메뉴 건너뛰기




Volumn 15, Issue 12, 2015, Pages 1957-1967

Proteomic analysis of the herpes simplex virus 1 virion protein 16 transactivator protein in infected cells

Author keywords

Herpes simplex virus; ICP4; Infected; Microbiology; VP16

Indexed keywords

CELL PROTEIN; HOST CELL FACTOR 1; INFECTED CELL PROTEIN 4; OCTAMER TRANSCRIPTION FACTOR 1; PROTEIN VP16; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG; HERPES SIMPLEX VIRUS IE3 PROTEIN, HUMAN HERPESVIRUS 1; IMMEDIATE EARLY PROTEIN; PROTEOME; TRANSACTIVATOR PROTEIN;

EID: 84930971966     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201500020     Document Type: Article
Times cited : (15)

References (97)
  • 1
    • 0023731010 scopus 로고
    • SV40 large tumor antigen forms a specific complex with the product of the retinoblastoma susceptibility gene
    • DeCaprio, J. A., Ludlow, J. W., Figge, J., Shew, J. Y. et al., SV40 large tumor antigen forms a specific complex with the product of the retinoblastoma susceptibility gene. Cell 1988, 54, 275-283.
    • (1988) Cell , vol.54 , pp. 275-283
    • DeCaprio, J.A.1    Ludlow, J.W.2    Figge, J.3    Shew, J.Y.4
  • 2
    • 0018348655 scopus 로고
    • T antigen is bound to a host protein in SV40-transformed cells
    • Lane, D. P., Crawford, L. V., T antigen is bound to a host protein in SV40-transformed cells. Nature 1979, 278, 261-263.
    • (1979) Nature , vol.278 , pp. 261-263
    • Lane, D.P.1    Crawford, L.V.2
  • 3
    • 0018769971 scopus 로고
    • Simian virus 40-transformed cells express new species of proteins precipitable by anti-simian virus 40 tumor serum
    • Kress, M., May, E., Cassingena, R., May, P., Simian virus 40-transformed cells express new species of proteins precipitable by anti-simian virus 40 tumor serum. J. Virol. 1979, 31, 472-483.
    • (1979) J. Virol. , vol.31 , pp. 472-483
    • Kress, M.1    May, E.2    Cassingena, R.3    May, P.4
  • 4
    • 0018760324 scopus 로고
    • Characterization of a 54K dalton cellular SV40 tumor antigen present in SV40-transformed cells and uninfected embryonal carcinoma cells
    • Linzer, D. I., Levine, A. J., Characterization of a 54K dalton cellular SV40 tumor antigen present in SV40-transformed cells and uninfected embryonal carcinoma cells. Cell 1979, 17, 43-52.
    • (1979) Cell , vol.17 , pp. 43-52
    • Linzer, D.I.1    Levine, A.J.2
  • 5
    • 0020079972 scopus 로고
    • Adenovirus E1b-58kd tumor antigen and SV40 large tumor antigen are physically associated with the same 54 kd cellular protein in transformed cells
    • Sarnow, P., Ho, Y. S., Williams, J., Levine, A. J., Adenovirus E1b-58kd tumor antigen and SV40 large tumor antigen are physically associated with the same 54 kd cellular protein in transformed cells. Cell 1982, 28, 387-394.
    • (1982) Cell , vol.28 , pp. 387-394
    • Sarnow, P.1    Ho, Y.S.2    Williams, J.3    Levine, A.J.4
  • 6
    • 0022589970 scopus 로고
    • Association of adenovirus early-region 1A proteins with cellular polypeptides
    • Harlow, E., Whyte, P., Franza, B. R., Jr., Schley, C., Association of adenovirus early-region 1A proteins with cellular polypeptides. Mol. Cell. Biol. 1986, 6, 1579-1589.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 1579-1589
    • Harlow, E.1    Whyte, P.2    Franza, B.R.3    Schley, C.4
  • 7
    • 0024968181 scopus 로고
    • Cellular targets for transformation by the adenovirus E1A proteins
    • Whyte, P., Williamson, N. M., Harlow, E., Cellular targets for transformation by the adenovirus E1A proteins. Cell 1989, 56, 67-75.
    • (1989) Cell , vol.56 , pp. 67-75
    • Whyte, P.1    Williamson, N.M.2    Harlow, E.3
  • 8
    • 0025271203 scopus 로고
    • Association of human papillomavirus types 16 and 18 E6 proteins with p53
    • Werness, B. A., Levine, A. J., Howley, P. M., Association of human papillomavirus types 16 and 18 E6 proteins with p53. Science 1990, 248, 76-79.
    • (1990) Science , vol.248 , pp. 76-79
    • Werness, B.A.1    Levine, A.J.2    Howley, P.M.3
  • 9
    • 0024535228 scopus 로고
    • The human papilloma virus-16 E7 oncoprotein is able to bind to the retinoblastoma gene product
    • Dyson, N., Howley, P. M., Munger, K., Harlow, E., The human papilloma virus-16 E7 oncoprotein is able to bind to the retinoblastoma gene product. Science 1989, 243, 934-937.
    • (1989) Science , vol.243 , pp. 934-937
    • Dyson, N.1    Howley, P.M.2    Munger, K.3    Harlow, E.4
  • 10
    • 0027358723 scopus 로고
    • The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53
    • Scheffner, M., Huibregtse, J. M., Vierstra, R. D., Howley, P. M., The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53. Cell 1993, 75, 495-505.
    • (1993) Cell , vol.75 , pp. 495-505
    • Scheffner, M.1    Huibregtse, J.M.2    Vierstra, R.D.3    Howley, P.M.4
  • 11
    • 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
  • 12
    • 0024384325 scopus 로고
    • Herpes simplex virus alpha protein ICP27 possesses separable positive and negative regulatory activities
    • Rice, S. A., Su, L. S., Knipe, D. M., Herpes simplex virus alpha protein ICP27 possesses separable positive and negative regulatory activities. J. Virol. 1989, 63, 3399-3407.
