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Volumn 15, Issue 12, 2015, Pages 2006-2022

Human cytomegalovirus pUL97 kinase induces global changes in the infected cell phosphoproteome

Author keywords

Cell biology; Herpesvirus; Human cytomegalovirus; Nuclear pore complex; TREX complex; Viral kinase

Indexed keywords

CELL DNA; HISTONE DEACETYLASE 1; PHOSPHOPEPTIDE; PHOSPHOPROTEOME; PROTEIN SERINE THREONINE KINASE; PROTEOME; PUL97 KINASE; RNA POLYMERASE II; UNCLASSIFIED DRUG; VIRUS ENZYME; GANCICLOVIR KINASE; PHOSPHOPROTEIN; PHOSPHOTRANSFERASE;

EID: 84931003658     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201400607     Document Type: Article
Times cited : (35)

References (90)
  • 1
    • 34548158284 scopus 로고    scopus 로고
    • Cytomegaloviruses
    • Knipe, D. M., Howley, P. M. (Eds.), Lippincott Williams and Wilkins, Philadelphia -
    • Mocarski, E. S., Shenk, T., Pass, R. F., Cytomegaloviruses, in: Knipe, D. M., Howley, P. M. (Eds.), Fields Virology, Lippincott Williams and Wilkins, Philadelphia 2007, pp. 2701-2772.
    • (2007) Fields Virology , pp. 2701-2772
    • Mocarski, E.S.1    Shenk, T.2    Pass, R.F.3
  • 2
    • 0023335127 scopus 로고
    • Alteration of protein phosphorylation patterns in cell lines morphologically transformed by human cytomegalovirus
    • Muganda-Ojiaku, P. M., Huang, E. S., Alteration of protein phosphorylation patterns in cell lines morphologically transformed by human cytomegalovirus. Cancer Biochem. Biophys. 1987, 9, 179-189.
    • (1987) Cancer Biochem. Biophys. , vol.9 , pp. 179-189
    • Muganda-Ojiaku, P.M.1    Huang, E.S.2
  • 3
    • 0037008483 scopus 로고    scopus 로고
    • Cytomegalovirus recruitment of cellular kinases to dissolve the nuclear lamina
    • Muranyi, W., Haas, J., Wagner, M., Krohne, G., Koszinowski, U. H., Cytomegalovirus recruitment of cellular kinases to dissolve the nuclear lamina. Science 2002, 297, 854-857.
    • (2002) Science , vol.297 , pp. 854-857
    • Muranyi, W.1    Haas, J.2    Wagner, M.3    Krohne, G.4    Koszinowski, U.H.5
  • 4
    • 0035159733 scopus 로고    scopus 로고
    • Modulation of human cytomegalovirus immediate-early gene enhancer by mitogen-activated protein kinase kinase kinase-1
    • Sun, B., Harrowe, G., Reinhard, C., Yoshihara, C. et al., Modulation of human cytomegalovirus immediate-early gene enhancer by mitogen-activated protein kinase kinase kinase-1. J. Cell. Biochem. 2001, 83, 563-573.
    • (2001) J. Cell. Biochem. , vol.83 , pp. 563-573
    • Sun, B.1    Harrowe, G.2    Reinhard, C.3    Yoshihara, C.4
  • 5
    • 35048861785 scopus 로고    scopus 로고
    • Cytomegaloviral proteins pUL50 and pUL53 are associated with the nuclear lamina and interact with cellular protein kinase C
    • Milbradt, J., Auerochs, S., Marschall, M., Cytomegaloviral proteins pUL50 and pUL53 are associated with the nuclear lamina and interact with cellular protein kinase C. J. Gen. Virol. 2007, 88, 2642-2650.
    • (2007) J. Gen. Virol. , vol.88 , pp. 2642-2650
    • Milbradt, J.1    Auerochs, S.2    Marschall, M.3
  • 6
    • 0033977267 scopus 로고    scopus 로고
    • Activation of the mitogen-activated protein kinase p38 by human cytomegalovirus infection through two distinct pathways: a novel mechanism for activation of p38
    • Johnson, R. A., Huong, S. M., Huang, E. S., Activation of the mitogen-activated protein kinase p38 by human cytomegalovirus infection through two distinct pathways: a novel mechanism for activation of p38. J. Virol. 2000, 74, 1158-1167.
    • (2000) J. Virol. , vol.74 , pp. 1158-1167
    • Johnson, R.A.1    Huong, S.M.2    Huang, E.S.3
  • 7
    • 0035112558 scopus 로고    scopus 로고
    • The role of MKK1/2 kinase activity in human cytomegalovirus infection
    • Johnson, R. A., Ma, X. L., Yurochko, A. D., Huang, E. S., The role of MKK1/2 kinase activity in human cytomegalovirus infection. J. Gen. Virol. 2001, 82, 493-497.
    • (2001) J. Gen. Virol. , vol.82 , pp. 493-497
    • Johnson, R.A.1    Ma, X.L.2    Yurochko, A.D.3    Huang, E.S.4
  • 8
    • 0034973856 scopus 로고    scopus 로고
    • Human cytomegalovirus up-regulates the phosphatidylinositol 3-kinase (PI3-K) pathway: inhibition of PI3-K activity inhibits viral replication and virus-induced signaling
    • Johnson, R. A., Wang, X., Ma, X. L., Huong, S. M., Huang, E. S., Human cytomegalovirus up-regulates the phosphatidylinositol 3-kinase (PI3-K) pathway: inhibition of PI3-K activity inhibits viral replication and virus-induced signaling. J. Virol. 2001, 75, 6022-6032.
