메뉴 건너뛰기




Volumn 15, Issue 9, 2016, Pages 2939-2953

HVint: A strategy for identifying novel protein-protein interactions in herpes simplex virus type 1

Author keywords

[No Author keywords available]

Indexed keywords

VIRAL PROTEIN;

EID: 84989182904     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M116.058552     Document Type: Article
Times cited : (16)

References (134)
  • 1
    • 84931004252 scopus 로고    scopus 로고
    • Investigating the biology of alpha herpesviruses with MS-based proteomics
    • Engel, E. A., Song, R., Koyuncu, O. O., and Enquist, L. W. (2015) Investigating the biology of alpha herpesviruses with MS-based proteomics. Proteomics 15, 1943-1956
    • (2015) Proteomics , vol.15 , pp. 1943-1956
    • Engel, E.A.1    Song, R.2    Koyuncu, O.O.3    Enquist, L.W.4
  • 2
    • 0344304755 scopus 로고    scopus 로고
    • Treatment of herpes simplex virus infections
    • Brady, R. C., and Bernstein, D. I. (2004) Treatment of herpes simplex virus infections. Antiviral Res. 61, 73-81
    • (2004) Antiviral Res. , vol.61 , pp. 73-81
    • Brady, R.C.1    Bernstein, D.I.2
  • 3
    • 84872800289 scopus 로고    scopus 로고
    • Mucosal herpes immunity and immunopathology to ocular and genital herpes simplex virus infections
    • Chentoufi, A. A., and Benmohamed, L. (2012) Mucosal herpes immunity and immunopathology to ocular and genital herpes simplex virus infections. Clin. Dev. Immunol. 2012, 149135
    • (2012) Clin. Dev. Immunol. , vol.2012 , pp. 149135
    • Chentoufi, A.A.1    Benmohamed, L.2
  • 4
    • 84931569620 scopus 로고    scopus 로고
    • Reactivated herpes simplex infection increases the risk of Alzheimer's disease
    • Lövheim, H., Gilthorpe, J., Adolfsson, R., Nilsson, L. G., and Elgh, F. (2014) Reactivated herpes simplex infection increases the risk of Alzheimer's disease. Alzheimers Dement. 11, 593-599
    • (2014) Alzheimers Dement , vol.11 , pp. 593-599
    • Lövheim, H.1    Gilthorpe, J.2    Adolfsson, R.3    Nilsson, L.G.4    Elgh, F.5
  • 5
    • 84900532147 scopus 로고    scopus 로고
    • Herpes simplex virus type-2 stimulates HIV-1 replication in cervical tissues: Implications for HIV-1 transmission and efficacy of anti-HIV-1 microbicides
    • Rollenhagen, C., Lathrop, M. J., Macura, S. L., Doncel, G. F., and Asin, S. N. (2014) Herpes simplex virus type-2 stimulates HIV-1 replication in cervical tissues: implications for HIV-1 transmission and efficacy of anti-HIV-1 microbicides. Mucosal Immunol. 7, 1165-1174
    • (2014) Mucosal Immunol , vol.7 , pp. 1165-1174
    • Rollenhagen, C.1    Lathrop, M.J.2    Macura, S.L.3    Doncel, G.F.4    Asin, S.N.5
  • 6
    • 84946397770 scopus 로고    scopus 로고
    • Towards integrative structural mass spectrometry: Benefits from hybrid approaches
    • Marcoux, J., and Cianférani, S. (2015) Towards integrative structural mass spectrometry: Benefits from hybrid approaches. Methods 89, 4-12
    • (2015) Methods , vol.89 , pp. 4-12
    • Marcoux, J.1    Cianférani, S.2
  • 9
    • 84861310336 scopus 로고    scopus 로고
    • From protein interaction networks to novel therapeutic strategies
    • Jaeger, S., and Aloy, P. (2012) From protein interaction networks to novel therapeutic strategies. IUBMB Life 64, 529-537
    • (2012) IUBMB Life , vol.64 , pp. 529-537
    • Jaeger, S.1    Aloy, P.2
  • 11
    • 84927516180 scopus 로고    scopus 로고
    • Computational approaches for prediction of pathogen-host protein-protein interactions
    • Nourani, E., Khunjush, F., and Durmu?, S. (2015) Computational approaches for prediction of pathogen-host protein-protein interactions. Front. Microbiol. 6, 94
    • (2015) Front. Microbiol. , vol.6 , pp. 94
    • Nourani, E.1    Khunjush, F.2    Durmuş, S.3
  • 12
    • 84866452395 scopus 로고    scopus 로고
    • Techniques to cope with missing data in host-pathogen protein interaction prediction
    • Kshirsagar, M., Carbonell, J., and Klein-Seetharaman, J. (2012) Techniques to cope with missing data in host-pathogen protein interaction prediction. Bioinformatics 28, i466-i472
    • (2012) Bioinformatics , vol.28 , pp. i466-i472
    • Kshirsagar, M.1    Carbonell, J.2    Klein-Seetharaman, J.3
  • 13
    • 84871820346 scopus 로고    scopus 로고
    • Systems biology of pathogenhost interaction: Networks of protein-protein interaction within pathogens and pathogen-human interactions in the post-genomic era
    • Durmuş Tekir, S. D., and Ülgen, K. Ö. (2013) Systems biology of pathogenhost interaction: Networks of protein-protein interaction within pathogens and pathogen-human interactions in the post-genomic era. Biotechnol. J. 8, 85-96
    • (2013) Biotechnol. J. , vol.8 , pp. 85-96
    • Durmuş Tekir, S.D.1    Ülgen, K.O.2
  • 14
    • 85017004540 scopus 로고    scopus 로고
    • The impact of mass spectrometry-based proteomics on fundamental discoveries in virology
    • Greco, T. M., Diner, B. A., and Cristea, I. M. (2014) The Impact of Mass Spectrometry-Based Proteomics on Fundamental Discoveries in Virology. Annu. Rev. Virol. 1, 581-604
    • (2014) Annu. Rev. Virol. , vol.1 , pp. 581-604
    • Greco, T.M.1    Diner, B.A.2    Cristea, I.M.3
  • 16
    • 79956351653 scopus 로고    scopus 로고
    • Unraveling the dynamics of protein interactions with quantitative mass spectrometry
    • Ramisetty, S. R., and Washburn, M. P. (2011) Unraveling the dynamics of protein interactions with quantitative mass spectrometry. Crit. Rev. Biochem. Mol. Biol. 46, 216-228
    • (2011) Crit. Rev. Biochem. Mol. Biol. , vol.46 , pp. 216-228
    • Ramisetty, S.R.1    Washburn, M.P.2
  • 18
    • 0033954256 scopus 로고    scopus 로고
    • The Protein Data Bank