    • (1989) J. Virol. , vol.63 , pp. 3399-3407
    • Rice, S.A.1    Su, L.S.2    Knipe, D.M.3
  • 13
    • 0024356969 scopus 로고
    • Herpes simplex virus alpha protein ICP27 can inhibit or augment viral gene transactivation
    • Su, L., Knipe, D. M., Herpes simplex virus alpha protein ICP27 can inhibit or augment viral gene transactivation. Virology 1989, 170, 496-504.
    • (1989) Virology , vol.170 , pp. 496-504
    • Su, L.1    Knipe, D.M.2
  • 14
    • 0024266415 scopus 로고
    • The herpes simplex virus type 1 alpha protein ICP27 can act as a trans-repressor or a trans-activator in combination with ICP4 and ICP0
    • Sekulovich, R. E., Leary, K., Sandri-Goldin, R. M., The herpes simplex virus type 1 alpha protein ICP27 can act as a trans-repressor or a trans-activator in combination with ICP4 and ICP0. J. Virol.1988, 62, 4510-4522.
    • (1988) J. Virol , vol.62 , pp. 4510-4522
    • Sekulovich, R.E.1    Leary, K.2    Sandri-Goldin, R.M.3
  • 15
    • 0023723156 scopus 로고
    • Gene-specific transactivation by herpes simplex virus type 1 alpha protein ICP27
    • Rice, S. A., Knipe, D. M., Gene-specific transactivation by herpes simplex virus type 1 alpha protein ICP27. J. Virol. 1988, 62, 3814-3823.
    • (1988) J. Virol. , vol.62 , pp. 3814-3823
    • Rice, S.A.1    Knipe, D.M.2
  • 16
    • 0035837047 scopus 로고    scopus 로고
    • Herpes simplex virus 1 ICP27 is required for transcription of two viral late (gamma 2) genes in infected cells
    • Jean, S., LeVan, K. M., Song, B., Levine, M., Knipe, D. M., Herpes simplex virus 1 ICP27 is required for transcription of two viral late (gamma 2) genes in infected cells. Virology 2001, 283, 273-284.
    • (2001) Virology , vol.283 , pp. 273-284
    • Jean, S.1    LeVan, K.M.2    Song, B.3    Levine, M.4    Knipe, D.M.5
  • 17
    • 0022268933 scopus 로고
    • Herpes simplex virus type 1 ICP27 is an essential regulatory protein
    • Sacks, W. R., Greene, C. C., Aschman, D. P., Schaffer, P. A., Herpes simplex virus type 1 ICP27 is an essential regulatory protein. J. Virol. 1985, 55, 796-805.
    • (1985) J. Virol. , vol.55 , pp. 796-805
    • Sacks, W.R.1    Greene, C.C.2    Aschman, D.P.3    Schaffer, P.A.4
  • 18
    • 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
  • 19
    • 0026696627 scopus 로고
    • A novel transcription factor reveals a functional link between the RNA polymerase II CTD and TFIID
    • Koleske, A. J., Buratowski, S., Nonet, M., Young, R. A., A novel transcription factor reveals a functional link between the RNA polymerase II CTD and TFIID. Cell 1992, 69, 883-894.
    • (1992) Cell , vol.69 , pp. 883-894
    • Koleske, A.J.1    Buratowski, S.2    Nonet, M.3    Young, R.A.4
  • 20
    • 25144501171 scopus 로고    scopus 로고
    • Yeast mediator and its role in transcriptional regulation
    • Biddick, R., Young, E. T., Yeast mediator and its role in transcriptional regulation. C. R. Biol. 2005, 328, 773-782.
    • (2005) C. R. Biol. , vol.328 , pp. 773-782
    • Biddick, R.1    Young, E.T.2
  • 21
    • 14844349559 scopus 로고    scopus 로고
    • Structural and functional characterization of PC2 and RNA polymerase II-associated subpopulations of metazoan mediator
    • Malik, S., Baek, H. J., Wu, W., Roeder, R. G., Structural and functional characterization of PC2 and RNA polymerase II-associated subpopulations of metazoan mediator. Mol. Cell. Biol. 2005, 25, 2117-2129.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 2117-2129
    • Malik, S.1    Baek, H.J.2    Wu, W.3    Roeder, R.G.4
  • 22
    • 0032900980 scopus 로고    scopus 로고
    • Intermediates in formation and activity of the RNA polymerase II preinitiation complex: holoenzyme recruitment and a postrecruitment role for the TATA box and TFIIB
    • Ranish, J. A., Yudkovsky, N., Hahn, S., Intermediates in formation and activity of the RNA polymerase II preinitiation complex: holoenzyme recruitment and a postrecruitment role for the TATA box and TFIIB. Genes Dev. 1999, 13, 49-63.
    • (1999) Genes Dev. , vol.13 , pp. 49-63
    • Ranish, J.A.1    Yudkovsky, N.2    Hahn, S.3
  • 23
    • 0142123132 scopus 로고    scopus 로고
    • Activation domain-mediator interactions promote transcription preinitiation complex assembly on promoter DNA
    • Cantin, G. T., Stevens, J. L., Berk, A. J., Activation domain-mediator interactions promote transcription preinitiation complex assembly on promoter DNA. Proc. Natl. Acad. Sci. U S A 2003, 100, 12003-12008.
    • (2003) Proc. Natl. Acad. Sci. U S A , vol.100 , pp. 12003-12008
    • Cantin, G.T.1    Stevens, J.L.2    Berk, A.J.3
  • 24
    • 48349122949 scopus 로고    scopus 로고
    • Mediator links epigenetic silencing of neuronal gene expression with x-linked mental retardation
    • Ding, N., Zhou, H., Esteve, P. O., Chin, H. G. et al., Mediator links epigenetic silencing of neuronal gene expression with x-linked mental retardation. Mol. Cell 2008, 31, 347-359.
    • (2008) Mol. Cell , vol.31 , pp. 347-359
    • Ding, N.1    Zhou, H.2    Esteve, P.O.3    Chin, H.G.4
  • 25
    • 59149096820 scopus 로고    scopus 로고
    • MED19 and MED26 are synergistic functional targets of the RE1 silencing transcription factor in epigenetic silencing of neuronal gene expression
    • Ding, N., Tomomori-Sato, C., Sato, S., Conaway, R. C. et al., MED19 and MED26 are synergistic functional targets of the RE1 silencing transcription factor in epigenetic silencing of neuronal gene expression. J. Biol. Chem. 2009, 284, 2648-2656.