    • (2001) J. Virol. , vol.75 , pp. 6022-6032
    • Johnson, R.A.1    Wang, X.2    Ma, X.L.3    Huong, S.M.4    Huang, E.S.5
  • 9
    • 33846597192 scopus 로고    scopus 로고
    • Viral and cell cycle-regulated kinases in cytomegalovirus-induced pseudomitosis and replication
    • Hertel, L., Chou, S., Mocarski, E. S., Viral and cell cycle-regulated kinases in cytomegalovirus-induced pseudomitosis and replication. PLoS Pathog. 2007, 3, e6.
    • (2007) PLoS Pathog. , vol.3 , pp. e6
    • Hertel, L.1    Chou, S.2    Mocarski, E.S.3
  • 10
    • 0036233141 scopus 로고    scopus 로고
    • Role of regulatory elements and the MAPK/ERK or p38 MAPK pathways for activation of human cytomegalovirus gene expression
    • Chen, J., Stinski, M. F., Role of regulatory elements and the MAPK/ERK or p38 MAPK pathways for activation of human cytomegalovirus gene expression. J. Virol. 2002, 76, 4873-4885.
    • (2002) J. Virol. , vol.76 , pp. 4873-4885
    • Chen, J.1    Stinski, M.F.2
  • 11
    • 84857428182 scopus 로고    scopus 로고
    • Human kinome profiling identifies a requirement for AMP-activated protein kinase during human cytomegalovirus infection
    • Terry, L. J., Vastag, L., Rabinowitz, J. D., Shenk, T., Human kinome profiling identifies a requirement for AMP-activated protein kinase during human cytomegalovirus infection. Proc. Natl. Acad. Sci. USA 2012, 109, 3071-3076.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 3071-3076
    • Terry, L.J.1    Vastag, L.2    Rabinowitz, J.D.3    Shenk, T.4
  • 12
    • 77951480815 scopus 로고    scopus 로고
    • Rapamycin-resistant mTORC1 kinase activity is required for herpesvirus replication
    • Moorman, N. J., Shenk, T., Rapamycin-resistant mTORC1 kinase activity is required for herpesvirus replication. J. Virol. 2010, 84, 5260-5269.
    • (2010) J. Virol. , vol.84 , pp. 5260-5269
    • Moorman, N.J.1    Shenk, T.2
  • 13
    • 47649088674 scopus 로고    scopus 로고
    • Cytomegalovirus UL97 mutations in the era of ganciclovir and maribavir
    • Chou, S., Cytomegalovirus UL97 mutations in the era of ganciclovir and maribavir. Rev. Med. Virol. 2008, 18, 233-246.
    • (2008) Rev. Med. Virol. , vol.18 , pp. 233-246
    • Chou, S.1
  • 14
    • 0037225808 scopus 로고    scopus 로고
    • The human cytomegalovirus UL97 protein kinase, an antiviral drug target, is required at the stage of nuclear egress
    • Krosky, P. M., Baek, M.-C., Coen, D. M., The human cytomegalovirus UL97 protein kinase, an antiviral drug target, is required at the stage of nuclear egress. J. Virol. 2003, 77, 905-914.
    • (2003) J. Virol. , vol.77 , pp. 905-914
    • Krosky, P.M.1    Baek, M.-C.2    Coen, D.M.3
  • 15
    • 59249092261 scopus 로고    scopus 로고
    • Viral mimicry of Cdc2/cyclin-dependent kinase 1 mediates disruption of nuclear lamina during human cytomegalovirus nuclear egress
    • Hamirally, S., Kamil, J. P., Ndassa-Colday, Y. M., Lin, A. J. et al., Viral mimicry of Cdc2/cyclin-dependent kinase 1 mediates disruption of nuclear lamina during human cytomegalovirus nuclear egress. PLoS Pathog. 2009, 5, e1000275.
    • (2009) PLoS Pathog. , vol.5 , pp. e1000275
    • Hamirally, S.1    Kamil, J.P.2    Ndassa-Colday, Y.M.3    Lin, A.J.4
  • 16
    • 44049107548 scopus 로고    scopus 로고
    • Phosphorylation of retinoblastoma protein by viral protein with cyclin-dependent kinase function
    • Hume, A. J., Finkel, J. S., Kamil, J. P., Coen, D. M. et al., Phosphorylation of retinoblastoma protein by viral protein with cyclin-dependent kinase function. Science 2008, 320, 797-799.
    • (2008) Science , vol.320 , pp. 797-799
    • Hume, A.J.1    Finkel, J.S.2    Kamil, J.P.3    Coen, D.M.4
  • 17
    • 43249118969 scopus 로고    scopus 로고
    • Human cytomegalovirus UL97 kinase activity is required for the hyperphosphorylation of retinoblastoma protein and inhibits the formation of nuclear aggresomes
    • Prichard, M. N., Sztul, E., Daily, S. L., Perry, A. L. et al., Human cytomegalovirus UL97 kinase activity is required for the hyperphosphorylation of retinoblastoma protein and inhibits the formation of nuclear aggresomes. J. Virol. 2008, 82, 5054-5067.
    • (2008) J. Virol. , vol.82 , pp. 5054-5067
    • Prichard, M.N.1    Sztul, E.2    Daily, S.L.3    Perry, A.L.4
  • 18
    • 0032954616 scopus 로고    scopus 로고
    • Cellular elongation factor 1delta is modified in cells infected with representative alpha-, beta-, or gammaherpesviruses
    • Kawaguchi, Y., Matsumura, T., Roizman, B., Hirai, K., Cellular elongation factor 1delta is modified in cells infected with representative alpha-, beta-, or gammaherpesviruses. J. Virol. 1999, 73, 4456-4460.
