메뉴 건너뛰기




Volumn 12, Issue 4, 2013, Pages 1820-1829

Proteomics analysis of Herpes Simplex Virus type 1-infected cells reveals dynamic changes of viral protein expression, ubiquitylation, and phosphorylation

Author keywords

DNA replication; gene expression; Herpes Simplex Virus; late proteins; phosphorylation; protein trafficking; proteome; ubiquitylation

Indexed keywords

ACICLOVIR; CAPSID PROTEIN; DNA POLYMERASE; HERPES SIMPLEX VIRUS 1 PROTEIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 84875938497     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr301157j     Document Type: Article
Times cited : (32)

References (55)
  • 2
    • 81155160868 scopus 로고    scopus 로고
    • Pseudorabies virus in wild swine: A global perspective
    • Müller, T. Pseudorabies virus in wild swine: a global perspective Arch. Virol. 2011, 156 (10) 1691-1705
    • (2011) Arch. Virol. , vol.156 , Issue.10 , pp. 1691-1705
    • Müller, T.1
  • 3
    • 0345306753 scopus 로고    scopus 로고
    • Three-dimensional structure of Herpes Simplex Virus from cryo-electron tomography
    • Grünewald, K. Three-dimensional structure of Herpes Simplex Virus from cryo-electron tomography Science 2003, 302 (5649) 1396-1398
    • (2003) Science , vol.302 , Issue.5649 , pp. 1396-1398
    • Grünewald, K.1
  • 5
    • 1442281992 scopus 로고    scopus 로고
    • Structural biology of hepatitis C virus
    • Penin, F. Structural biology of hepatitis C virus Hepatology 2004, 39 (1) 5-19
    • (2004) Hepatology , vol.39 , Issue.1 , pp. 5-19
    • Penin, F.1
  • 6
    • 84858214799 scopus 로고    scopus 로고
    • Assembly and Architecture of HIV.
    • In; Rossmann, M. G. Rao, V. B. Springer: New York
    • Ganser-Pornillos, B. K.; Yeager, M.;; Pornillos, O. Assembly and Architecture of HIV. In Viral Molecular Machines; Rossmann, M. G.; Rao, V. B., Eds.; Springer: New York, 2012; pp 441-465.
    • (2012) Viral Molecular Machines , pp. 441-465
    • Ganser-Pornillos, B.K.1    Yeager, M.2    Pornillos, O.3
  • 7
    • 25444439491 scopus 로고    scopus 로고
    • The first 30 minutes in the life of a virus: UnREST in the nucleus
    • Roizman, B.; Gu, H.; Mandel, G. The first 30 minutes in the life of a virus: unREST in the nucleus Cell Cycle 2005, 4 (8) 1019-1021
    • (2005) Cell Cycle , vol.4 , Issue.8 , pp. 1019-1021
    • Roizman, B.1    Gu, H.2    Mandel, G.3
  • 8
    • 34249950342 scopus 로고    scopus 로고
    • Herpes simplex virus.
    • In; Fields, B.N. Howley, P.M. Lippincott Williams & Wilkins: Philadelphia
    • Roizman, B.; Knipe, D.M.;; Whitley, R.J. Herpes simplex virus. In Fundamental Virology; Fields, B.N.,; Howley, P.M., Eds.; Lippincott Williams & Wilkins: Philadelphia, 2007; pp 2502-2601.