    • Berman, H. M. (2000) The Protein Data Bank. Nucleic Acids Res. 28, 235-242
    • (2000) Nucleic Acids Res. , vol.28 , pp. 235-242
    • Berman, H.M.1
  • 20
    • 84941117508 scopus 로고    scopus 로고
    • VirHostNet 2.0: Surfing on the web of virus/host molecular interactions data
    • Guirimand, T., Delmotte, S., and Navratil, V. (2015) VirHostNet 2.0: surfing on the web of virus/host molecular interactions data. Nucleic Acids Res. 43, D583-D7
    • (2015) Nucleic Acids Res. , vol.43 , pp. D583-D587
    • Guirimand, T.1    Delmotte, S.2    Navratil, V.3
  • 22
    • 84907424304 scopus 로고    scopus 로고
    • A mass spectrometry view of stable and transient protein interactions
    • Budayeva, H. G., and Cristea, I. M. (2014) A mass spectrometry view of stable and transient protein interactions. Adv. Exp. Med. Biol. 806, 263-282
    • (2014) Adv. Exp. Med. Biol. , vol.806 , pp. 263-282
    • Budayeva, H.G.1    Cristea, I.M.2
  • 23
    • 58149178567 scopus 로고    scopus 로고
    • PIPs: Human protein-protein interaction prediction database
    • McDowall, M. D., Scott, M. S., and Barton, G. J. (2009) PIPs: human protein-protein interaction prediction database. Nucleic Acids Res. 37, D651-D6
    • (2009) Nucleic Acids Res. , vol.37 , pp. D651-D656
    • McDowall, M.D.1    Scott, M.S.2    Barton, G.J.3
  • 24
    • 84865545263 scopus 로고    scopus 로고
    • A computational framework for boosting confidence in high-throughput protein-protein interaction datasets
    • Hosur, R., Peng, J., Vinayagam, A., Stelzl, U., Xu, J., Perrimon, N., Bienkowska, J., and Berger, B. (2012) A computational framework for boosting confidence in high-throughput protein-protein interaction datasets. Genome Biol. 13, R76
    • (2012) Genome Biol. , vol.13 , pp. R76
    • Hosur, R.1    Peng, J.2    Vinayagam, A.3    Stelzl, U.4    Xu, J.5    Perrimon, N.6    Bienkowska, J.7    Berger, B.8
  • 25
    • 84888103756 scopus 로고    scopus 로고
    • Computational prediction of protein-protein interaction networks: Algorithms and resources
    • Zahiri, J., Bozorgmehr, J. H., and Masoudi-Nejad, A. (2013) Computational prediction of protein-protein interaction networks: algorithms and resources. Curr. Genomics 14, 397-414
    • (2013) Curr. Genomics , vol.14 , pp. 397-414
    • Zahiri, J.1    Bozorgmehr, J.H.2    Masoudi-Nejad, A.3
  • 26
    • 78751584760 scopus 로고    scopus 로고
    • iWRAP: An interface threading approach with application to prediction of cancerrelated protein-protein interactions
    • Hosur, R., Xu, J., Bienkowska, J., and Berger, B. (2011) iWRAP: An interface threading approach with application to prediction of cancerrelated protein-protein interactions. J. Mol. Biol. 405, 1295-1310
    • (2011) J. Mol. Biol. , vol.405 , pp. 1295-1310
    • Hosur, R.1    Xu, J.2    Bienkowska, J.3    Berger, B.4
  • 27
    • 77954278629 scopus 로고    scopus 로고
    • Struct2Net: A web service to predict protein-protein interactions using a structurebased approach
    • Singh, R., Park, D., Xu, J., Hosur, R., and Berger, B. (2010) Struct2Net: a web service to predict protein-protein interactions using a structurebased approach. Nucleic Acids Res. 38, W508-W15
    • (2010) Nucleic Acids Res. , vol.38 , pp. W508-W515
    • Singh, R.1    Park, D.2    Xu, J.3    Hosur, R.4    Berger, B.5
  • 28
    • 84929094094 scopus 로고    scopus 로고
    • Predicting protein-protein interactions from primary protein sequences using a novel multi-scale local feature representation scheme and the random forest
    • You, Z. H., Chan, K. C. C., and Hu, P. (2015) Predicting protein-protein interactions from primary protein sequences using a novel multi-scale local feature representation scheme and the random forest. PLoS ONE 10, e0125811
    • (2015) PLoS ONE , vol.10 , pp. e0125811
    • You, Z.H.1    Chan, K.C.C.2    Hu, P.3
  • 29
    • 79958028560 scopus 로고    scopus 로고
    • Adaptive compressive learning for prediction of protein-protein interactions from primary sequence
    • Zhang, Y. N., Pan, X. Y., Huang, Y., and Shen, H. Bin (2011) Adaptive compressive learning for prediction of protein-protein interactions from primary sequence. J. Theor. Biol. 283, 44-52
    • (2011) J. Theor. Biol. , vol.283 , pp. 44-52
    • Zhang, Y.N.1    Pan, X.Y.2    Huang, Y.3    Bin, S.H.4
  • 30
    • 84908213903 scopus 로고    scopus 로고
    • An improved interolog mapping-based computational prediction of protein-protein interactions with increased network coverage
    • Folador, E. L., Hassan, S. S., Lemke, N., Barh, D., Silva, A., Ferreira, R. S., and Azevedo, V. (2014) An improved interolog mapping-based computational prediction of protein-protein interactions with increased network coverage. Integr. Biol. 6, 1080-1087
    • (2014) Integr. Biol. , vol.6 , pp. 1080-1087
    • Folador, E.L.1    Hassan, S.S.2    Lemke, N.3    Barh, D.4    Silva, A.5    Ferreira, R.S.6    Azevedo, V.7
  • 32
    • 84902747099 scopus 로고    scopus 로고
    • Homology-based prediction of interactions between proteins using averaged one-dependence estimators
    • Murakami, Y., and Mizuguchi, K. (2014) Homology-based prediction of interactions between proteins using Averaged One-Dependence Estimators. BMC Bioinformatics 15, 213
    • (2014) BMC Bioinformatics , vol.15 , pp. 213
    • Murakami, Y.1    Mizuguchi, K.2
  • 33
    • 40049092465 scopus 로고    scopus 로고
    • An assessment of the uses of homologous interactions
    • Saeed, R., and Deane, C. (2008) An assessment of the uses of homologous interactions. Bioinformatics 24, 689-695
    • (2008) Bioinformatics , vol.24 , pp. 689-695
    • Saeed, R.1    Deane, C.2
  • 34
    • 50149119228 scopus 로고    scopus 로고