    • (1999) J. Virol. , vol.73 , pp. 4456-4460
    • Kawaguchi, Y.1    Matsumura, T.2    Roizman, B.3    Hirai, K.4
  • 19
    • 2942585139 scopus 로고    scopus 로고
    • Phosphorylation of the RNA polymerase II carboxyl-terminal domain in human cytomegalovirus-infected cells and in vitro by the viral UL97 protein kinase
    • Baek, M.-C., Krosky, P. M., Pearson, A., Coen, D. M., Phosphorylation of the RNA polymerase II carboxyl-terminal domain in human cytomegalovirus-infected cells and in vitro by the viral UL97 protein kinase. Virology 2004, 324, 184-193.
    • (2004) Virology , vol.324 , pp. 184-193
    • Baek, M.-C.1    Krosky, P.M.2    Pearson, A.3    Coen, D.M.4
  • 20
    • 0030955930 scopus 로고    scopus 로고
    • The human cytomegalovirus UL97 protein is phosphorylated and a component of virions
    • van Zeijl, M., Fairhurst, J., Baum, E. Z., Sun, L., Jones, T. R., The human cytomegalovirus UL97 protein is phosphorylated and a component of virions. Virology 1997, 231, 72-80.
    • (1997) Virology , vol.231 , pp. 72-80
    • van Zeijl, M.1    Fairhurst, J.2    Baum, E.Z.3    Sun, L.4    Jones, T.R.5
  • 21
    • 34648830842 scopus 로고    scopus 로고
    • Human cytomegalovirus protein kinase UL97 forms a complex with the tegument phosphoprotein pp65
    • Kamil, J. P., Coen, D. M., Human cytomegalovirus protein kinase UL97 forms a complex with the tegument phosphoprotein pp65. J. Virol. 2007, 81, 10659-10668.
    • (2007) J. Virol. , vol.81 , pp. 10659-10668
    • Kamil, J.P.1    Coen, D.M.2
  • 22
    • 0033033631 scopus 로고    scopus 로고
    • A recombinant human cytomegalovirus with a large deletion in UL97 has a severe replication deficiency
    • Prichard, M. N., Gao, N., Jairath, S., Mulamba, G. et al., A recombinant human cytomegalovirus with a large deletion in UL97 has a severe replication deficiency. J. Virol. 1999, 73, 5663-5670.
    • (1999) J. Virol. , vol.73 , pp. 5663-5670
    • Prichard, M.N.1    Gao, N.2    Jairath, S.3    Mulamba, G.4
  • 23
    • 0142091343 scopus 로고    scopus 로고
    • Functional map of human cytomegalovirus AD169 defined by global mutational analysis
    • Yu, D., Silva, M. C., Shenk, T., Functional map of human cytomegalovirus AD169 defined by global mutational analysis. Proc. Natl. Acad. Sci. USA 2003, 100, 12396-12401.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12396-12401
    • Yu, D.1    Silva, M.C.2    Shenk, T.3
  • 24
    • 0037119463 scopus 로고    scopus 로고
    • Specific phosphorylation of exogenous protein and peptide substrates by the human cytomegalovirus UL97 protein kinase
    • Baek, M.-C., Krosky, P. M., He, Z., Coen, D. M., Specific phosphorylation of exogenous protein and peptide substrates by the human cytomegalovirus UL97 protein kinase. Importance of the P+5 position. J. Biol. Chem. 2002, 277, 29593-29599.
    • (2002) Importance of the P+5 position. J. Biol. Chem. , vol.277 , pp. 29593-29599
    • Baek, M.-C.1    Krosky, P.M.2    He, Z.3    Coen, D.M.4
  • 25
    • 0038082392 scopus 로고    scopus 로고
    • The human cytomegalovirus UL44 protein is a substrate for the UL97 protein kinase
    • Krosky, P. M., Baek, M.-C., Jahng, W. J., Barrera, I. et al., The human cytomegalovirus UL44 protein is a substrate for the UL97 protein kinase. J. Virol. 2003, 77, 7720-7727.
    • (2003) J. Virol. , vol.77 , pp. 7720-7727
    • Krosky, P.M.1    Baek, M.-C.2    Jahng, W.J.3    Barrera, I.4
  • 26
    • 0031060542 scopus 로고    scopus 로고
    • The human cytomegalovirus UL97 protein is a protein kinase that autophosphorylates on serines and threonines
    • He, Z., He, Y. S., Kim, Y., Chu, L. et al., The human cytomegalovirus UL97 protein is a protein kinase that autophosphorylates on serines and threonines. J. Virol. 1997, 71, 405-411.
    • (1997) J. Virol. , vol.71 , pp. 405-411
    • He, Z.1    He, Y.S.2    Kim, Y.3    Chu, L.4
  • 27
    • 0037708793 scopus 로고    scopus 로고
    • The protein kinase pUL97 of human cytomegalovirus interacts with and phosphorylates the DNA polymerase processivity factor pUL44
    • Marschall, M., Freitag, M., Suchy, P., Romaker, D. et al., The protein kinase pUL97 of human cytomegalovirus interacts with and phosphorylates the DNA polymerase processivity factor pUL44. Virology 2003, 311, 60-71.
    • (2003) Virology , vol.311 , pp. 60-71
    • Marschall, M.1    Freitag, M.2    Suchy, P.3    Romaker, D.4
  • 28
    • 63449097589 scopus 로고    scopus 로고
    • Cytomegaloviral protein kinase pUL97 interacts with the nuclear mRNA export factor pUL69 to modulate its intranuclear localization and activity
    • Thomas, M., Rechter, S., Milbradt, J., Auerochs, S. et al., Cytomegaloviral protein kinase pUL97 interacts with the nuclear mRNA export factor pUL69 to modulate its intranuclear localization and activity. J. Gen. Virol. 2009, 90, 567-578.