    • (2007) Fundamental Virology , pp. 2502-2601
    • Roizman, B.1    Knipe, D.M.2    Whitley, R.J.3
  • 9
    • 55249088121 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 ICP0 phosphorylation mutants impair the E3 ubiquitin ligase activity of ICP0 in a cell type-dependent manner
    • Boutell, C. Herpes simplex virus type 1 ICP0 phosphorylation mutants impair the E3 ubiquitin ligase activity of ICP0 in a cell type-dependent manner J. Virol. 2008, 82 (21) 10647-10656
    • (2008) J. Virol. , vol.82 , Issue.21 , pp. 10647-10656
    • Boutell, C.1
  • 10
    • 79955455003 scopus 로고    scopus 로고
    • Role of the herpes simplex virus 1 Us3 kinase phosphorylation site and endocytosis motifs in the intracellular transport and neurovirulence of envelope glycoprotein B
    • Imai, T. Role of the herpes simplex virus 1 Us3 kinase phosphorylation site and endocytosis motifs in the intracellular transport and neurovirulence of envelope glycoprotein B J. Virol. 2011, 85 (10) 5003-5015
    • (2011) J. Virol. , vol.85 , Issue.10 , pp. 5003-5015
    • Imai, T.1
  • 11
    • 35148834647 scopus 로고    scopus 로고
    • Intracellular trafficking and maturation of herpes simplex virus gB and virus egress require functional biogenesis of multivesicular bodies
    • Calistri, A. Intracellular trafficking and maturation of herpes simplex virus gB and virus egress require functional biogenesis of multivesicular bodies J. Virol. 2007, 81 (20) 11468-11478
    • (2007) J. Virol. , vol.81 , Issue.20 , pp. 11468-11478
    • Calistri, A.1
  • 12
    • 50149119228 scopus 로고    scopus 로고
    • Comprehensive characterization of extracellular herpes simplex virus type 1 virions
    • Loret, S.; Guay, G.; Lippé, R. Comprehensive characterization of extracellular herpes simplex virus type 1 virions J. Virol. 2008, 82 (17) 8605-8618
    • (2008) J. Virol. , vol.82 , Issue.17 , pp. 8605-8618
    • Loret, S.1    Guay, G.2    Lippé, R.3
  • 13
    • 84875680653 scopus 로고    scopus 로고
    • Contribution of MS-based proteomics to the understanding of Herpes Simplex Virus type 1 interaction with host cells
    • 10.3389/fmicb.2012.00107
    • Santamaria, E. Contribution of MS-based proteomics to the understanding of Herpes Simplex Virus type 1 interaction with host cells Front. Microbiol. 2012, 10.3389/fmicb.2012.00107
    • (2012) Front. Microbiol.
    • Santamaria, E.1
  • 14
    • 65349109171 scopus 로고    scopus 로고
    • Isolation and preliminary characterization of Herpes Simplex Virus 1 primary enveloped virions from the perinuclear space
    • Padula, M. E.; Sydnor, M. L.; Wilson, D. W. Isolation and preliminary characterization of Herpes Simplex Virus 1 primary enveloped virions from the perinuclear space J. Virol. 2009, 83 (10) 4757-4765
    • (2009) J. Virol. , vol.83 , Issue.10 , pp. 4757-4765
    • Padula, M.E.1    Sydnor, M.L.2    Wilson, D.W.3
  • 15
    • 33751424925 scopus 로고    scopus 로고
    • Pseudorabies virus particles lacking tegument proteins pUL11 or pUL16 incorporate less full-length pUL36 than wild-type virus, but specifically accumulate a pUL36 N-terminal fragment
    • Michael, K. Pseudorabies virus particles lacking tegument proteins pUL11 or pUL16 incorporate less full-length pUL36 than wild-type virus, but specifically accumulate a pUL36 N-terminal fragment J. Gen. Virol. 2006, 87 (12) 3503-3507
    • (2006) J. Gen. Virol. , vol.87 , Issue.12 , pp. 3503-3507
    • Michael, K.1
  • 16
    • 84867231810 scopus 로고    scopus 로고
    • Deciphering novel host-Herpesvirus interactions by virion proteomics
    • Lippé, R. Deciphering novel host-Herpesvirus interactions by virion proteomics Front. Microbiol. 2012, 3, 181-190
    • (2012) Front. Microbiol. , vol.3 , pp. 181-190
    • Lippé, R.1
  • 17