    • (2009) J. Biol. Chem. , vol.284 , pp. 2648-2656
    • Ding, N.1    Tomomori-Sato, C.2    Sato, S.3    Conaway, R.C.4
  • 26
    • 84876895132 scopus 로고    scopus 로고
    • Suv4-20h2 mediates chromatin compaction and is important for cohesin recruitment to heterochromatin
    • Hahn, M., Dambacher, S., Dulev, S., Kuznetsova, A. Y. et al., Suv4-20h2 mediates chromatin compaction and is important for cohesin recruitment to heterochromatin. Genes Dev. 2013, 27, 859-872.
    • (2013) Genes Dev. , vol.27 , pp. 859-872
    • Hahn, M.1    Dambacher, S.2    Dulev, S.3    Kuznetsova, A.Y.4
  • 27
    • 84880560782 scopus 로고    scopus 로고
    • Mediator complex recruits epigenetic regulators via its two cyclin-dependent kinase subunits to repress transcription of immune response genes
    • Tsutsui, T., Fukasawa, R., Shinmyouzu, K., Nakagawa, R. et al., Mediator complex recruits epigenetic regulators via its two cyclin-dependent kinase subunits to repress transcription of immune response genes. J. Biol. Chem. 2013, 288, 20955-20965.
    • (2013) J. Biol. Chem. , vol.288 , pp. 20955-20965
    • Tsutsui, T.1    Fukasawa, R.2    Shinmyouzu, K.3    Nakagawa, R.4
  • 28
    • 84876216563 scopus 로고    scopus 로고
    • Master transcription factors and mediator establish super-enhancers at key cell identity genes
    • Whyte, W. A., Orlando, D. A., Hnisz, D., Abraham, B. J. et al., Master transcription factors and mediator establish super-enhancers at key cell identity genes. Cell 2013, 153, 307-319.
    • (2013) Cell , vol.153 , pp. 307-319
    • Whyte, W.A.1    Orlando, D.A.2    Hnisz, D.3    Abraham, B.J.4
  • 29
    • 84876222028 scopus 로고    scopus 로고
    • Selective inhibition of tumor oncogenes by disruption of super-enhancers
    • Loven, J., Hoke, H. A., Lin, C. Y., Lau, A. et al., Selective inhibition of tumor oncogenes by disruption of super-enhancers. Cell 2013, 153, 320-334.
    • (2013) Cell , vol.153 , pp. 320-334
    • Loven, J.1    Hoke, H.A.2    Lin, C.Y.3    Lau, A.4
  • 30
    • 34547525335 scopus 로고    scopus 로고
    • Identification of a regulator of transcription elongation as an accessory factor for the human Mediator coactivator
    • Malik, S., Barrero, M. J., Jones, T., Identification of a regulator of transcription elongation as an accessory factor for the human Mediator coactivator. Proc. Natl. Acad. Sci. USA 2007, 104, 6182-6187.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 6182-6187
    • Malik, S.1    Barrero, M.J.2    Jones, T.3
  • 31
    • 76349090199 scopus 로고    scopus 로고
    • CDK8 is a positive regulator of transcriptional elongation within the serum response network
    • Donner, A. J., Ebmeier, C. C., Taatjes, D. J., Espinosa, J. M., CDK8 is a positive regulator of transcriptional elongation within the serum response network. Nat. Struct. Mol. Biol. 2010, 17, 194-201.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 194-201
    • Donner, A.J.1    Ebmeier, C.C.2    Taatjes, D.J.3    Espinosa, J.M.4
  • 32
    • 79959939884 scopus 로고    scopus 로고
    • Human mediator subunit MED26 functions as a docking site for transcription elongation factors
    • Takahashi, H., Parmely, T. J., Sato, S., Tomomori-Sato, C. et al., Human mediator subunit MED26 functions as a docking site for transcription elongation factors. Cell 2011, 146, 92-104.
    • (2011) Cell , vol.146 , pp. 92-104
    • Takahashi, H.1    Parmely, T.J.2    Sato, S.3    Tomomori-Sato, C.4
  • 33
    • 80054818717 scopus 로고    scopus 로고
    • Novel role for mediator complex subunit Srb5/Med18 in termination of transcription
    • Mukundan, B., Ansari, A., Novel role for mediator complex subunit Srb5/Med18 in termination of transcription. J. Biol. Chem. 2011, 286, 37053-37057.
    • (2011) J. Biol. Chem. , vol.286 , pp. 37053-37057
    • Mukundan, B.1    Ansari, A.2
  • 34
    • 84862777556 scopus 로고    scopus 로고
    • Mediator complex regulates alternative mRNA processing via the MED23 subunit
    • Huang, Y., Li, W., Yao, X., Lin, Q. J. et al., Mediator complex regulates alternative mRNA processing via the MED23 subunit. Mol. Cell 2012, 45, 459-469.
    • (2012) Mol. Cell , vol.45 , pp. 459-469
    • Huang, Y.1    Li, W.2    Yao, X.3    Lin, Q.J.4
  • 35
    • 0033614417 scopus 로고    scopus 로고
    • Ligand-dependent transcription activation by nuclear receptors requires the DRIP complex
    • Rachez, C., Lemon, B. D., Suldan, Z., Bromleigh, V. et al., Ligand-dependent transcription activation by nuclear receptors requires the DRIP complex. Nature 1999, 398, 824-828.