    • (2009) J. Gen. Virol. , vol.90 , pp. 567-578
    • Thomas, M.1    Rechter, S.2    Milbradt, J.3    Auerochs, S.4
  • 29
    • 80054896036 scopus 로고    scopus 로고
    • Conserved herpesvirus kinases target the DNA damage response pathway and TIP60 histone acetyltransferase to promote virus replication
    • Li, R., Zhu, J., Xie, Z., Liao, G. et al., Conserved herpesvirus kinases target the DNA damage response pathway and TIP60 histone acetyltransferase to promote virus replication. Cell Host Microbe 2011, 10, 390-400.
    • (2011) Cell Host Microbe , vol.10 , pp. 390-400
    • Li, R.1    Zhu, J.2    Xie, Z.3    Liao, G.4
  • 30
    • 34247396011 scopus 로고    scopus 로고
    • A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC)
    • Ong, S.-E., Mann, M., A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC). Nat. Protoc. 2006, 1, 2650-2660.
    • (2006) Nat. Protoc. , vol.1 , pp. 2650-2660
    • Ong, S.-E.1    Mann, M.2
  • 31
    • 67349266694 scopus 로고    scopus 로고
    • Universal sample preparation method for proteome analysis
    • Wisniewski, J. R., Zougman, A., Nagaraj, N., Mann, M., Universal sample preparation method for proteome analysis. Nat. Methods 2009, 6, 359-362.
    • (2009) Nat. Methods , vol.6 , pp. 359-362
    • Wisniewski, J.R.1    Zougman, A.2    Nagaraj, N.3    Mann, M.4
  • 32
    • 0037317228 scopus 로고    scopus 로고
    • Stop and go extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics
    • Rappsilber, J., Ishihama, Y., Mann, M., Stop and go extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics. Anal. Chem. 2003, 75, 663-670.
    • (2003) Anal. Chem. , vol.75 , pp. 663-670
    • Rappsilber, J.1    Ishihama, Y.2    Mann, M.3
  • 33
    • 84892720954 scopus 로고    scopus 로고
    • Phosphopeptide enrichment using offline titanium dioxide columns for phosphoproteomics
    • Yu, L. R., Veenstra, T., Phosphopeptide enrichment using offline titanium dioxide columns for phosphoproteomics. Methods Mol. Biol. 2013, 1002, 93-103.
    • (2013) Methods Mol. Biol. , vol.1002 , pp. 93-103
    • Yu, L.R.1    Veenstra, T.2
  • 34
    • 35748972060 scopus 로고    scopus 로고
    • Semi-supervised learning for peptide identification from shotgun proteomics datasets
    • Kall, L., Canterbury, J. D., Weston, J., Noble, W. S., MacCoss, M. J., Semi-supervised learning for peptide identification from shotgun proteomics datasets. Nat. Methods 2007, 4, 923-925.
    • (2007) Nat. Methods , vol.4 , pp. 923-925
    • Kall, L.1    Canterbury, J.D.2    Weston, J.3    Noble, W.S.4    MacCoss, M.J.5
  • 35
    • 82755182013 scopus 로고    scopus 로고
    • Universal and confident phosphorylation site localization using phosphoRS
    • Taus, T., Kocher, T., Pichler, P., Paschke, C. et al., Universal and confident phosphorylation site localization using phosphoRS. J. Proteome Res. 2011, 10, 5354-5362.
    • (2011) J. Proteome Res. , vol.10 , pp. 5354-5362
    • Taus, T.1    Kocher, T.2    Pichler, P.3    Paschke, C.4
  • 36
    • 84863304598 scopus 로고    scopus 로고
    • R: A language and environment for statistical computing
    • R Foundation for Statistical Computing, Vienna, Austria
    • R Core Team, R: A language and environment for statistical computing. R Foundation for Statistical Computing, Vienna, Austria, 2014. http://www.R-project.org/.
    • (2014)
  • 37
    • 84893488015 scopus 로고    scopus 로고
    • fitdistrplus: help to fit of a parametric distribution to non-censored or censored data
    • Delignette-Muller, M. L., Pouillot, R., Denis, J.-B., Dutang, C., fitdistrplus: help to fit of a parametric distribution to non-censored or censored data, 2014.
    • (2014)
    • Delignette-Muller, M.L.1    Pouillot, R.2    Denis, J.-B.3    Dutang, C.4
  • 38
    • 18544382833 scopus 로고    scopus 로고
    • Generalized additive models for location, scale and shape, (with discussion)
    • Rigby, R. A., Stasinopoulos, D. M., Generalized additive models for location, scale and shape, (with discussion). Appl. Statist. 2005, 54, 507-554.
    • (2005) Appl. Statist , vol.54 , pp. 507-554
    • Rigby, R.A.1    Stasinopoulos, D.M.2
  • 39
    • 79961013401 scopus 로고    scopus 로고
    • Correct interpretation of comprehensive phosphorylation dynamics requires normalization by protein expression changes
    • M111 009654
    • Wu, R., Dephoure, N., Haas, W., Huttlin, E. L. et al., Correct interpretation of comprehensive phosphorylation dynamics requires normalization by protein expression changes. Mol. Cell. Proteomics 2011, 10, M111 009654.
    • (2011) Mol. Cell. Proteomics , vol.10
    • Wu, R.1    Dephoure, N.2    Haas, W.3    Huttlin, E.L.4
  • 40
    • 84882733620 scopus 로고    scopus 로고
    • IsobarPTM: a software tool for the quantitative analysis of post-translationally modified proteins
    • Breitwieser, F. P., Colinge, J., IsobarPTM: a software tool for the quantitative analysis of post-translationally modified proteins. J. Proteomics 2013, 90, 77-84.