    • 84869232621 scopus 로고    scopus 로고
    • Global secretome characterization of Herpes Simplex Virus 1-infected human primary macrophages
    • Miettinen, J. J.; Matikainen, S.; Nyman, T. A. Global secretome characterization of Herpes Simplex Virus 1-infected human primary macrophages J. Virol. 2012, 86, 12770-12778
    • (2012) J. Virol. , vol.86 , pp. 12770-12778
    • Miettinen, J.J.1    Matikainen, S.2    Nyman, T.A.3
  • 18
    • 79960958455 scopus 로고    scopus 로고
    • Divergent effects of human cytomegalovirus and Herpes Simplex Virus-1 on cellular metabolism
    • Vastag, L. Divergent effects of human cytomegalovirus and Herpes Simplex Virus-1 on cellular metabolism PLoS Pathog. 2011, 7 (7) e1002124
    • (2011) PLoS Pathog. , vol.7 , Issue.7 , pp. 1002124
    • Vastag, L.1
  • 19
    • 68549125523 scopus 로고    scopus 로고
    • Proteomic analysis of cells in the early stages of herpes simplex virus type-1 infection reveals widespread changes in the host cell proteome
    • Antrobus, R. Proteomic analysis of cells in the early stages of herpes simplex virus type-1 infection reveals widespread changes in the host cell proteome Proteomics 2009, 9 (15) 3913-3927
    • (2009) Proteomics , vol.9 , Issue.15 , pp. 3913-3927
    • Antrobus, R.1
  • 20
    • 77952878717 scopus 로고    scopus 로고
    • Gene expression profiling of Pseudorabies virus (PrV) infected bovine cells by combination of transcript analysis and quantitative proteomic techniques
    • Skiba, M. Gene expression profiling of Pseudorabies virus (PrV) infected bovine cells by combination of transcript analysis and quantitative proteomic techniques Vet. Microbiol. 2010, 143 (1) 14-20
    • (2010) Vet. Microbiol. , vol.143 , Issue.1 , pp. 14-20
    • Skiba, M.1
  • 21
    • 0028910938 scopus 로고
    • A phagosome-to-cytosol pathway for exogenous antigens presented on MHC class i molecules
    • Kovacsovics-Bankowski, M.; Rock., K. L. A phagosome-to-cytosol pathway for exogenous antigens presented on MHC class I molecules Science 1995, 267 (5195) 243-246
    • (1995) Science , vol.267 , Issue.5195 , pp. 243-246
    • Kovacsovics-Bankowski, M.1    Rock, K.L.A.2
  • 22
    • 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. Eclipse phase of Herpes Simplex Virus Type 1 infection: efficient dynein-mediated capsid transport without the small capsid protein VP26 J. Virol. 2006, 80 (16) 8211-8224
    • (2006) J. Virol. , vol.80 , Issue.16 , pp. 8211-8224
    • Döhner, K.1
  • 23
    • 12144291497 scopus 로고    scopus 로고
    • Tandem MS analysis of brain clathrin-coated vesicles reveals their critical involvement in synaptic vesicle recycling
    • Blondeau, F. Tandem MS analysis of brain clathrin-coated vesicles reveals their critical involvement in synaptic vesicle recycling Proc. Natl. Acad. Sci. U.S.A. 2004, 101 (11) 3833-3838
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , Issue.11 , pp. 3833-3838
    • Blondeau, F.1
  • 24
    • 33845500104 scopus 로고    scopus 로고
    • Quantitative proteomics analysis of the secretory pathway
    • Gilchrist, A. Quantitative proteomics analysis of the secretory pathway Cell 2006, 127 (6) 1265-1281
    • (2006) Cell , vol.127 , Issue.6 , pp. 1265-1281
    • Gilchrist, A.1
  • 25
    • 84869205080 scopus 로고    scopus 로고
    • Proteomic characterization of phagosomal membrane microdomains during phagolysosome biogenesis and evolution
    • Goyette, G. Proteomic characterization of phagosomal membrane microdomains during phagolysosome biogenesis and evolution Mol. Cell. Proteomics 2012, 14 (11) 941-950
    • (2012) Mol. Cell. Proteomics , vol.14 , Issue.11 , pp. 941-950
    • Goyette, G.1
  • 26
    • 80051631238 scopus 로고    scopus 로고
    • GProX, a user-friendly platform for bioinformatics analysis and visualization of quantitative proteomics data