    • (1999) Nature , vol.398 , pp. 824-828
    • Rachez, C.1    Lemon, B.D.2    Suldan, Z.3    Bromleigh, V.4
  • 36
    • 0037022631 scopus 로고    scopus 로고
    • The TRAP/mediator coactivator complex interacts directly with estrogen receptors alpha and beta through the TRAP220 subunit and directly enhances estrogen receptor function in vitro
    • Kang, Y. K., Guermah, M., Yuan, C. X., Roeder, R. G., The TRAP/mediator coactivator complex interacts directly with estrogen receptors alpha and beta through the TRAP220 subunit and directly enhances estrogen receptor function in vitro. Proc. Natl. Acad. Sci. USA 2002, 99, 2642-2647.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 2642-2647
    • Kang, Y.K.1    Guermah, M.2    Yuan, C.X.3    Roeder, R.G.4
  • 37
    • 33747053907 scopus 로고    scopus 로고
    • An ARC/mediator subunit required for SREBP control of cholesterol and lipid homeostasis
    • Yang, F., Vought, B. W., Satterlee, J. S., Walker, A. K. et al., An ARC/mediator subunit required for SREBP control of cholesterol and lipid homeostasis. Nature 2006, 442, 700-704.
    • (2006) Nature , vol.442 , pp. 700-704
    • Yang, F.1    Vought, B.W.2    Satterlee, J.S.3    Walker, A.K.4
  • 38
    • 84894084126 scopus 로고    scopus 로고
    • The mediator complex: a master coordinator of transcription and cell lineage development
    • Yin, J. W., Wang, G., The mediator complex: a master coordinator of transcription and cell lineage development. Development 2014, 141, 977-987.
    • (2014) Development , vol.141 , pp. 977-987
    • Yin, J.W.1    Wang, G.2
  • 39
    • 51849135855 scopus 로고    scopus 로고
    • Knipe, D. M., Howley, P. M. (Eds.), Lippincott Williams & Wilkins, Philadelphia
    • Roizman, B., Knipe, D. M., Whitley, R. J., in: Knipe, D. M., Howley, P. M. (Eds.), Fields Virology, Lippincott Williams & Wilkins, Philadelphia 2013, pp. 1823-1897.
    • (2013) Fields Virology , pp. 1823-1897
    • Roizman, B.1    Knipe, D.M.2    Whitley, R.J.3
  • 40
    • 84870662113 scopus 로고    scopus 로고
    • Snapshots: chromatin control of viral infection
    • Knipe, D. M., Lieberman, P. M., Jung, J. U., McBride, A. A. et al., Snapshots: chromatin control of viral infection. Virology 2013, 435, 141-156.
    • (2013) Virology , vol.435 , pp. 141-156
    • Knipe, D.M.1    Lieberman, P.M.2    Jung, J.U.3    McBride, A.A.4
  • 41
    • 0025375785 scopus 로고
    • Structural requirements in the herpes simplex virus type 1 transactivator Vmw65 for interaction with the cellular octamer-binding protein and target TAATGARAT sequences
    • Greaves, R. F., O'Hare, P., Structural requirements in the herpes simplex virus type 1 transactivator Vmw65 for interaction with the cellular octamer-binding protein and target TAATGARAT sequences. J. Virol. 1990, 64, 2716-2724.
    • (1990) J. Virol. , vol.64 , pp. 2716-2724
    • Greaves, R.F.1    O'Hare, P.2
  • 42
    • 0033166256 scopus 로고    scopus 로고
    • Crystal structure of the conserved core of the herpes simplex virus transcriptional regulatory protein VP16
    • Liu, Y., Gong, W., Huang, C. C., Herr, W., Cheng, X., Crystal structure of the conserved core of the herpes simplex virus transcriptional regulatory protein VP16. Genes Dev. 1999, 13, 1692-1703.
    • (1999) Genes Dev. , vol.13 , pp. 1692-1703
    • Liu, Y.1    Gong, W.2    Huang, C.C.3    Herr, W.4    Cheng, X.5
  • 43
    • 0030756675 scopus 로고    scopus 로고
    • Induced alpha helix in the VP16 activation domain upon binding to a human TAF
    • Uesugi, M., Nyanguile, O., Lu, H., Levine, A. J., Verdine, G. L., Induced alpha helix in the VP16 activation domain upon binding to a human TAF. Science 1997, 277, 1310-1313.
    • (1997) Science , vol.277 , pp. 1310-1313
    • Uesugi, M.1    Nyanguile, O.2    Lu, H.3    Levine, A.J.4    Verdine, G.L.5
  • 44
    • 0028820136 scopus 로고
    • A class of activation domains interacts directly with TFIIA and stimulates TFIIA-TFIID-promoter complex assembly
    • Kobayashi, N., Boyer, T. G., Berk, A. J., A class of activation domains interacts directly with TFIIA and stimulates TFIIA-TFIID-promoter complex assembly. Mol. Cell. Biol. 1995, 15, 6465-6473.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6465-6473
    • Kobayashi, N.1    Boyer, T.G.2    Berk, A.J.3
  • 45
    • 0026076314 scopus 로고
    • Binding of general transcription factor TFIIB to an acidic activating region
    • Lin, Y. S., Ha, I., Maldonado, E., Reinberg, D., Green, M. R., Binding of general transcription factor TFIIB to an acidic activating region. Nature 1991, 353, 569-571.
    • (1991) Nature , vol.353 , pp. 569-571
    • Lin, Y.S.1    Ha, I.2    Maldonado, E.3    Reinberg, D.4    Green, M.R.5
  • 46
    • 0025345242 scopus 로고
    • Direct and selective binding of an acidic transcriptional activation domain to the TATA-box factor TFIID
    • Stringer, K. F., Ingles, C. J., Greenblatt, J., Direct and selective binding of an acidic transcriptional activation domain to the TATA-box factor TFIID. Nature 1990, 345, 783-786.
    • (1990) Nature , vol.345 , pp. 783-786
    • Stringer, K.F.1    Ingles, C.J.2    Greenblatt, J.3
  • 47
    • 0025731605 scopus 로고
    • Reduced binding of TFIID to transcriptionally compromised mutants of VP16
    • Ingles, C. J., Shales, M., Cress, W. D., Triezenberg, S. J., Greenblatt, J., Reduced binding of TFIID to transcriptionally compromised mutants of VP16. Nature 1991, 351, 588-590.