    • Comprehensive characterization of extracellular herpes simplex virus type 1 virions
    • Loret, S., Guay, G., and Lippé, R. (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    Lippé, R.3
  • 39
    • 0031022820 scopus 로고    scopus 로고
    • Physical and functional interactions between herpes simplex virus immediate-early proteins ICP4 and ICP27
    • Panagiotidis, C. A., Lium, E. K., and Silverstein, S. J. (1997) Physical and functional interactions between herpes simplex virus immediate-early proteins ICP4 and ICP27. J. Virol. 71, 1547-1557
    • (1997) J. Virol. , vol.71 , pp. 1547-1557
    • Panagiotidis, C.A.1    Lium, E.K.2    Silverstein, S.J.3
  • 40
    • 43249090955 scopus 로고    scopus 로고
    • Virion-wide protein interactions of Kaposi's sarcoma-associated herpesvirus
    • Rozen, R., Sathish, N., Li, Y., and Yuan, Y. (2008) Virion-wide protein interactions of Kaposi's sarcoma-associated herpesvirus. J. Virol. 82, 4742-4750
    • (2008) J. Virol. , vol.82 , pp. 4742-4750
    • Rozen, R.1    Sathish, N.2    Li, Y.3    Yuan, Y.4
  • 41
    • 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., and Knipe, D. M. (2004) Proteomics of herpes simplex virus replication compartments: association of cellular DNA replication, repair, recombination, and chromatin remodeling proteins with ICP8. J. Virol. 78, 5856-5866
    • (2004) J. Virol. , vol.78 , pp. 5856-5866
    • Taylor, T.J.1    Knipe, D.M.2
  • 43
    • 79953661477 scopus 로고    scopus 로고
    • Yeast two hybrid analyses reveal novel binary interactions between human cytomegalovirus-encoded virion proteins
    • To, A., Bai, Y., Shen, A., Gong, H., Umamoto, S., Lu, S., and Liu, F. (2011) Yeast two hybrid analyses reveal novel binary interactions between human cytomegalovirus-encoded virion proteins. PLoS ONE 6, e17796
    • (2011) PLoS ONE , vol.6 , pp. e17796
    • To, A.1    Bai, Y.2    Shen, A.3    Gong, H.4    Umamoto, S.5    Lu, S.6    Liu, F.7
  • 44
    • 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., and Diefenbach, R. J. (2008) Identification of structural protein-protein interactions of herpes simplex virus type 1. Virology 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
  • 46
    • 77949440090 scopus 로고    scopus 로고
    • Improving the yeast two-hybrid system with permutated fusions proteins: The varicella zoster virus interactome
    • Stellberger, T., Häuser, R., Baiker, A., Pothineni, V. R., Haas, J., and Uetz, P. (2010) Improving the yeast two-hybrid system with permutated fusions proteins: the Varicella Zoster Virus interactome. Proteome Sci. 8, 8
    • (2010) Proteome Sci. , vol.8 , pp. 8
    • Stellberger, T.1    Häuser, R.2    Baiker, A.3    Pothineni, V.R.4    Haas, J.5    Uetz, P.6
  • 48
    • 84946069451 scopus 로고    scopus 로고
    • UniProt: A hub for protein information
    • The UniProt Consortium
    • The UniProt Consortium (2014) UniProt: a hub for protein information. Nucleic Acids Res. 43, D204-D212
    • (2014) Nucleic Acids Res. , vol.43 , pp. D204-D212
  • 49
    • 84856489442 scopus 로고    scopus 로고
    • HHblits: Lightning-fast iterative protein sequence searching by HMM-HMM alignment
    • Remmert, M., Biegert, A., Hauser, A., and Söding, J. (2012) HHblits: lightning-fast iterative protein sequence searching by HMM-HMM alignment. Nat. Methods 9, 173-175
    • (2012) Nat. Methods , vol.9 , pp. 173-175
    • Remmert, M.1    Biegert, A.2    Hauser, A.3    Söding, J.4
  • 50
    • 84925267288 scopus 로고    scopus 로고
    • UniRef clusters: A comprehensive and scalable alternative for improving sequence similarity searches
    • Suzek, B. E., Wang, Y., Huang, H., McGarvey, P. B., and Wu, C. H. (2015) UniRef clusters: a comprehensive and scalable alternative for improving sequence similarity searches. Bioinformatics 31, 926-932
    • (2015) Bioinformatics , vol.31 , pp. 926-932
    • Suzek, B.E.1    Wang, Y.2    Huang, H.3    McGarvey, P.B.4    Wu, C.H.5
  • 55
    • 84868647779 scopus 로고    scopus 로고
    • Effects of protein interaction data integration, representation and reliability on the use of network properties for drug target prediction
    • Mora, A., and Donaldson, I. M. (2012) Effects of protein interaction data integration, representation and reliability on the use of network properties for drug target prediction. BMC Bioinformatics 13, 294
    • (2012) BMC Bioinformatics , vol.13 , pp. 294
    • Mora, A.1    Donaldson, I.M.2
  • 58
    • 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., Döhner, K., Binz, A., Bauerfeind, R., and Sodeik, B. (2012) Improper tagging of the non-essential small capsid protein VP26 impairs nuclear capsid egress of herpes simplex virus. PLoS ONE 7, e44177
    • (2012) PLoS ONE , vol.7 , pp. e44177
    • Nagel, C.H.1    Döhner, K.2    Binz, A.3    Bauerfeind, R.4    Sodeik, B.5
  • 60
    • 84931006688 scopus 로고    scopus 로고
    • DNA methyltransferase DNMT3A associates with viral proteins and impacts HSV-1 infection
    • Rowles, D. L., Tsai, Y. C., Greco, T. M., Lin, A. E., Li, M., Yeh, J., and Cristea, I. M. (2015) DNA methyltransferase DNMT3A associates with viral proteins and impacts HSV-1 infection. Proteomics 15, 1968-1982
    • (2015) Proteomics , vol.15 , pp. 1968-1982
    • Rowles, D.L.1    Tsai, Y.C.2    Greco, T.M.3    Lin, A.E.4    Li, M.5    Yeh, J.6    Cristea, I.M.7
  • 61
    • 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., Döhner, K., Sodeik, B., and Cristea, I. M. (2013) 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 12, 3237-3252
    • (2013) Mol. Cell. Proteomics , vol.12 , pp. 3237-3252
    • Lin, A.E.1    Greco, T.M.2    Döhner, K.3    Sodeik, B.4    Cristea, I.M.5
  • 63
    • 84895538371 scopus 로고    scopus 로고
