pp. 187-205
    • Jones, C.1    Chowdhury, S.2
  • 104
    • 84940215060 scopus 로고    scopus 로고
    • Transneuronal circuit analysis with pseudorabies viruses
    • Card, J. P., Enquist, L. W., Transneuronal circuit analysis with pseudorabies viruses. Curr. Protoc. Neurosci. 2014, 68, 1.5.1-1.5.39.
    • (2014) Curr. Protoc. Neurosci. , vol.68 , pp. 151-1539
    • Card, J.P.1    Enquist, L.W.2
  • 105
    • 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
  • 106
    • 84891760953 scopus 로고    scopus 로고
    • Biosafety of gene therapy vectors derived from herpes simplex virus type 1
    • Lim, F., Khalique, H., Ventosa, M., Baldo, A., Biosafety of gene therapy vectors derived from herpes simplex virus type 1. Curr. Gene Ther. 2013, 13, 478-491.
    • (2013) Curr. Gene Ther. , vol.13 , pp. 478-491
    • Lim, F.1    Khalique, H.2    Ventosa, M.3    Baldo, A.4
  • 107
    • 84928788632 scopus 로고    scopus 로고
    • The number of alphaherpesvirus particles infecting axons and the axonal protein repertoire determines the outcome of neuronal nfection.
    • Koyuncu, O. O., Song, R., Greco, T. M., Cristea, I. M. et al. The number of alphaherpesvirus particles infecting axons and the axonal protein repertoire determines the outcome of neuronal nfection. 2015, 6, e00276-15.
    • (2015) , vol.6 , pp. e00215-e00276
    • Koyuncu, O.O.1    Song, R.2    Greco, T.M.3    Cristea, I.M.4


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