    • (2013) J. Proteomics , vol.90 , pp. 77-84
    • Breitwieser, F.P.1    Colinge, J.2
  • 42
    • 27944499451 scopus 로고    scopus 로고
    • An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets
    • Schwartz, D., Gygi, S. P., An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets. Nat. Biotechnol. 2005, 23, 1391-1398.
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1391-1398
    • Schwartz, D.1    Gygi, S.P.2
  • 44
    • 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
  • 45
    • 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
  • 46
    • 84874741556 scopus 로고    scopus 로고
    • CluePedia Cytoscape plugin: pathway insights using integrated experimental and in silico data
    • Bindea, G., Galon, J., Mlecnik, B., CluePedia Cytoscape plugin: pathway insights using integrated experimental and in silico data. Bioinformatics 2013, 29, 661-663.
    • (2013) Bioinformatics , vol.29 , pp. 661-663
    • Bindea, G.1    Galon, J.2    Mlecnik, B.3
  • 47
    • 0029841220 scopus 로고    scopus 로고
    • The UL97 gene product of human cytomegalovirus is an early-late protein with a nuclear localization but is not a nucleoside kinase
    • Michel, D., Pavic, I., Zimmermann, A., Haupt, E. et al., The UL97 gene product of human cytomegalovirus is an early-late protein with a nuclear localization but is not a nucleoside kinase. J. Virol. 1996, 70, 6340-6346.
    • (1996) J. Virol. , vol.70 , pp. 6340-6346
    • Michel, D.1    Pavic, I.2    Zimmermann, A.3    Haupt, E.4
  • 48
    • 84919459578 scopus 로고    scopus 로고
    • Human cytomegalovirus UL97 phosphorylates the viral nuclear egress complex
    • Sharma, M., Bender, B. J., Kamil, J. P., Lye, M. F. et al., Human cytomegalovirus UL97 phosphorylates the viral nuclear egress complex. J. Virol. 2015, 89, 523-534.
    • (2015) J. Virol. , vol.89 , pp. 523-534
    • Sharma, M.1    Bender, B.J.2    Kamil, J.P.3    Lye, M.F.4
  • 49
    • 84906350501 scopus 로고    scopus 로고
    • Comparison of effects of inhibitors of viral and cellular protein kinases on human cytomegalovirus disruption of nuclear lamina and nuclear egress
    • Sharma, M., Coen, D. M., Comparison of effects of inhibitors of viral and cellular protein kinases on human cytomegalovirus disruption of nuclear lamina and nuclear egress. J. Virol. 2014, 88, 10982-10985.
    • (2014) J. Virol. , vol.88 , pp. 10982-10985
    • Sharma, M.1    Coen, D.M.2
  • 50
    • 84890880476 scopus 로고    scopus 로고
    • Human cytomegalovirus UL50 and UL53 recruit viral protein kinase UL97, not protein kinase C, for disruption of nuclear lamina and nuclear egress in infected cells
    • Sharma, M., Kamil, J. P., Coughlin, M., Reim, N. I., Coen, D. M., Human cytomegalovirus UL50 and UL53 recruit viral protein kinase UL97, not protein kinase C, for disruption of nuclear lamina and nuclear egress in infected cells. J. Virol. 2014, 88, 249-262.
    • (2014) J. Virol. , vol.88 , pp. 249-262
    • Sharma, M.1    Kamil, J.P.2    Coughlin, M.3    Reim, N.I.4    Coen, D.M.5
  • 51
    • 59249092261 scopus 로고    scopus 로고
    • Viral mimicry of Cdc2/cyclin-dependent kinase 1 mediates disruption of nuclear lamina during human cytomegalovirus nuclear egress
    • Hamirally, S., Kamil, J. P., Ndassa-Colday, Y. M., Lin, A. J. et al., Viral mimicry of Cdc2/cyclin-dependent kinase 1 mediates disruption of nuclear lamina during human cytomegalovirus nuclear egress. PLoS Pathog. 2009, 5, e1000275.
    • (2009) PLoS Pathog. , vol.5 , pp. e1000275
    • Hamirally, S.1    Kamil, J.P.2    Ndassa-Colday, Y.M.3    Lin, A.J.4
  • 52
    • 0038082392 scopus 로고    scopus 로고
    • The human cytomegalovirus UL44 protein is a substrate for the UL97 protein kinase
    • Krosky, P. M., Baek, M. C., Jahng, W. J., Barrera, I. et al., The human cytomegalovirus UL44 protein is a substrate for the UL97 protein kinase. J. Virol. 2003, 77, 7720-7727.
    • (2003) J. Virol. , vol.77 , pp. 7720-7727
    • Krosky, P.M.1    Baek, M.C.2    Jahng, W.J.3    Barrera, I.4
  • 53
    • 84919459578 scopus 로고    scopus 로고
    • Human cytomegalovirus UL97 phosphorylates the viral nuclear egress complex
    • Sharma, M., Bender, B. J., Kamil, J. P., Lye, M. F. et al., Human cytomegalovirus UL97 phosphorylates the viral nuclear egress complex. J. Virol. 2015, 89, 523-534.
    • (2015) J. Virol. , vol.89 , pp. 523-534
    • Sharma, M.1    Bender, B.J.2    Kamil, J.P.3    Lye, M.F.4
  • 54
    • 63449097589 scopus 로고    scopus 로고
    • Cytomegaloviral protein kinase pUL97 interacts with the nuclear mRNA export factor pUL69 to modulate its intranuclear localization and activity
    • Thomas, M., Rechter, S., Milbradt, J., Auerochs, S. et al., Cytomegaloviral protein kinase pUL97 interacts with the nuclear mRNA export factor pUL69 to modulate its intranuclear localization and activity. J. Gen. Virol. 2009, 90, 567-578.