    • Rigbolt, K. T.; Vanselow, J. T.; Blagoev., B. GProX, a user-friendly platform for bioinformatics analysis and visualization of quantitative proteomics data Mol. Cell. Proteomics 2011, 10 (8) O110.007450
    • (2011) Mol. Cell. Proteomics , vol.10 , Issue.8 , pp. 110007450
    • Rigbolt, K.T.1    Vanselow, J.T.2    Blagoev, B.3
  • 27
    • 79959733666 scopus 로고    scopus 로고
    • Proteoconnections: A bioinformatics platform to facilitate proteome and phosphoproteome analysis
    • Courcelles, M. Proteoconnections: A bioinformatics platform to facilitate proteome and phosphoproteome analysis Proteomics 2011, 11, 2654-2671
    • (2011) Proteomics , vol.11 , pp. 2654-2671
    • Courcelles, M.1
  • 28
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • Olsen, J. V. Global, in vivo, and site-specific phosphorylation dynamics in signaling networks Cell 2006, 127, 635-648
    • (2006) Cell , vol.127 , pp. 635-648
    • Olsen, J.V.1
  • 29
    • 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 (11) 1391-1398
    • (2005) Nat. Biotechnol. , vol.23 , Issue.11 , pp. 1391-1398
    • Schwartz, D.1    Gygi, S.P.2
  • 30
    • 30344486584 scopus 로고    scopus 로고
    • Antiviral prodrugs - The development of successful prodrug strategies for antiviral chemotherapy
    • De Clercq, E.; Field, H. J. Antiviral prodrugs-the development of successful prodrug strategies for antiviral chemotherapy Br. J. Pharmacol. 2006, 147 (1) 1-11
    • (2006) Br. J. Pharmacol. , vol.147 , Issue.1 , pp. 1-11
    • De Clercq, E.1    Field, H.J.2
  • 31
    • 0023133240 scopus 로고
    • The Herpes Simplex Virus Type 1 DNA polymerase gene: Site of phosphonoacetic acid resistance mutation in strain Angelotti is highly conserved
    • Knopf, C. W. The Herpes Simplex Virus Type 1 DNA polymerase gene: site of phosphonoacetic acid resistance mutation in strain Angelotti is highly conserved J. Gen. Virol. 1987, 68 (5) 1429-1433
    • (1987) J. Gen. Virol. , vol.68 , Issue.5 , pp. 1429-1433
    • Knopf, C.W.1
  • 32
    • 0033771363 scopus 로고    scopus 로고
    • Global analysis of Herpes Simplex Virus Type 1 transcription using an oligonucleotide-based DNA microarray
    • Stingley, S. W. Global analysis of Herpes Simplex Virus Type 1 transcription using an oligonucleotide-based DNA microarray J. Virol. 2000, 74, 9916-9927
    • (2000) J. Virol. , vol.74 , pp. 9916-9927
    • Stingley, S.W.1
  • 33
    • 84861867814 scopus 로고    scopus 로고
    • Ubiquitin and membrane protein turnover: From cradle to grave
    • MacGurn, J. A.; Hsu, P. C.; Emr., S. D. Ubiquitin and membrane protein turnover: from cradle to grave Annu. Rev. Biochem. 2012, 81, 231-259
    • (2012) Annu. Rev. Biochem. , vol.81 , pp. 231-259
    • MacGurn, J.A.1    Hsu, P.C.2    Emr, S.D.3
  • 34
    • 84863588585 scopus 로고    scopus 로고
    • Functional characterization of residues required for the herpes simplex virus 1 E3 ubiquitin ligase ICP0 to interact with the cellular E2 ubiquitin-conjugating enzyme UBE2D1 (UbcH5a)
    • Vanni, E. Functional characterization of residues required for the herpes simplex virus 1 E3 ubiquitin ligase ICP0 to interact with the cellular E2 ubiquitin-conjugating enzyme UBE2D1 (UbcH5a) J. Virol. 2012, 86 (11) 6323-6333
    • (2012) J. Virol. , vol.86 , Issue.11 , pp. 6323-6333
    • Vanni, E.1
  • 35
    • 80053459914 scopus 로고    scopus 로고
    • A viral ubiquitin ligase has substrate preferential SUMO targeted ubiquitin ligase activity that counteracts intrinsic antiviral defence
    • Boutell, C. A viral ubiquitin ligase has substrate preferential SUMO targeted ubiquitin ligase activity that counteracts intrinsic antiviral defence PLoS Pathog. 2011, 7 (9) e1002245
    • (2011) PLoS Pathog. , vol.7 , Issue.9 , pp. 1002245