    • (1991) Nature , vol.351 , pp. 588-590
    • Ingles, C.J.1    Shales, M.2    Cress, W.D.3    Triezenberg, S.J.4    Greenblatt, J.5
  • 48
    • 0027983521 scopus 로고
    • Binding of basal transcription factor TFIIH to the acidic activation domains of VP16 and p53
    • Xiao, H., Pearson, A., Coulombe, B., Truant, R. et al., Binding of basal transcription factor TFIIH to the acidic activation domains of VP16 and p53. Mol. Cell. Biol. 1994, 14, 7013-7024.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7013-7024
    • Xiao, H.1    Pearson, A.2    Coulombe, B.3    Truant, R.4
  • 49
    • 0033105821 scopus 로고    scopus 로고
    • Identity between TRAP and SMCC complexes indicates novel pathways for the function of nuclear receptors and diverse mammalian activators
    • Ito, M., Yuan, C. X., Malik, S., Gu, W. et al., Identity between TRAP and SMCC complexes indicates novel pathways for the function of nuclear receptors and diverse mammalian activators. Mol. Cell. 1999, 3, 361-370.
    • (1999) Mol. Cell. , vol.3 , pp. 361-370
    • Ito, M.1    Yuan, C.X.2    Malik, S.3    Gu, W.4
  • 50
    • 0034459504 scopus 로고    scopus 로고
    • In vivo requirement of activator-specific binding targets of mediator
    • Park, J. M., Kim, H. S., Han, S. J., Hwang, M. S. et al., In vivo requirement of activator-specific binding targets of mediator. Mol. Cell. Biol. 2000, 20, 8709-8719.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8709-8719
    • Park, J.M.1    Kim, H.S.2    Han, S.J.3    Hwang, M.S.4
  • 51
    • 0346993714 scopus 로고    scopus 로고
    • A novel docking site on Mediator is critical for activation by VP16 in mammalian cells
    • Mittler, G., Stuhler, T., Santolin, L., Uhlmann, T. et al., A novel docking site on Mediator is critical for activation by VP16 in mammalian cells. EMBO J. 2003, 22, 6494-6504.
    • (2003) EMBO J. , vol.22 , pp. 6494-6504
    • Mittler, G.1    Stuhler, T.2    Santolin, L.3    Uhlmann, T.4
  • 52
    • 33744921070 scopus 로고    scopus 로고
    • Trimethylation of histone H3 lysine 4 by Set1 in the lytic infection of human herpes simplex virus 1
    • Huang, J., Kent, J. R., Placek, B., Whelan, K. A. et al., Trimethylation of histone H3 lysine 4 by Set1 in the lytic infection of human herpes simplex virus 1. J. Virol. 2006, 80, 5740-5746.
    • (2006) J. Virol. , vol.80 , pp. 5740-5746
    • Huang, J.1    Kent, J.R.2    Placek, B.3    Whelan, K.A.4
  • 53
    • 70449122130 scopus 로고    scopus 로고
    • Inhibition of the histone demethylase LSD1 blocks alpha-herpesvirus lytic replication and reactivation from latency
    • Liang, Y., Vogel, J. L., Narayanan, A., Peng, H., Kristie, T. M., Inhibition of the histone demethylase LSD1 blocks alpha-herpesvirus lytic replication and reactivation from latency. Nat. Med. 2009, 15, 1312-1317.
    • (2009) Nat. Med. , vol.15 , pp. 1312-1317
    • Liang, Y.1    Vogel, J.L.2    Narayanan, A.3    Peng, H.4    Kristie, T.M.5
  • 54
    • 84872330923 scopus 로고    scopus 로고
    • Targeting the JMJD2 histone demethylases to epigenetically control herpesvirus infection and reactivation from latency
    • 167ra165
    • Liang, Y., Vogel, J. L., Arbuckle, J. H., Rai, G. et al., Targeting the JMJD2 histone demethylases to epigenetically control herpesvirus infection and reactivation from latency. Sci. Transl. Med. 2013, 5, 167ra165.
    • (2013) Sci. Transl. Med. , vol.5
    • Liang, Y.1    Vogel, J.L.2    Arbuckle, J.H.3    Rai, G.4
  • 55
    • 59749104270 scopus 로고    scopus 로고
    • The histone variant H3.3 regulates gene expression during lytic infection with herpes simplex virus type 1
    • Placek, B. J., Huang, J., Kent, J. R., Dorsey, J. et al., The histone variant H3.3 regulates gene expression during lytic infection with herpes simplex virus type 1. J. Virol. 2009, 83, 1416-1421.
    • (2009) J. Virol. , vol.83 , pp. 1416-1421
    • Placek, B.J.1    Huang, J.2    Kent, J.R.3    Dorsey, J.4
  • 56
    • 77249148862 scopus 로고    scopus 로고
    • Transcriptional coactivator HCF-1 couples the histone chaperone Asf1b to HSV-1 DNA replication components
    • Peng, H., Nogueira, M. L., Vogel, J. L., Kristie, T. M., Transcriptional coactivator HCF-1 couples the histone chaperone Asf1b to HSV-1 DNA replication components. Proc. Natl. Acad. Sci. USA 2010, 107, 2461-2466.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 2461-2466
    • Peng, H.1    Nogueira, M.L.2    Vogel, J.L.3    Kristie, T.M.4
  • 57
    • 69249216590 scopus 로고    scopus 로고
    • Epigenetic modulation of gene expression from quiescent herpes simplex virus genomes
    • Ferenczy, M. W., DeLuca, N. A., Epigenetic modulation of gene expression from quiescent herpes simplex virus genomes. J. Virol. 2009, 83, 8514-8524.
    • (2009) J. Virol , vol.83 , pp. 8514-8524
    • Ferenczy, M.W.1    DeLuca, N.A.2
  • 58
    • 57349146688 scopus 로고    scopus 로고
    • Herpes simplex virus ICP0 promotes both histone removal and acetylation on viral DNA during lytic infection
    • Cliffe, A. R., Knipe, D. M., Herpes simplex virus ICP0 promotes both histone removal and acetylation on viral DNA during lytic infection. J. Virol. 2008, 82, 12030-12038.