    • (2009) J. Gen. Virol. , vol.90 , pp. 567-578
    • Thomas, M.1    Rechter, S.2    Milbradt, J.3    Auerochs, S.4
  • 55
    • 2942585139 scopus 로고    scopus 로고
    • Phosphorylation of the RNA polymerase II carboxyl-terminal domain in human cytomegalovirus-infected cells and in vitro by the viral UL97 protein kinase
    • Baek, M. C., Krosky, P. M., Pearson, A., Coen, D. M., Phosphorylation of the RNA polymerase II carboxyl-terminal domain in human cytomegalovirus-infected cells and in vitro by the viral UL97 protein kinase. Virology 2004, 324, 184-193.
    • (2004) Virology , vol.324 , pp. 184-193
    • Baek, M.C.1    Krosky, P.M.2    Pearson, A.3    Coen, D.M.4
  • 56
    • 84880367640 scopus 로고    scopus 로고
    • Human cytomegalovirus pUL97 regulates the viral major immediate early promoter by phosphorylation-mediated disruption of histone deacetylase 1 binding
    • Bigley, T. M., Reitsma, J. M., Mirza, S. P., Terhune, S. S., Human cytomegalovirus pUL97 regulates the viral major immediate early promoter by phosphorylation-mediated disruption of histone deacetylase 1 binding. J. Virol. 2013, 87, 7393-7408.
    • (2013) J. Virol. , vol.87 , pp. 7393-7408
    • Bigley, T.M.1    Reitsma, J.M.2    Mirza, S.P.3    Terhune, S.S.4
  • 57
    • 0037119463 scopus 로고    scopus 로고
    • Specific phosphorylation of exogenous protein and peptide substrates by the human cytomegalovirus UL97 protein kinase
    • Baek, M.-C., Krosky, P. M., He, Z., Coen, D. M., Specific phosphorylation of exogenous protein and peptide substrates by the human cytomegalovirus UL97 protein kinase. Importance of the P+5 position. J. Biol. Chem. 2002, 277, 29593-29599.
    • (2002) Importance of the P+5 position. J. Biol. Chem. , vol.277 , pp. 29593-29599
    • Baek, M.-C.1    Krosky, P.M.2    He, Z.3    Coen, D.M.4
  • 59
    • 84908473540 scopus 로고    scopus 로고
    • Cyclin-dependent kinases
    • Malumbres, M., Cyclin-dependent kinases. Genome Biol. 2014, 15, 122.
    • (2014) Genome Biol. , vol.15 , pp. 122
    • Malumbres, M.1
  • 61
    • 84941051170 scopus 로고    scopus 로고
    • STRING v10: protein-protein interaction networks, integrated over the tree of life
    • Szklarczyk, D., Franceschini, A., Wyder, S., Forslund, K. et al., STRING v10: protein-protein interaction networks, integrated over the tree of life. Nucleic Acids Res. 2015, 43, D447-D452.
    • (2015) Nucleic Acids Res. , vol.43 , pp. D447-D452
    • Szklarczyk, D.1    Franceschini, A.2    Wyder, S.3    Forslund, K.4
  • 63
    • 84860473143 scopus 로고    scopus 로고
    • mRNA export and the TREX complex
    • Katahira, J., mRNA export and the TREX complex. Biochim. Biophys. Acta 2012, 1819, 507-513.
    • (2012) Biochim. Biophys. Acta , vol.1819 , pp. 507-513
    • Katahira, J.1
  • 64
    • 80051950471 scopus 로고    scopus 로고
    • Sites and roles of phosphorylation of the human cytomegalovirus DNA polymerase subunit UL44
    • Silva, L. A., Strang, B. L., Lin, E. W., Kamil, J. P., Coen, D. M., Sites and roles of phosphorylation of the human cytomegalovirus DNA polymerase subunit UL44. Virology 2011, 417, 268-280.
    • (2011) Virology , vol.417 , pp. 268-280
    • Silva, L.A.1    Strang, B.L.2    Lin, E.W.3    Kamil, J.P.4    Coen, D.M.5
  • 65
    • 0032843725 scopus 로고    scopus 로고
    • Amino acids of conserved kinase motifs of cytomegalovirus protein UL97 are essential for autophosphorylation
    • Michel, D., Kramer, S., Hohn, S., Schaarschmidt, P. et al., Amino acids of conserved kinase motifs of cytomegalovirus protein UL97 are essential for autophosphorylation. J. Virol. 1999, 73, 8898-8901.
    • (1999) J. Virol. , vol.73 , pp. 8898-8901
    • Michel, D.1    Kramer, S.2    Hohn, S.3    Schaarschmidt, P.4
  • 66
    • 0036888936 scopus 로고    scopus 로고
    • Relationship between autophosphorylation and phosphorylation of exogenous substrates by the human cytomegalovirus UL97 protein kinase
    • Baek, M. C., Krosky, P. M., Coen, D. M., Relationship between autophosphorylation and phosphorylation of exogenous substrates by the human cytomegalovirus UL97 protein kinase. J. Virol. 2002, 76, 11943-11952.
    • (2002) J. Virol. , vol.76 , pp. 11943-11952
    • Baek, M.C.1    Krosky, P.M.2    Coen, D.M.3
  • 67
    • 0028931265 scopus 로고
    • Principles of CDK regulation
    • Morgan, D. O., Principles of CDK regulation. Nature 1995, 374, 131-134.
    • (1995) Nature , vol.374 , pp. 131-134
    • Morgan, D.O.1
  • 69
    • 1542405310 scopus 로고    scopus 로고
    • Eukaryotic MCM proteins: beyond replication initiation
    • Forsburg, S. L., Eukaryotic MCM proteins: beyond replication initiation. Microbiol. Mol. Biol. Rev. 2004, 68, 109-131.