    • Boutell, C.1
  • 36
    • 80052289989 scopus 로고    scopus 로고
    • Autocatalytic activity of the ubiquitin-specific protease domain of herpes simplex virus 1 VP1-2
    • Bolstad, M. Autocatalytic activity of the ubiquitin-specific protease domain of herpes simplex virus 1 VP1-2 J. Virol. 2011, 85 (17) 8738-8751
    • (2011) J. Virol. , vol.85 , Issue.17 , pp. 8738-8751
    • Bolstad, M.1
  • 37
    • 32244436490 scopus 로고    scopus 로고
    • Identification and evolution of dual-topology membrane proteins
    • Rapp, M. Identification and evolution of dual-topology membrane proteins Nat. Struct. Mol. Biol. 2006, 13, 112-116
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 112-116
    • Rapp, M.1
  • 38
    • 32244440745 scopus 로고    scopus 로고
    • Flip-flopping membrane proteins
    • Bowie, J. U. Flip-flopping membrane proteins Nat. Struct. Mol. Biol. 2006, 13, 94-96
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 94-96
    • Bowie, J.U.1
  • 39
    • 80053131428 scopus 로고    scopus 로고
    • A novel virus encoded nucleocytoplasmic shuttling protein: The UL3 protein of herpes simplex virus type 1
    • Zheng, C. A novel virus encoded nucleocytoplasmic shuttling protein: the UL3 protein of herpes simplex virus type 1 J. Virol. Methods 2011, 177 (2) 206-210
    • (2011) J. Virol. Methods , vol.177 , Issue.2 , pp. 206-210
    • Zheng, C.1
  • 40
    • 80054911147 scopus 로고    scopus 로고
    • Molecular determinants responsible for the subcellular localization of HSV-1 UL4 protein
    • Pan, W. W. Molecular determinants responsible for the subcellular localization of HSV-1 UL4 protein Virol. Sin. 2011, 26 (5) 347-356
    • (2011) Virol. Sin. , vol.26 , Issue.5 , pp. 347-356
    • Pan, W.W.1
  • 41
    • 0032579608 scopus 로고    scopus 로고
    • Genetic analysis of the UL15 gene locus for the putative terminase of Herpes Simplex Virus Type 1
    • Yu, D.; Weller, S. K. Genetic analysis of the UL15 gene locus for the putative terminase of Herpes Simplex Virus Type 1 Virology 1998, 243, 32-44
    • (1998) Virology , vol.243 , pp. 32-44
    • Yu, D.1    Weller, S.K.2
  • 42
    • 84862246069 scopus 로고    scopus 로고
    • Herpes simplex virus US3 protein kinase regulates host responses and determines neurovirulence
    • Mori, I. Herpes simplex virus US3 protein kinase regulates host responses and determines neurovirulence Microbiol. Immunol. 2012, 56 (6) 351-355
    • (2012) Microbiol. Immunol. , vol.56 , Issue.6 , pp. 351-355
    • Mori, I.1
  • 43
    • 35649019773 scopus 로고    scopus 로고
    • Identification of proteins directly phosphorylated by UL13 protein kinase from herpes simplex virus 1
    • Asai, R. Identification of proteins directly phosphorylated by UL13 protein kinase from herpes simplex virus 1 Microb. Infect. 2007, 9 (12-13) 1434-1438
    • (2007) Microb. Infect. , vol.9 , Issue.1213 , pp. 1434-1438
    • Asai, R.1
  • 44
    • 84859731169 scopus 로고    scopus 로고
    • Viral E3 Ubiquitin ligase-mediated degradation of a cellular E3: Viral mimicry of a cellular phosphorylation mark targets the RNF8 FHA domain
    • Chaurushiya, M. S. Viral E3 Ubiquitin ligase-mediated degradation of a cellular E3: viral mimicry of a cellular phosphorylation mark targets the RNF8 FHA domain Mol. Cell 2012, 46, 79-90
    • (2012) Mol. Cell , vol.46 , pp. 79-90
    • Chaurushiya, M.S.1
  • 45
    • 81255163727 scopus 로고    scopus 로고
    • Herpes simplex virus 1 ICP0 phosphorylation site mutants are attenuated for viral replication and impaired for explant-induced reactivation
    • Mostafa, H. H. Herpes simplex virus 1 ICP0 phosphorylation site mutants are attenuated for viral replication and impaired for explant-induced reactivation J. Virol. 2011, 85 (23) 12631-12637