    • (2008) J. Virol. , vol.82 , pp. 12030-12038
    • Cliffe, A.R.1    Knipe, D.M.2
  • 59
    • 0034469709 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 ICP4 promotes transcription preinitiation complex formation by enhancing the binding of TFIID to DNA
    • Grondin, B., DeLuca, N., Herpes simplex virus type 1 ICP4 promotes transcription preinitiation complex formation by enhancing the binding of TFIID to DNA. J. Virol. 2000, 74, 11504-11510.
    • (2000) J. Virol. , vol.74 , pp. 11504-11510
    • Grondin, B.1    DeLuca, N.2
  • 60
    • 0028096996 scopus 로고
    • Requirements for activation of the herpes simplex virus glycoprotein C promoter in vitro by the viral regulatory protein ICP4
    • Gu, B., DeLuca, N., Requirements for activation of the herpes simplex virus glycoprotein C promoter in vitro by the viral regulatory protein ICP4. J. Virol. 1994, 68, 7953-7965.
    • (1994) J. Virol. , vol.68 , pp. 7953-7965
    • Gu, B.1    DeLuca, N.2
  • 61
    • 0345662686 scopus 로고
    • Transcriptional control of herpesvirus gene expression: gene functions required for positive and negative regulation
    • Godowski, P. J., Knipe, D. M., Transcriptional control of herpesvirus gene expression: gene functions required for positive and negative regulation. Proc. Natl. Acad. Sci. USA 1986, 83, 256-260.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 256-260
    • Godowski, P.J.1    Knipe, D.M.2
  • 62
    • 0022457155 scopus 로고
    • Herpes simplex virus immediate early infected-cell polypeptide 4 binds to DNA and promotes transcription
    • Beard, P., Faber, S., Wilcox, K. W., Pizer, L. I., Herpes simplex virus immediate early infected-cell polypeptide 4 binds to DNA and promotes transcription. Proc. Natl. Acad. Sci. USA 1986, 83, 4016-4020.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 4016-4020
    • Beard, P.1    Faber, S.2    Wilcox, K.W.3    Pizer, L.I.4
  • 63
    • 0018634067 scopus 로고
    • Abnormal properties of an immediate early polypeptide in cells infected with the herpes simplex virus type 1 mutant tsK
    • Preston, C. M., Abnormal properties of an immediate early polypeptide in cells infected with the herpes simplex virus type 1 mutant tsK. J. Virol. 1979, 32, 357-369.
    • (1979) J. Virol. , vol.32 , pp. 357-369
    • Preston, C.M.1
  • 64
    • 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
  • 65
    • 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
  • 66
    • 0037315911 scopus 로고    scopus 로고
    • Signal-induced transcriptional activation by Dif requires the dTRAP80 mediator module
    • Park, J. M., Kim, J. M., Kim, L. K., Kim, S. N. et al., Signal-induced transcriptional activation by Dif requires the dTRAP80 mediator module. Mol. Cell. Biol. 2003, 23, 1358-1367.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 1358-1367
    • Park, J.M.1    Kim, J.M.2    Kim, L.K.3    Kim, S.N.4
  • 67
    • 1442354965 scopus 로고    scopus 로고
    • The activator-recruited cofactor/mediator coactivator subunit ARC92 is a functionally important target of the VP16 transcriptional activator
    • Yang, F., DeBeaumont, R., Zhou, S., Naar, A. M., The activator-recruited cofactor/mediator coactivator subunit ARC92 is a functionally important target of the VP16 transcriptional activator. Proc. Natl. Acad. Sci. USA 2004, 101, 2339-2344.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2339-2344
    • Yang, F.1    DeBeaumont, R.2    Zhou, S.3    Naar, A.M.4
  • 68
    • 84862655632 scopus 로고    scopus 로고
    • Resolving protein interactions and complexes by affinity purification followed by label-based quantitative mass spectrometry
    • Trinkle-Mulcahy, L., Resolving protein interactions and complexes by affinity purification followed by label-based quantitative mass spectrometry. Proteomics 2012, 12, 1623-1638.
    • (2012) Proteomics , vol.12 , pp. 1623-1638
    • Trinkle-Mulcahy, L.1
  • 69
    • 84872524590 scopus 로고    scopus 로고
    • Proteomics-based methods for discovery, quantification, and validation of protein-protein interactions
    • Miteva, Y. V., Budayeva, H. G., Cristea, I. M., Proteomics-based methods for discovery, quantification, and validation of protein-protein interactions. Anal. Chem. 2013, 85, 749-768.
    • (2013) Anal. Chem. , vol.85 , pp. 749-768
    • Miteva, Y.V.1    Budayeva, H.G.2    Cristea, I.M.3
  • 70
    • 77951790602 scopus 로고    scopus 로고
    • A targeted spatial-temporal proteomics approach implicates multiple cellular trafficking pathways in human cytomegalovirus virion maturation
    • Moorman, N. J., Sharon-Friling, R., Shenk, T., Cristea, I. M., A targeted spatial-temporal proteomics approach implicates multiple cellular trafficking pathways in human cytomegalovirus virion maturation. Mol. Cell. Proteomics 2010, 9, 851-860.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 851-860
    • Moorman, N.J.1    Sharon-Friling, R.2    Shenk, T.3    Cristea, I.M.4
  • 71
    • 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., Cristea, I. M., 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    Cristea, I.M.5
  • 72
    • 84910613036 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of host-virus interactions reveals a role for Golgi brefeldin A resistance factor 1 (GBF1) in dengue infection
    • Carpp, L. N., Rogers, R. S., Moritz, R. L., Aitchison, J. D., Quantitative proteomic analysis of host-virus interactions reveals a role for Golgi brefeldin A resistance factor 1 (GBF1) in dengue infection. Mol. Cell. Proteomics 2014, 13, 2836-2854.
    • (2014) Mol. Cell. Proteomics , vol.13 , pp. 2836-2854
    • Carpp, L.N.1    Rogers, R.S.2    Moritz, R.L.3    Aitchison, J.D.4
  • 73
    • 31944439843 scopus 로고    scopus 로고
    • Phosphorylation of the VP16 transcriptional activator protein during herpes simplex virus infection and mutational analysis of putative phosphorylation sites
    • Ottosen, S., Herrera, F. J., Doroghazi, J. R., Hull, A. et al., Phosphorylation of the VP16 transcriptional activator protein during herpes simplex virus infection and mutational analysis of putative phosphorylation sites. Virology 2006, 345, 468-481.