    • Minimal, encapsulated proteomic-sample processing applied to copynumber estimation in eukaryotic cells
    • Kulak, N. a, Pichler, G., Paron, I., Nagaraj, N., and Mann, M. (2014) Minimal, encapsulated proteomic-sample processing applied to copynumber estimation in eukaryotic cells. Nat. Methods 11, 319-324
    • (2014) Nat. Methods , vol.11 , pp. 319-324
    • Kulak, N.A.1    Pichler, G.2    Paron, I.3    Nagaraj, N.4    Mann, M.5
  • 66
    • 84881455143 scopus 로고    scopus 로고
    • Mentha: A resource for browsing integrated protein-interaction networks
    • Calderone, A., Castagnoli, L., and Cesareni, G. (2013) mentha: a resource for browsing integrated protein-interaction networks. Nat. Methods 10, 690- 691
    • (2013) Nat. Methods , vol.10 , pp. 690-691
    • Calderone, A.1    Castagnoli, L.2    Cesareni, G.3
  • 67
    • 84891773554 scopus 로고    scopus 로고
    • Negatome 2.0: A database of non-interacting proteins derived by literature mining, manual annotation and protein structure analysis
    • Blohm, P., Frishman, G., Smialowski, P., Goebels, F., Wachinger, B., Ruepp, A., and Frishman, D. (2014) Negatome 2.0: a database of non-interacting proteins derived by literature mining, manual annotation and protein structure analysis. Nucleic Acids Res. 42, D396-D400
    • (2014) Nucleic Acids Res. , vol.42 , pp. D396-D400
    • Blohm, P.1    Frishman, G.2    Smialowski, P.3    Goebels, F.4    Wachinger, B.5    Ruepp, A.6    Frishman, D.7
  • 69
    • 79954617024 scopus 로고    scopus 로고
    • Fusing structure and function: A structural view of the herpesvirus entry machinery
    • Connolly, S. A., Jackson, J. O., Jardetzky, T. S., and Longnecker, R. (2011) Fusing structure and function: a structural view of the herpesvirus entry machinery. Nat. Rev. Microbiol. 9, 369-381
    • (2011) Nat. Rev. Microbiol. , vol.9 , pp. 369-381
    • Connolly, S.A.1    Jackson, J.O.2    Jardetzky, T.S.3    Longnecker, R.4
  • 70
    • 79960400096 scopus 로고    scopus 로고
    • The herpes simplex virus 1 UL17 protein is the second constituent of the capsid vertex-specific component required for DNA packaging and retention
    • Toropova, K., Huffman, J. B., Homa, F. L., and Conway, J. F. (2011) The herpes simplex virus 1 UL17 protein is the second constituent of the capsid vertex-specific component required for DNA packaging and retention. J. Virol. 85, 7513-7522
    • (2011) J. Virol. , vol.85 , pp. 7513-7522
    • Toropova, K.1    Huffman, J.B.2    Homa, F.L.3    Conway, J.F.4
  • 71
    • 0028783737 scopus 로고
    • Herpes simplex virus capsids assembled in insect cells infected with recombinant baculoviruses: Structural authenticity and localization of VP26
    • Trus, B. L., Homa, F. L., Booy, F. P., Newcomb, W. W., Thomsen, D. R., Cheng, N., Brown, J. C., and Steven, A. C. (1995) Herpes simplex virus capsids assembled in insect cells infected with recombinant baculoviruses: structural authenticity and localization of VP26. J. Virol. 69, 7362-7366
    • (1995) J. Virol. , vol.69 , pp. 7362-7366
    • Trus, B.L.1    Homa, F.L.2    Booy, F.P.3    Newcomb, W.W.4    Thomsen, D.R.5    Cheng, N.6    Brown, J.C.7    Steven, A.C.8
  • 72
    • 84861375995 scopus 로고    scopus 로고
    • The UL36 tegument protein of herpes simplex virus 1 has a composite binding site at the capsid vertices
    • Cardone, G., Newcomb, W. W., Cheng, N., Wingfield, P. T., Trus, B. L., Brown, J. C., and Steven, A. C. (2012) The UL36 Tegument Protein of Herpes Simplex Virus 1 Has a Composite Binding Site at the Capsid Vertices. J. Virol. 86, 4058-4064
    • (2012) J. Virol. , vol.86 , pp. 4058-4064
    • Cardone, G.1    Newcomb, W.W.2    Cheng, N.3    Wingfield, P.T.4    Trus, B.L.5    Brown, J.C.6    Steven, A.C.7
  • 73
    • 0028804828 scopus 로고
    • Assembly of VP26 in herpes simplex virus-1 inferred from structures of wild-type and recombinant capsids
    • Zhou, Z. H., He, J., Jakana, J., Tatman, J. D., Rixon, F. J., and Chiu, W. (1995) Assembly of VP26 in herpes simplex virus-1 inferred from structures of wild-type and recombinant capsids. Nat. Struct. Biol. 2, 1026-1030
    • (1995) Nat. Struct. Biol , vol.2 , pp. 1026-1030
    • Zhou, Z.H.1    He, J.2    Jakana, J.3    Tatman, J.D.4    Rixon, F.J.5    Chiu, W.6
  • 74
    • 3142545772 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 capsid protein VP26 Interacts with dynein light chains RP3 and Tctex1 and plays a role in retrograde cellular transport
    • Douglas, M. W., Diefenbach, R. J., Homa, F. L., Miranda-Saksena, M., Rixon, F. J., Vittone, V., Byth, K., and Cunningham, A. L. (2004) Herpes Simplex Virus Type 1 Capsid Protein VP26 Interacts with Dynein Light Chains RP3 and Tctex1 and Plays a Role in Retrograde Cellular Transport. J. Biol. Chem. 279, 28522-28530
    • (2004) J. Biol. Chem. , vol.279 , pp. 28522-28530
    • Douglas, M.W.1    Diefenbach, R.J.2    Homa, F.L.3    Miranda-Saksena, M.4    Rixon, F.J.5    Vittone, V.6    Byth, K.7    Cunningham, A.L.8
  • 75
    • 84923138880 scopus 로고    scopus 로고
    • The herpes simplex virus 1 UL51 protein interacts with the UL7 protein and plays a role in its recruitment into the Virion
    • Roller, R. J., and Fetters, R. (2015) The Herpes Simplex Virus 1 UL51 Protein Interacts with the UL7 Protein and Plays a Role in Its Recruitment into the Virion. J. Virol. 89, 3112-3122
    • (2015) J. Virol. , vol.89 , pp. 3112-3122
    • Roller, R.J.1    Fetters, R.2
  • 76
    • 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., Radtke, K., Schmidt, S., and Sodeik, B. (2006) Eclipse phase of herpes simplex virus type 1 infection: Efficient dynein-mediated 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