    • (2011) J. Virol. , vol.85 , Issue.23 , pp. 12631-12637
    • Mostafa, H.H.1
  • 47
    • 72849114717 scopus 로고    scopus 로고
    • Effects of phosphorylation of herpes simplex virus 1 envelope glycoprotein B by Us3 kinase in vivo and in vitro
    • Imai, T. Effects of phosphorylation of herpes simplex virus 1 envelope glycoprotein B by Us3 kinase in vivo and in vitro J. Virol. 2010, 84 (1) 153-162
    • (2010) J. Virol. , vol.84 , Issue.1 , pp. 153-162
    • Imai, T.1
  • 48
    • 0021964094 scopus 로고
    • Protein kinase activities associated with the virions of pseudorabies and herpes simplex virus
    • Stevely, W. S. Protein kinase activities associated with the virions of pseudorabies and herpes simplex virus J. Gen. Virol. 1985, 66, 661-673
    • (1985) J. Gen. Virol. , vol.66 , pp. 661-673
    • Stevely, W.S.1
  • 49
    • 77649203653 scopus 로고    scopus 로고
    • ICP27 phosphorylation site mutants are defective in herpes simplex virus 1 replication and gene expression
    • Rojas, S. ICP27 phosphorylation site mutants are defective in herpes simplex virus 1 replication and gene expression J. Virol. 2010, 84, 2200-2211
    • (2010) J. Virol. , vol.84 , pp. 2200-2211
    • Rojas, S.1
  • 50
    • 84863998594 scopus 로고    scopus 로고
    • The N terminus and C terminus of herpes simplex virus 1 ICP4 cooperate to activate viral gene expression
    • Wagner, L. M. The N terminus and C terminus of herpes simplex virus 1 ICP4 cooperate to activate viral gene expression J. Virol. 2012, 86 (12) 6862-6874
    • (2012) J. Virol. , vol.86 , Issue.12 , pp. 6862-6874
    • Wagner, L.M.1
  • 51
    • 58149386424 scopus 로고    scopus 로고
    • Identification of sequences in herpes simplex virus type 1 ICP22 that influence RNA polymerase II modification and viral late gene expression
    • Bastian, T. W.; Rice, S. A. Identification of sequences in herpes simplex virus type 1 ICP22 that influence RNA polymerase II modification and viral late gene expression J. Virol. 2009, 83 (1) 128-139
    • (2009) J. Virol. , vol.83 , Issue.1 , pp. 128-139
    • Bastian, T.W.1    Rice, S.A.2
  • 52
    • 41649117065 scopus 로고    scopus 로고
    • Substrate specificity of the herpes simplex virus type 2 UL13 protein kinase
    • Cano-Monreal, G. L.; Tavis, J. E.; Morrison, L. A. Substrate specificity of the herpes simplex virus type 2 UL13 protein kinase Virology 2008, 374 (1) 1-10
    • (2008) Virology , vol.374 , Issue.1 , pp. 1-10
    • Cano-Monreal, G.L.1    Tavis, J.E.2    Morrison, L.A.3
  • 53
    • 0023281035 scopus 로고
    • Herpes simplex virus 1 protein kinase is encoded by open reading frame US3 which is not essential for virus growth in cell culture
    • Purves, F. C. Herpes simplex virus 1 protein kinase is encoded by open reading frame US3 which is not essential for virus growth in cell culture J. Virol. 1987, 61 (9) 2896-2901
    • (1987) J. Virol. , vol.61 , Issue.9 , pp. 2896-2901
    • Purves, F.C.1
  • 54
    • 21444459417 scopus 로고    scopus 로고
    • Identification of proteins phosphorylated directly by the Us3 protein kinase encoded by herpes simplex virus 1
    • Kato, A. Identification of proteins phosphorylated directly by the Us3 protein kinase encoded by herpes simplex virus 1 J. Virol. 2005, 79 (14) 9325-9331
    • (2005) J. Virol. , vol.79 , Issue.14 , pp. 9325-9331
    • Kato, A.1
  • 55
    • 0033015083 scopus 로고    scopus 로고
    • Analysis of the phosphorylation sites of herpes simplex virus 1 regulatory protein ICP27
    • Zhi, Y.; Sandri-Goldin, R. M. Analysis of the phosphorylation sites of herpes simplex virus 1 regulatory protein ICP27 J. Virol. 1999, 73, 3246-3257
    • (1999) J. Virol. , vol.73 , pp. 3246-3257
    • Zhi, Y.1    Sandri-Goldin, R.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.