    • (2004) Microbiol. Mol. Biol. Rev. , vol.68 , pp. 109-131
    • Forsburg, S.L.1
  • 70
    • 0037221209 scopus 로고    scopus 로고
    • Human cytomegalovirus prevents replication licensing by inhibiting MCM loading onto chromatin
    • Wiebusch, L., Uecker, R., Hagemeier, C., Human cytomegalovirus prevents replication licensing by inhibiting MCM loading onto chromatin. EMBO Rep. 2003, 4, 42-46.
    • (2003) EMBO Rep. , vol.4 , pp. 42-46
    • Wiebusch, L.1    Uecker, R.2    Hagemeier, C.3
  • 71
    • 0037323293 scopus 로고    scopus 로고
    • Human cytomegalovirus infection leads to accumulation of geminin and inhibition of the licensing of cellular DNA replication
    • Biswas, N., Sanchez, V., Spector, D. H., Human cytomegalovirus infection leads to accumulation of geminin and inhibition of the licensing of cellular DNA replication. J. Virol. 2003, 77, 2369-2376.
    • (2003) J. Virol. , vol.77 , pp. 2369-2376
    • Biswas, N.1    Sanchez, V.2    Spector, D.H.3
  • 72
    • 77950419555 scopus 로고    scopus 로고
    • Human cytomegalovirus protein pUL117 targets the mini-chromosome maintenance complex and suppresses cellular DNA synthesis
    • Qian, Z., Leung-Pineda, V., Xuan, B., Piwnica-Worms, H., Yu, D., Human cytomegalovirus protein pUL117 targets the mini-chromosome maintenance complex and suppresses cellular DNA synthesis. PLoS Pathog. 2010, 6, e1000814.
    • (2010) PLoS Pathog. , vol.6 , pp. e1000814
    • Qian, Z.1    Leung-Pineda, V.2    Xuan, B.3    Piwnica-Worms, H.4    Yu, D.5
  • 73
    • 79954599465 scopus 로고    scopus 로고
    • Herpesviruses remodel host membranes for virus egress
    • Johnson, D. C., Baines, J. D., Herpesviruses remodel host membranes for virus egress. Nat. Rev. Microbiol. 2011, 9, 382-394.
    • (2011) Nat. Rev. Microbiol. , vol.9 , pp. 382-394
    • Johnson, D.C.1    Baines, J.D.2
  • 74
    • 0036148284 scopus 로고    scopus 로고
    • Herpesvirus assembly and egress
    • Mettenleiter, T. C., Herpesvirus assembly and egress. J. Virol. 2002, 76, 1537-1547.
    • (2002) J. Virol. , vol.76 , pp. 1537-1547
    • Mettenleiter, T.C.1
  • 75
    • 84876319086 scopus 로고    scopus 로고
    • Inactivation of retinoblastoma protein does not overcome the requirement for human cytomegalovirus UL97 in lamina disruption and nuclear egress
    • Reim, N. I., Kamil, J. P., Wang, D., Lin, A. et al., Inactivation of retinoblastoma protein does not overcome the requirement for human cytomegalovirus UL97 in lamina disruption and nuclear egress. J. Virol. 2013, 87, 5019-5027.
    • (2013) J. Virol. , vol.87 , pp. 5019-5027
    • Reim, N.I.1    Kamil, J.P.2    Wang, D.3    Lin, A.4
  • 76
    • 58149388279 scopus 로고    scopus 로고
    • Exploring the nuclear envelope of herpes simplex virus 1-infected cells by high-resolution microscopy
    • Wild, P., Senn, C., Manera, C. L., Sutter, E. et al., Exploring the nuclear envelope of herpes simplex virus 1-infected cells by high-resolution microscopy. J. Virol. 2009, 83, 408-419.
    • (2009) J. Virol. , vol.83 , pp. 408-419
    • Wild, P.1    Senn, C.2    Manera, C.L.3    Sutter, E.4
  • 77
    • 50149097733 scopus 로고    scopus 로고
    • Nuclear pore composition and gating in herpes simplex virus-infected cells
    • Hofemeister, H., O'Hare, P., Nuclear pore composition and gating in herpes simplex virus-infected cells. J. Virol. 2008, 82, 8392-8399.
    • (2008) J. Virol. , vol.82 , pp. 8392-8399
    • Hofemeister, H.1    O'Hare, P.2
  • 78
    • 84859501317 scopus 로고    scopus 로고
    • Herpes simplex virus ICP27 protein directly interacts with the nuclear pore complex through Nup62, inhibiting host nucleocytoplasmic transport pathways
    • Malik, P., Tabarraei, A., Kehlenbach, R. H., Korfali, N. et al., Herpes simplex virus ICP27 protein directly interacts with the nuclear pore complex through Nup62, inhibiting host nucleocytoplasmic transport pathways. J. Biol. Chem. 2012, 287, 12277-12292.
    • (2012) J. Biol. Chem. , vol.287 , pp. 12277-12292
    • Malik, P.1    Tabarraei, A.2    Kehlenbach, R.H.3    Korfali, N.4
  • 79
    • 33644870991 scopus 로고    scopus 로고
    • RNA-binding of the human cytomegalovirus transactivator protein UL69, mediated by arginine-rich motifs, is not required for nuclear export of unspliced RNA
    • Toth, Z., Lischka, P., Stamminger, T., RNA-binding of the human cytomegalovirus transactivator protein UL69, mediated by arginine-rich motifs, is not required for nuclear export of unspliced RNA. Nucleic Acids Res. 2006, 34, 1237-1249.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 1237-1249
    • Toth, Z.1    Lischka, P.2    Stamminger, T.3
  • 80
    • 33644518219 scopus 로고    scopus 로고
    • The UL69 transactivator protein of human cytomegalovirus interacts with DEXD/H-Box RNA helicase UAP56 to promote cytoplasmic accumulation of unspliced RNA
    • Lischka, P., Toth, Z., Thomas, M., Mueller, R., Stamminger, T., The UL69 transactivator protein of human cytomegalovirus interacts with DEXD/H-Box RNA helicase UAP56 to promote cytoplasmic accumulation of unspliced RNA. Mol. Cell. Biol. 2006, 26, 1631-1643.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 1631-1643
    • Lischka, P.1    Toth, Z.2    Thomas, M.3    Mueller, R.4    Stamminger, T.5
  • 81
    • 22344438756 scopus 로고    scopus 로고
    • Recruitment of the human TREX complex to mRNA during splicing
    • Masuda, S., Das, R., Cheng, H., Hurt, E. et al., Recruitment of the human TREX complex to mRNA during splicing. Genes Dev. 2005, 19, 1512-1517.