  • 77
    • 77951952127 scopus 로고    scopus 로고
    • The power of protein interaction networks for associating genes with diseases
    • Navlakha, S., and Kingsford, C. (2010) The power of protein interaction networks for associating genes with diseases. Bioinformatics 26, 1057-1063
    • (2010) Bioinformatics , vol.26 , pp. 1057-1063
    • Navlakha, S.1    Kingsford, C.2
  • 81
    • 0036733722 scopus 로고    scopus 로고
    • Treasures and traps in genome-wide data sets: Case examples from yeast
    • Grünenfelder, B., and Winzeler, E. A. (2002) Treasures and traps in genome-wide data sets: case examples from yeast. Nat. Rev. Genet. 3, 653-661
    • (2002) Nat. Rev. Genet. , vol.3 , pp. 653-661
    • Grünenfelder, B.1    Winzeler, E.A.2
  • 82
    • 77956321519 scopus 로고    scopus 로고
    • Exhaustive benchmarking of the yeast two-hybrid system
    • Chen, Y. C., Rajagopala, S. V., Stellberger, T., and Uetz, P. (2010) Exhaustive benchmarking of the yeast two-hybrid system. Nat. Methods 7, 667-668
    • (2010) Nat. Methods , vol.7 , pp. 667-668
    • Chen, Y.C.1    Rajagopala, S.V.2    Stellberger, T.3    Uetz, P.4
  • 83
    • 0037432528 scopus 로고    scopus 로고
    • How reliable are experimental protein-protein interaction data? J
    • Sprinzak, E., Sattath, S., and Margalit, H. (2003) How reliable are experimental protein-protein interaction data? J. Mol. Biol. 327, 919-923
    • (2003) Mol. Biol. , vol.327 , pp. 919-923
    • Sprinzak, E.1    Sattath, S.2    Margalit, H.3
  • 84
    • 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., and Person, S. (2008) Localization of herpes simplex virus type 1 UL37 in the Golgi complex requires UL36 but not capsid structures. J. Virol. 82, 11354-11361
    • (2008) J. Virol. , vol.82 , pp. 11354-11361
    • Desai, P.1    Sexton, G.L.2    Huang, E.3    Person, S.4
  • 85
    • 40149086016 scopus 로고    scopus 로고
    • Nuclear egress and envelopment of herpes simplex virus capsids analyzed with dual-color fluorescence HSV1(17ô)
    • Nagel, C. H., Döhner, K., Fathollahy, M., Strive, T., Borst, E. M., Messerle, M., and Sodeik, B. (2008) Nuclear egress and envelopment of herpes simplex virus capsids analyzed with dual-color fluorescence HSV1(17ô). J. Virol. 82, 3109-3124
    • (2008) J. Virol. , vol.82 , pp. 3109-3124
    • Nagel, C.H.1    Döhner, K.2    Fathollahy, M.3    Strive, T.4    Borst, E.M.5    Messerle, M.6    Sodeik, B.7
  • 87
    • 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., and Kawaguchi, Y. (2008) Simultaneous tracking of capsid, tegument, and envelope protein localization in living cells infected with triply fluorescent herpes simplex virus 1. J. Virol. 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
  • 88
    • 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., and Person, S. (2003) Residues of VP26 of herpes simplex virus type 1 that are required for its interaction with capsids. J. Virol. 77, 391-404
    • (2003) J. Virol. , vol.77 , pp. 391-404
    • Desai, P.1    Akpa, J.C.2    Person, S.3
  • 89
    • 33646750547 scopus 로고    scopus 로고
    • The Herpesvirus capsid surface protein, VP26, and the majority of the tegument proteins are dispensable for capsid transport toward the nucleus
    • Antinone, S. E., Shubeita, G. T., Coller, K. E., Lee, J. I., Haverlock-Moyns, S., Gross, S. P., and Smith, G. A. (2006) The Herpesvirus capsid surface protein, VP26, and the majority of the tegument proteins are dispensable for capsid transport toward the nucleus. J. Virol. 80, 5494-5498
    • (2006) J. Virol. , vol.80 , pp. 5494-5498
    • Antinone, S.E.1    Shubeita, G.T.2    Coller, K.E.3    Lee, J.I.4    Haverlock-Moyns, S.5    Gross, S.P.6    Smith, G.A.7
  • 90
    • 0031846233 scopus 로고    scopus 로고
    • Incorporation of the green fluorescent protein into the herpes simplex virus type 1 capsid
    • Desai, P., and Person, S. (1998) Incorporation of the green fluorescent protein into the herpes simplex virus type 1 capsid. J. Virol. 72, 7563-7568
    • (1998) J. Virol. , vol.72 , pp. 7563-7568
    • Desai, P.1    Person, S.2
  • 91
    • 45949096784 scopus 로고    scopus 로고
    • Deletion or green fluorescent protein tagging of the pUL35 capsid component of pseudorabies virus impairs virus replication in cell culture and neuroinvasion in mice
    • Krautwald, M., Maresch, C., Klupp, B. G., Fuchs, W., and Mettenleiter, T. C. (2008) Deletion or green fluorescent protein tagging of the pUL35 capsid component of pseudorabies virus impairs virus replication in cell culture and neuroinvasion in mice. J. Gen. Virol. 89, 1346-1351
    • (2008) J. Gen. Virol. , vol.89 , pp. 1346-1351
    • Krautwald, M.1    Maresch, C.2    Klupp, B.G.3    Fuchs, W.4    Mettenleiter, T.C.5
  • 92
    • 84929625422 scopus 로고    scopus 로고
    • Function of the herpes simplex virus 1 small capsid protein VP26 is regulated by phosphorylation at a specific site
    • Kobayashi, R., Kato, A., Oda, S., Koyanagi, N., Oyama, M., Kozuka-Hata, H., Arii, J., and Kawaguchi, Y. (2015) Function of the Herpes Simplex Virus 1 Small Capsid Protein VP26 Is Regulated by Phosphorylation at a Specific Site. J. Virol. 89, 6141-6147
    • (2015) J. Virol. , vol.89 , pp. 6141-6147
    • Kobayashi, R.1    Kato, A.2    Oda, S.3    Koyanagi, N.4    Oyama, M.5    Kozuka-Hata, H.6    Arii, J.7    Kawaguchi, Y.8
  • 93
    • 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., Steffen, W., Scholz, T., Karger, A., and Sodeik, B. (2010) Plus- and minus-end directed microtubule motors bind simultaneously to herpes simplex virus capsids using different inner tegument structures. PLoS Pathog. 6, 1-20