    • (2006) Virology , vol.345 , pp. 468-481
    • Ottosen, S.1    Herrera, F.J.2    Doroghazi, J.R.3    Hull, A.4
  • 74
    • 17044458937 scopus 로고    scopus 로고
    • Compartmentalization of VP16 in cells infected with recombinant herpes simplex virus expressing VP16-green fluorescent protein fusion proteins
    • LaBoissiere, S., Izeta, A., Malcomber, S., O'Hare, P., Compartmentalization of VP16 in cells infected with recombinant herpes simplex virus expressing VP16-green fluorescent protein fusion proteins. J. Virol. 2004, 78, 8002-8014.
    • (2004) J. Virol. , vol.78 , pp. 8002-8014
    • La Boissiere, S.1    Izeta, A.2    Malcomber, S.3    O'Hare, P.4
  • 75
    • 0014899508 scopus 로고
    • Temperature-sensitive mutants of herpes simplex virus
    • Schaffer, P., Vonka, V., Lewis, R., Benyesh-Melnick, M., Temperature-sensitive mutants of herpes simplex virus. Virology 1970, 42, 1144-1146.
    • (1970) Virology , vol.42 , pp. 1144-1146
    • Schaffer, P.1    Vonka, V.2    Lewis, R.3    Benyesh-Melnick, M.4
  • 76
    • 0019789105 scopus 로고
    • Monoclonal antibodies to herpes simplex virus type 1 proteins, including the immediate-early protein ICP 4
    • Showalter, S. D., Zweig, M., Hampar, B., Monoclonal antibodies to herpes simplex virus type 1 proteins, including the immediate-early protein ICP 4. Infect. Immun. 1981, 34, 684-692.
    • (1981) Infect. Immun. , vol.34 , pp. 684-692
    • Showalter, S.D.1    Zweig, M.2    Hampar, B.3
  • 77
    • 0022751326 scopus 로고
    • A mutant herpesvirus protein leads to a block in nuclear localization of other viral proteins
    • Knipe, D. M., Smith, J. L., A mutant herpesvirus protein leads to a block in nuclear localization of other viral proteins. Mol. Cell. Biol. 1986, 6, 2371-2381.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 2371-2381
    • Knipe, D.M.1    Smith, J.L.2
  • 78
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O., Mann, M., Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem. 1996, 68, 850-858.
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 79
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng, J. K., McCormack, A. L., Yates, J. R., An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J Am. Soc. Mass Spectrom. 1994, 5, 976-989.
    • (1994) J Am. Soc. Mass Spectrom. , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates, J.R.3
  • 80
    • 0242490780 scopus 로고    scopus 로고
    • Cytoscape: a software environment for integrated models of biomolecular interaction networks
    • Shannon, P., Markiel, A., Ozier, O., Baliga, N. S. et al., Cytoscape: a software environment for integrated models of biomolecular interaction networks. Genome Res. 2003, 13, 2498-2504.
    • (2003) Genome Res. , vol.13 , pp. 2498-2504
    • Shannon, P.1    Markiel, A.2    Ozier, O.3    Baliga, N.S.4
  • 81
    • 64549104807 scopus 로고    scopus 로고
    • ClueGO: a Cytoscape plug-in to decipher functionally grouped gene ontology and pathway annotation networks
    • Bindea, G., Mlecnik, B., Hackl, H., Charoentong, P. et al., ClueGO: a Cytoscape plug-in to decipher functionally grouped gene ontology and pathway annotation networks. Bioinformatics 2009, 25, 1091-1093.
    • (2009) Bioinformatics , vol.25 , pp. 1091-1093
    • Bindea, G.1    Mlecnik, B.2    Hackl, H.3    Charoentong, P.4
  • 82
    • 84903365434 scopus 로고    scopus 로고
    • A targeted RNA interference screen reveals novel epigenetic factors that regulate herpesviral gene expression
    • Oh, H. S., Bryant, K. F., Nieland, T. J., Mazumder, A. et al., A targeted RNA interference screen reveals novel epigenetic factors that regulate herpesviral gene expression. MBio 2014, 5, e01086-e01013.
    • (2014) MBio , vol.5 , pp. e01013-e01086
    • Oh, H.S.1    Bryant, K.F.2    Nieland, T.J.3    Mazumder, A.4
  • 83
    • 84857844970 scopus 로고    scopus 로고
    • Roles of the nuclear lamina in stable nuclear association and assembly of a herpesviral transactivator complex on viral immediate-early genes
    • Silva, L., Oh, H. S., Chang, L., Yan, Z. et al., Roles of the nuclear lamina in stable nuclear association and assembly of a herpesviral transactivator complex on viral immediate-early genes. MBio 2012, 3, e00300-e00311.
    • (2012) MBio , vol.3 , pp. e00300-e00311
    • Silva, L.1    Oh, H.S.2    Chang, L.3    Yan, Z.4
  • 84
    • 0025668617 scopus 로고
    • Interactions of the Oct-1 POU subdomains with specific DNA sequences and with the HSV alpha-trans-activator protein
    • Kristie, T. M., Sharp, P. A., Interactions of the Oct-1 POU subdomains with specific DNA sequences and with the HSV alpha-trans-activator protein. Genes Dev. 1990, 4, 2383-2396.
    • (1990) Genes Dev. , vol.4 , pp. 2383-2396
    • Kristie, T.M.1    Sharp, P.A.2
  • 85
    • 10744232895 scopus 로고    scopus 로고
    • A mammalian mediator subunit that shares properties with Saccharomyces cerevisiae mediator subunit Cse2
    • Tomomori-Sato, C., Sato, S., Parmely, T. J., Banks, C. A. et al., A mammalian mediator subunit that shares properties with Saccharomyces cerevisiae mediator subunit Cse2. J. Biol. Chem. 2004, 279, 5846-5851.