    • (2005) Genes Dev. , vol.19 , pp. 1512-1517
    • Masuda, S.1    Das, R.2    Cheng, H.3    Hurt, E.4
  • 82
    • 81255208061 scopus 로고    scopus 로고
    • The many roles of the highly interactive HSV protein ICP27, a key regulator of infection
    • Sandri-Goldin, R. M., The many roles of the highly interactive HSV protein ICP27, a key regulator of infection. Future Microbiol. 2011, 6, 1261-1277.
    • (2011) Future Microbiol. , vol.6 , pp. 1261-1277
    • Sandri-Goldin, R.M.1
  • 83
    • 77956850226 scopus 로고    scopus 로고
    • ATP is required for interactions between UAP56 and two conserved mRNA export proteins, Aly and CIP29, to assemble the TREX complex
    • Dufu, K., Livingstone, M. J., Seebacher, J., Gygi, S. P. et al., ATP is required for interactions between UAP56 and two conserved mRNA export proteins, Aly and CIP29, to assemble the TREX complex. Genes Dev. 2010, 24, 2043-2053.
    • (2010) Genes Dev. , vol.24 , pp. 2043-2053
    • Dufu, K.1    Livingstone, M.J.2    Seebacher, J.3    Gygi, S.P.4
  • 84
    • 70450227426 scopus 로고    scopus 로고
    • UIF, a new mRNA export adaptor that works together with REF/ALY, requires FACT for recruitment to mRNA
    • Hautbergue, G. M., Hung, M. L., Walsh, M. J., Snijders, A. P. et al., UIF, a new mRNA export adaptor that works together with REF/ALY, requires FACT for recruitment to mRNA. Curr. Biol. 2009, 19, 1918-1924.
    • (2009) Curr. Biol. , vol.19 , pp. 1918-1924
    • Hautbergue, G.M.1    Hung, M.L.2    Walsh, M.J.3    Snijders, A.P.4
  • 85
    • 67449089967 scopus 로고    scopus 로고
    • Herpesvirus capsid association with the nuclear pore complex and viral DNA release involve the nucleoporin CAN/Nup214 and the capsid protein pUL25
    • Pasdeloup, D., Blondel, D., Isidro, A. L., Rixon, F. J., Herpesvirus capsid association with the nuclear pore complex and viral DNA release involve the nucleoporin CAN/Nup214 and the capsid protein pUL25. J. Virol. 2009, 83, 6610-6623.
    • (2009) J. Virol. , vol.83 , pp. 6610-6623
    • Pasdeloup, D.1    Blondel, D.2    Isidro, A.L.3    Rixon, F.J.4
  • 86
    • 79960216982 scopus 로고    scopus 로고
    • Regulatory roles of protein kinases in cytomegalovirus replication
    • Marschall, M., Feichtinger, S., Milbradt, J., Regulatory roles of protein kinases in cytomegalovirus replication. Ad. Virus Res. 2011, 80, 69-101.
    • (2011) Ad. Virus Res. , vol.80 , pp. 69-101
    • Marschall, M.1    Feichtinger, S.2    Milbradt, J.3
  • 87
    • 84878463182 scopus 로고    scopus 로고
    • Potential of protein kinase inhibitors for treating herpesvirus-associated disease
    • Li, R., Hayward, S. D., Potential of protein kinase inhibitors for treating herpesvirus-associated disease. Trends Microbiol. 2013, 21, 286-295.
    • (2013) Trends Microbiol. , vol.21 , pp. 286-295
    • Li, R.1    Hayward, S.D.2
  • 88
    • 4644312884 scopus 로고    scopus 로고
    • Identification of proteins in human cytomegalovirus (HCMV) particles: the HCMV proteome
    • Varnum, S. M., Streblow, D. N., Monroe, M. E., Smith, P. et al., Identification of proteins in human cytomegalovirus (HCMV) particles: the HCMV proteome. J. Virol. 2004, 78, 10960-10966.
    • (2004) J. Virol. , vol.78 , pp. 10960-10966
    • Varnum, S.M.1    Streblow, D.N.2    Monroe, M.E.3    Smith, P.4
  • 89
    • 50149119228 scopus 로고    scopus 로고
    • Comprehensive characterization of extracellular herpes simplex virus type 1 virions
    • Loret, S., Guay, G., Lippe, R., Comprehensive characterization of extracellular herpes simplex virus type 1 virions. J. Virol. 2008, 82, 8605-8618.
    • (2008) J. Virol. , vol.82 , pp. 8605-8618
    • Loret, S.1    Guay, G.2    Lippe, R.3
  • 90
    • 27944499451 scopus 로고    scopus 로고
    • An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets
    • Schwartz, D., Gygi, S. P., An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets. Nat. Biotechnol. 2005, 23, 1391-1398.
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1391-1398
    • Schwartz, D.1    Gygi, S.P.2


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