    • (2010) PLoS Pathog , vol.6 , pp. 1-20
    • Radtke, K.1    Kieneke, D.2    Wolfstein, A.3    Michael, K.4    Steffen, W.5    Scholz, T.6    Karger, A.7    Sodeik, B.8
  • 94
    • 84883422214 scopus 로고    scopus 로고
    • The smallest capsid protein mediates binding of the essential tegument protein pp150 to stabilize DNA-containing capsids in human cytomegalovirus
    • Dai, X., Yu, X., Gong, H., Jiang, X., Abenes, G., Liu, H., Shivakoti, S., Britt, W. J., Zhu, H., Liu, F., and Zhou, Z. H. (2013) The smallest capsid protein mediates binding of the essential tegument protein pp150 to stabilize DNA-containing capsids in human cytomegalovirus. PLoS Pathog. 9, e1003525
    • (2013) PLoS Pathog , vol.9 , pp. e1003525
    • Dai, X.1    Yu, X.2    Gong, H.3    Jiang, X.4    Abenes, G.5    Liu, H.6    Shivakoti, S.7    Britt, W.J.8    Zhu, H.9    Liu, F.10    Zhou, Z.H.11
  • 95
    • 84923308126 scopus 로고    scopus 로고
    • CryoEM and mutagenesis reveal that the smallest capsid protein cements and stabilizes Kaposi's sarcoma-associated herpesvirus capsid
    • Dai, X., Gong, D., Xiao, Y., Wu, T.-T., Sun, R., and Zhou, Z. H. (2015) CryoEM and mutagenesis reveal that the smallest capsid protein cements and stabilizes Kaposi's sarcoma-associated herpesvirus capsid. Proc. Natl. Acad. Sci. U.S.A. 112, E649-E56
    • (2015) Proc. Natl. Acad. Sci. U. S. A , vol.112 , pp. E649-E6456
    • Dai, X.1    Gong, D.2    Xiao, Y.3    Wu, T.-T.4    Sun, R.5    Zhou, Z.H.6
  • 96
    • 0028261190 scopus 로고
    • Finding a needle in a haystack: Detection of a small protein (the 12-kDa VP26) in a large complex (the 200-MDa capsid of herpes simplex virus)
    • Booy, F. P., Trus, B. L., Newcomb, W. W., Brown, J. C., Conway, J. F., and Steven, A. C. (1994) Finding a needle in a haystack: detection of a small protein (the 12-kDa VP26) in a large complex (the 200-MDa capsid of herpes simplex virus). Proc. Natl. Acad. Sci. U.S.A. 91, 5652-5656
    • (1994) Proc. Natl. Acad. Sci. U. S. A , vol.91 , pp. 5652-5656
    • Booy, F.P.1    Trus, B.L.2    Newcomb, W.W.3    Brown, J.C.4    Conway, J.F.5    Steven, A.C.6
  • 97
    • 0035162989 scopus 로고    scopus 로고
    • The pattern of tegument-capsid interaction in the herpes simplex virus type 1 virion is not influenced by the small hexon-associated protein VP26
    • Chen, D. H., Jakana, J., McNab, D., Mitchell, J., Zhou, Z. H., Dougherty, M., Chiu, W., and Rixon, F. J. (2001) The pattern of tegument-capsid interaction in the herpes simplex virus type 1 virion is not influenced by the small hexon-associated protein VP26. J. Virol. 75, 11863-11867
    • (2001) J. Virol. , vol.75 , pp. 11863-11867
    • Chen, D.H.1    Jakana, J.2    McNab, D.3    Mitchell, J.4    Zhou, Z.H.5    Dougherty, M.6    Chiu, W.7    Rixon, F.J.8
  • 98
    • 84895427394 scopus 로고    scopus 로고
    • Association of herpes simplex virus pUL31 with capsid vertices and components of the capsid vertex-specific complex
    • Yang, K., Wills, E., Lim, H. Y., Zhou, Z. H., and Baines, J. D. (2014) Association of herpes simplex virus pUL31 with capsid vertices and components of the capsid vertex-specific complex. J. Virol. 88, 3815-3825
    • (2014) J. Virol. , vol.88 , pp. 3815-3825
    • Yang, K.1    Wills, E.2    Lim, H.Y.3    Zhou, Z.H.4    Baines, J.D.5
  • 99
    • 0034892972 scopus 로고    scopus 로고
    • U(L)31 and U(L)34 proteins of herpes simplex virus type 1 form a complex that accumulates at the nuclear rim and is required for envelopment of nucleocapsids
    • Reynolds, A. E., Ryckman, B. J., Baines, J. D., Zhou, Y., Liang, L., and Roller, R. J. (2001) U(L)31 and U(L)34 proteins of herpes simplex virus type 1 form a complex that accumulates at the nuclear rim and is required for envelopment of nucleocapsids. J. Virol. 75, 8803-8817
    • (2001) J. Virol. , vol.75 , pp. 8803-8817
    • Reynolds, A.E.1    Ryckman, B.J.2    Baines, J.D.3    Zhou, Y.4    Liang, L.5    Roller, R.J.6
  • 100
    • 65349186030 scopus 로고    scopus 로고
    • The U(L)31 and U(L)34 gene products of herpes simplex virus 1 are required for optimal localization of viral glycoproteins D and M to the inner nuclear membranes of infected cells
    • Wills, E., Mou, F., and Baines, J. D. (2009) The U(L)31 and U(L)34 gene products of herpes simplex virus 1 are required for optimal localization of viral glycoproteins D and M to the inner nuclear membranes of infected cells. J. Virol. 83, 4800- 4809
    • (2009) J. Virol. , vol.83 , pp. 4800-4809
    • Wills, E.1    Mou, F.2    Baines, J.D.3
  • 101
    • 33751234823 scopus 로고    scopus 로고
    • Common and specific properties of herpesvirus UL34/UL31 protein family members revealed by protein complementation assay
    • Schnee, M., Ruzsics, Z., Bubeck, A., and Koszinowski, U. H. (2006) Common and specific properties of herpesvirus UL34/UL31 protein family members revealed by protein complementation assay. J. Virol. 80, 11658-11666
    • (2006) J. Virol. , vol.80 , pp. 11658-11666
    • Schnee, M.1    Ruzsics, Z.2    Bubeck, A.3    Koszinowski, U.H.4
  • 102
    • 84936774563 scopus 로고    scopus 로고
    • The herpes simplex virus protein pUL31 escorts nucleocapsids to sites of nuclear egress, a process coordinated by Its N-Terminal domain
    • Funk, C., Ott, M., Raschbichler, V., Nagel, C. H., Binz, A., Sodeik, B., Bauerfeind, R., and Bailer, S. M. (2015) The Herpes Simplex Virus Protein pUL31 Escorts Nucleocapsids to Sites of Nuclear Egress, a Process Coordinated by Its N-Terminal Domain. PLoS Pathog. 11, e1004957
    • (2015) PLoS Pathog , vol.11 , pp. e1004957
    • Funk, C.1    Ott, M.2    Raschbichler, V.3    Nagel, C.H.4    Binz, A.5    Sodeik, B.6    Bauerfeind, R.7    Bailer, S.M.8