    • (2004) J. Biol. Chem. , vol.279 , pp. 5846-5851
    • Tomomori-Sato, C.1    Sato, S.2    Parmely, T.J.3    Banks, C.A.4
  • 86
    • 0040368298 scopus 로고    scopus 로고
    • Composite co-activator ARC mediates chromatin-directed transcriptional activation
    • Naar, A. M., Beaurang, P. A., Zhou, S., Abraham, S. et al., Composite co-activator ARC mediates chromatin-directed transcriptional activation. Nature 1999, 398, 828-832.
    • (1999) Nature , vol.398 , pp. 828-832
    • Naar, A.M.1    Beaurang, P.A.2    Zhou, S.3    Abraham, S.4
  • 87
    • 0033587187 scopus 로고    scopus 로고
    • Mammalian Srb/Mediator complex is targeted by adenovirus E1A protein
    • Boyer, T. G., Martin, M. E., Lees, E., Ricciardi, R. P., Berk, A. J., Mammalian Srb/Mediator complex is targeted by adenovirus E1A protein. Nature 1999, 399, 276-279.
    • (1999) Nature , vol.399 , pp. 276-279
    • Boyer, T.G.1    Martin, M.E.2    Lees, E.3    Ricciardi, R.P.4    Berk, A.J.5
  • 88
    • 34047243849 scopus 로고    scopus 로고
    • The VP16 activation domain establishes an active mediator lacking CDK8 in vivo
    • Uhlmann, T., Boeing, S., Lehmbacher, M., Meisterernst, M., The VP16 activation domain establishes an active mediator lacking CDK8 in vivo. J. Biol. Chem. 2007, 282, 2163-2173.
    • (2007) J. Biol. Chem. , vol.282 , pp. 2163-2173
    • Uhlmann, T.1    Boeing, S.2    Lehmbacher, M.3    Meisterernst, M.4
  • 89
    • 0347379968 scopus 로고    scopus 로고
    • A mammalian homolog of Drosophila melanogaster transcriptional coactivator intersex is a subunit of the mammalian mediator complex
    • Sato, S., Tomomori-Sato, C., Banks, C. A., Parmely, T. J. et al., A mammalian homolog of Drosophila melanogaster transcriptional coactivator intersex is a subunit of the mammalian mediator complex. J. Biol. Chem. 2003, 278, 49671-49674.
    • (2003) J. Biol. Chem. , vol.278 , pp. 49671-49674
    • Sato, S.1    Tomomori-Sato, C.2    Banks, C.A.3    Parmely, T.J.4
  • 90
    • 79952606829 scopus 로고    scopus 로고
    • Crosstalk between O-GlcNAcylation and proteolytic cleavage regulates the host cell factor-1 maturation pathway
    • Daou, S., Mashtalir, N., Hammond-Martel, I., Pak, H. et al., Crosstalk between O-GlcNAcylation and proteolytic cleavage regulates the host cell factor-1 maturation pathway. Proc. Natl. Acad. Sci. USA 2011, 108, 2747-2752.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 2747-2752
    • Daou, S.1    Mashtalir, N.2    Hammond-Martel, I.3    Pak, H.4
  • 91
    • 22544438727 scopus 로고    scopus 로고
    • Determination of interactions between tegument proteins of herpes simplex virus type 1
    • Vittone, V., Diefenbach, E., Triffett, D., Douglas, M. W. et al., Determination of interactions between tegument proteins of herpes simplex virus type 1. J. Virol. 2005, 79, 9566-9571.
    • (2005) J. Virol. , vol.79 , pp. 9566-9571
    • Vittone, V.1    Diefenbach, E.2    Triffett, D.3    Douglas, M.W.4
  • 92
    • 0028289280 scopus 로고
    • Herpes simplex virus VP16 forms a complex with the virion host shutoff protein vhs
    • Smibert, C. A., Popova, B., Xiao, P., Capone, J. P., Smiley, J. R., Herpes simplex virus VP16 forms a complex with the virion host shutoff protein vhs. J. Virol. 1994, 68, 2339-2346.
    • (1994) J. Virol. , vol.68 , pp. 2339-2346
    • Smibert, C.A.1    Popova, B.2    Xiao, P.3    Capone, J.P.4    Smiley, J.R.5
  • 93
    • 0028849796 scopus 로고
    • VP16 interacts via its activation domain with VP22, a tegument protein of herpes simplex virus, and is relocated to a novel macromolecular assembly in coexpressing cells
    • Elliott, G., Mouzakitis, G., O'Hare, P., VP16 interacts via its activation domain with VP22, a tegument protein of herpes simplex virus, and is relocated to a novel macromolecular assembly in coexpressing cells. J. Virol. 1995, 69, 7932-7941.
    • (1995) J. Virol. , vol.69 , pp. 7932-7941
    • Elliott, G.1    Mouzakitis, G.2    O'Hare, P.3
  • 94
    • 0346367068 scopus 로고    scopus 로고
    • The cytoplasmic tail of Herpes simplex virus glycoprotein H binds to the tegument protein VP16 in vitro and in vivo
    • Gross, S. T., Harley, C. A., Wilson, D. W., The cytoplasmic tail of Herpes simplex virus glycoprotein H binds to the tegument protein VP16 in vitro and in vivo. Virology 2003, 317, 1-12.
    • (2003) Virology , vol.317 , pp. 1-12
    • Gross, S.T.1    Harley, C.A.2    Wilson, D.W.3
  • 95
    • 84869237367 scopus 로고    scopus 로고
    • A network of protein interactions around the herpes simplex virus tegument protein VP22
    • Maringer, K., Stylianou, J., Elliott, G., A network of protein interactions around the herpes simplex virus tegument protein VP22. J. Virol. 2012, 86, 12971-12982.
    • (2012) J. Virol. , vol.86 , pp. 12971-12982
    • Maringer, K.1    Stylianou, J.2    Elliott, G.3
  • 96
    • 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
  • 97
    • 0021966699 scopus 로고
    • Stimulation of expression of a herpes simplex virus DNA-binding protein by two viral functions
    • Quinlan, M. P., Knipe, D. M., Stimulation of expression of a herpes simplex virus DNA-binding protein by two viral functions. Mol. Cell. Biol. 1985, 5, 957-963.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 957-963
    • Quinlan, M.P.1    Knipe, D.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.