  • 106
    • 80052277727 scopus 로고    scopus 로고
    • The ribonucleotide reductase R1 subunits of herpes simplex virus 1 and 2 protect cells against poly(I ô C)-induced apoptosis
    • Dufour, F., Bertrand, L., Pearson, A., Grandvaux, N., and Langelier, Y. (2011) The ribonucleotide reductase R1 subunits of herpes simplex virus 1 and 2 protect cells against poly(I ô C)-induced apoptosis. J. Virol. 85, 8689- 8701
    • (2011) J. Virol. , vol.85 , pp. 8689-8701
    • Dufour, F.1    Bertrand, L.2    Pearson, A.3    Grandvaux, N.4    Langelier, Y.5
  • 107
    • 33747090604 scopus 로고    scopus 로고
    • Ribonucleotide reductase inhibitors as anti-herpes agents
    • Wnuk, S. F., and Robins, M. J. (2006) Ribonucleotide reductase inhibitors as anti-herpes agents. Antiviral Res. 71, 122-126
    • (2006) Antiviral Res. , vol.71 , pp. 122-126
    • Wnuk, S.F.1    Robins, M.J.2
  • 109
    • 0036843525 scopus 로고    scopus 로고
    • The R1 subunit of herpes simplex virus ribonucleotide reductase protects cells against apoptosis at, or upstream of, caspase-8 activation
    • Langelier, Y., Bergeron, S., Chabaud, S., Lippens, J., Guilbault, C., Sasseville, A. M. J., Denis, S., Mosser, D. D., and Massie, B. (2002) The R1 subunit of herpes simplex virus ribonucleotide reductase protects cells against apoptosis at, or upstream of, caspase-8 activation. J. Gen. Virol. 83, 2779-2789
    • (2002) J. Gen. Virol. , vol.83 , pp. 2779-2789
    • Langelier, Y.1    Bergeron, S.2    Chabaud, S.3    Lippens, J.4    Guilbault, C.5    Sasseville, A.M.J.6    Denis, S.7    Mosser, D.D.8    Massie, B.9
  • 110
    • 33846794626 scopus 로고    scopus 로고
    • The ribonucleotide reductase domain of the R1 subunit of herpes simplex virus type 2 ribonucleotide reductase is essential for R1 antiapoptotic function
    • Chabaud, S., Sasseville, A. M. J., Elahi, S. M., Caron, A., Dufour, F., Massie, B., and Langelier, Y. (2007) The ribonucleotide reductase domain of the R1 subunit of herpes simplex virus type 2 ribonucleotide reductase is essential for R1 antiapoptotic function. J. Gen. Virol. 88, 384-394
    • (2007) J. Gen. Virol. , vol.88 , pp. 384-394
    • Chabaud, S.1    Sasseville, A.M.J.2    Elahi, S.M.3    Caron, A.4    Dufour, F.5    Massie, B.6    Langelier, Y.7
  • 111
    • 84929948113 scopus 로고    scopus 로고
    • Manipulation of apoptosis and necroptosis signaling by herpesviruses
    • Guo, H., Kaiser, W. J., and Mocarski, E. S. (2015) Manipulation of apoptosis and necroptosis signaling by herpesviruses. Med. Microbiol. Immunol. 204, 439-448
    • (2015) Med. Microbiol. Immunol , vol.204 , pp. 439-448
    • Guo, H.1    Kaiser, W.J.2    Mocarski, E.S.3
  • 112
    • 0033928112 scopus 로고    scopus 로고
    • Evidence for controlled incorporation of herpes simplex virus type 1 UL26 protease into capsids
    • Sheaffer, A. K., Newcomb, W. W., Brown, J. C., Gao, M., Weller, S. K., and Tenney, D. J. (2000) Evidence for controlled incorporation of herpes simplex virus type 1 UL26 protease into capsids. J. Virol. 74, 6838-6848
    • (2000) J. Virol. , vol.74 , pp. 6838-6848
    • Sheaffer, A.K.1    Newcomb, W.W.2    Brown, J.C.3    Gao, M.4    Weller, S.K.5    Tenney, D.J.6
  • 113
    • 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., and Homa, F. L. (1995) 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. 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
  • 114
    • 84919431403 scopus 로고    scopus 로고
    • The Putative Herpes Simplex Virus 1 Chaperone Protein UL32 modulates disulfide bond formation during infection
    • Albright, B. S., Kosinski, A., Szczepaniak, R., Cook, E. a, Stow, N. D., Conway, J. F., and Weller, S. K. (2015) The Putative Herpes Simplex Virus 1 Chaperone Protein UL32 Modulates Disulfide Bond Formation during Infection. J. Virol. 89, 443- 453
    • (2015) J. Virol. , vol.89 , pp. 443-453
    • Albright, B.S.1    Kosinski, A.2    Szczepaniak, R.3    Cook, E.A.4    Stow, N.D.5    Conway, J.F.6    Weller, S.K.7
  • 115
    • 35148896264 scopus 로고    scopus 로고
    • Pseudorabies virus Us9 directs axonal sorting of viral capsids
    • Lyman, M. G., Feierbach, B., Curanovic, D., Bisher, M., and Enquist, L. W. (2007) Pseudorabies virus Us9 directs axonal sorting of viral capsids. J. Virol. 81, 11363-11371
    • (2007) J. Virol. , vol.81 , pp. 11363-11371
    • Lyman, M.G.1    Feierbach, B.2    Curanovic, D.3    Bisher, M.4    Enquist, L.W.5
  • 116
    • 55249103906 scopus 로고    scopus 로고
    • Herpes simplex virus gE/gI and US9 proteins promote transport of both capsids and virion glycoproteins in neuronal axons
    • Snyder, A., Polcicova, K., and Johnson, D. C. (2008) Herpes simplex virus gE/gI and US9 proteins promote transport of both capsids and virion glycoproteins in neuronal axons. J. Virol. 82, 10613-10624
    • (2008) J. Virol. , vol.82 , pp. 10613-10624
    • Snyder, A.1    Polcicova, K.2    Johnson, D.C.3
  • 117
    • 0035921429 scopus 로고    scopus 로고
    • A conserved alpha-herpesvirus protein necessary for axonal localization of viral membrane proteins
    • Tomishima, M. J., and Enquist, L. W. (2001) A conserved alpha-herpesvirus protein necessary for axonal localization of viral membrane proteins. J. Cell Biol. 154, 741-752
    • (2001) J. Cell Biol. , vol.154 , pp. 741-752
    • Tomishima, M.J.1    Enquist, L.W.2
  • 118
    • 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., and Steven, A. C. (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    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
  • 119
    • 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. H., Ueda, A., and Smith, G. A. (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.H.2    Ueda, A.3    Smith, G.A.4
  • 120
    • 84861163767 scopus 로고    scopus 로고
    • Alphaherpesvirus infection disrupts mitochondrial transport in neurons
    • Kramer, T., and Enquist, L. W. (2012) Alphaherpesvirus infection disrupts mitochondrial transport in neurons. Cell. Host Microbe 11, 504-514
    • (2012) Cell. Host Microbe , vol.11 , pp. 504-514
    • Kramer, T.1    Enquist, L.W.2
  • 122
    • 84874657339 scopus 로고    scopus 로고
    • Stuck in the middle: Structural insights into the role of the gH/gL heterodimer in herpesvirus entry
    • Stampfer, S. D., and Heldwein, E. E. (2013) Stuck in the middle: structural insights into the role of the gH/gL heterodimer in herpesvirus entry. Curr. Opin. Virol. 3, 13-19
    • (2013) Curr. Opin. Virol. , vol.3 , pp. 13-19
    • Stampfer, S.D.1    Heldwein, E.E.2
  • 125
    • 0032424034 scopus 로고    scopus 로고
    • Identification and characterization of the herpes simplex virus type 1 UL51 gene product
    • Daikoku, T., Ikenoya, K., Yamada, H., Goshima, F., and Nishiyama, Y. (1998) Identification and characterization of the herpes simplex virus type 1 UL51 gene product. J. Gen. Virol. 79, 3027-3031
    • (1998) J. Gen. Virol. , vol.79 , pp. 3027-3031
    • Daikoku, T.1    Ikenoya, K.2    Yamada, H.3    Goshima, F.4    Nishiyama, Y.5
  • 126
    • 0031010137 scopus 로고    scopus 로고
    • The pseudorabies virus UL51 gene product is a 30-kilodalton virion component
    • Lenk, M., Visser, N., and Mettenleiter, T. C. (1997) The pseudorabies virus UL51 gene product is a 30-kilodalton virion component. J. Virol. 71, 5635-5638
    • (1997) J. Virol. , vol.71 , pp. 5635-5638
    • Lenk, M.1    Visser, N.2    Mettenleiter, T.C.3
  • 127
    • 18744413267 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 UL51 protein is involved in maturation and egress of virus particles
    • Nozawa, N., Kawaguchi, Y., Tanaka, M., Kato, A., Kato, A., Kimura, H., and Nishiyama, Y. (2005) Herpes simplex virus type 1 UL51 protein is involved in maturation and egress of virus particles. J. Virol. 79, 6947-6956
    • (2005) J. Virol. , vol.79 , pp. 6947-6956
    • Nozawa, N.1    Kawaguchi, Y.2    Tanaka, M.3    Kato, A.4    Kato, A.5    Kimura, H.6    Nishiyama, Y.7
  • 128
    • 84896969898 scopus 로고    scopus 로고
    • The herpes simplex virus 1 UL51 gene product has cell type-specific functions in cell-to-cell spread
    • Roller, R. J., Haugo, A. C., Yang, K., and Baines, J. D. (2014) The Herpes Simplex Virus 1 UL51 Gene Product Has Cell Type-Specific Functions in Cell-to-Cell Spread. J. Virol. 88, 4058-4068
    • (2014) J. Virol. , vol.88 , pp. 4058-4068
    • Roller, R.J.1    Haugo, A.C.2    Yang, K.3    Baines, J.D.4
  • 129
    • 1542377535 scopus 로고    scopus 로고
    • Simultaneous deletion of pseudorabies virus tegument protein UL11 and glycoprotein M severely impairs secondary envelopment
    • Kopp, M., Granzow, H., Fuchs, W., Klupp, B., and Mettenleiter, T. C. (2004) Simultaneous deletion of pseudorabies virus tegument protein UL11 and glycoprotein M severely impairs secondary envelopment. J. Virol. 78, 3024-3034
    • (2004) J. Virol. , vol.78 , pp. 3024-3034
    • Kopp, M.1    Granzow, H.2    Fuchs, W.3    Klupp, B.4    Mettenleiter, T.C.5
  • 130
    • 58149502561 scopus 로고    scopus 로고
    • Effects of simultaneous deletion of pUL11 and glycoprotein M on virion maturation of herpes simplex virus type 1
    • Leege, T., Fuchs, W., Granzow, H., Kopp, M., Klupp, B. G., and Mettenleiter, T. C. (2009) Effects of simultaneous deletion of pUL11 and glycoprotein M on virion maturation of herpes simplex virus type 1. J. Virol. 83, 896-907
    • (2009) J. Virol. , vol.83 , pp. 896-907
    • Leege, T.1    Fuchs, W.2    Granzow, H.3    Kopp, M.4    Klupp, B.G.5    Mettenleiter, T.C.6
  • 131
    • 36348978139 scopus 로고    scopus 로고
    • Dynamic interactions of the UL16 tegument protein with the capsid of herpes simplex virus
    • Meckes, D. G., and Wills, J. W. (2007) Dynamic interactions of the UL16 tegument protein with the capsid of herpes simplex virus. J. Virol. 81, 13028-13036
    • (2007) J. Virol. , vol.81 , pp. 13028-13036
    • Meckes, D.G.1    Wills, J.W.2
  • 132
    • 55249090937 scopus 로고    scopus 로고
    • Analysis of the interaction between the UL11 and UL16 tegument proteins of herpes simplex virus
    • Yeh, P. C., Meckes, D. G., and Wills, J. W. (2008) Analysis of the interaction between the UL11 and UL16 tegument proteins of herpes simplex virus. J. Virol. 82, 10693-10700
    • (2008) J. Virol. , vol.82 , pp. 10693-10700
    • Yeh, P.C.1    Meckes, D.G.2    Wills, J.W.3
  • 133
    • 0344080584 scopus 로고    scopus 로고
    • The pseudorabies virus UL11 protein is a virion component involved in secondary envelopment in the cytoplasm
    • Kopp, M., Granzow, H., Fuchs, W., Klupp, B. G., Mundt, E., Karger, A., and Mettenleiter, T. C. (2003) The pseudorabies virus UL11 protein is a virion component involved in secondary envelopment in the cytoplasm. J. Virol. 77, 5339-5351
    • (2003) J. Virol. , vol.77 , pp. 5339-5351
    • Kopp, M.1    Granzow, H.2    Fuchs, W.3    Klupp, B.G.4    Mundt, E.5    Karger, A.6    Mettenleiter, T.C.7
  • 134
    • 0142092454 scopus 로고    scopus 로고
    • Binding partners for the UL11 tegument protein of herpes simplex virus type 1
    • Loomis, J. S., Courtney, R. J., and Wills, J. W. (2003) Binding partners for the UL11 tegument protein of herpes simplex virus type 1. J. Virol. 77, 11417-11424
    • (2003) J. Virol. , vol.77 , pp. 11417-11424
    • Loomis, J.S.1    Courtney, R.J.2    Wills, J.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.