메뉴 건너뛰기




Volumn 78, Issue 15, 2004, Pages 8068-8077

Herpes simplex virus type 1 infection induces the stabilization of p53 in a USP7- and ATM-independent manner

Author keywords

[No Author keywords available]

Indexed keywords

ATM PROTEIN; PROTEIN ICP0; PROTEIN P53; PROTEIN USP7; REGULATOR PROTEIN; SERINE; UNCLASSIFIED DRUG; VIRUS DNA; VIRUS PROTEIN;

EID: 3242701316     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.78.15.8068-8077.2004     Document Type: Article
Times cited : (39)

References (83)
  • 1
    • 0021228172 scopus 로고
    • Characterization of herpes simplex virus 1 alpha proteins 0, 4, and 27 with monoclonal antibodies
    • Ackermann, M., D. K. Braun, L. Pereira, and B. Roizman. 1984. Characterization of herpes simplex virus 1 alpha proteins 0, 4, and 27 with monoclonal antibodies. J. Virol. 52:108-118.
    • (1984) J. Virol. , vol.52 , pp. 108-118
    • Ackermann, M.1    Braun, D.K.2    Pereira, L.3    Roizman, B.4
  • 2
    • 0034812986 scopus 로고    scopus 로고
    • Modulation of apoptosis during herpes simplex virus infection in human cells
    • Aubert, M., and J. A. Blaho. 2001. Modulation of apoptosis during herpes simplex virus infection in human cells. Microbes Infect. 3:859-866.
    • (2001) Microbes Infect. , vol.3 , pp. 859-866
    • Aubert, M.1    Blaho, J.A.2
  • 3
    • 0027263408 scopus 로고
    • Enhanced degradation of p53 protein in HPV-6 and BPV-1 E6-immortalized human mammary epithelial cells
    • Band, V., S. Dalai, L. Delmolino, and E. J. Androphy. 1993. Enhanced degradation of p53 protein in HPV-6 and BPV-1 E6-immortalized human mammary epithelial cells. EMBO J. 12:1847-1852.
    • (1993) EMBO J. , vol.12 , pp. 1847-1852
    • Band, V.1    Dalai, S.2    Delmolino, L.3    Androphy, E.J.4
  • 4
    • 0042157103 scopus 로고    scopus 로고
    • Viruses and the 26S proteasome: Hacking into destruction
    • Banks, L., D. Piro, and M. Thomas. 2003. Viruses and the 26S proteasome: hacking into destruction. Trends Biochem. Sci. 28:452-459.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 452-459
    • Banks, L.1    Piro, D.2    Thomas, M.3
  • 5
    • 0025858631 scopus 로고
    • Wild-type but not mutant p53 immunopurified proteins bind to sequences adjacent to the SV40 origin of replication
    • Bargonetti, J., P. N. Friedman, S. E. Kern, B. Vogelstein, and C. Prives. 1991. Wild-type but not mutant p53 immunopurified proteins bind to sequences adjacent to the SV40 origin of replication. Cell 65:1083-1091.
    • (1991) Cell , vol.65 , pp. 1083-1091
    • Bargonetti, J.1    Friedman, P.N.2    Kern, S.E.3    Vogelstein, B.4    Prives, C.5
  • 6
    • 0037127284 scopus 로고    scopus 로고
    • Regulation of the accumulation and function of p53 by phosphorylation of two residues within the domain that binds to Mdm2
    • Bean, L. J., and G. R. Stark. 2002. Regulation of the accumulation and function of p53 by phosphorylation of two residues within the domain that binds to Mdm2. J. Biol. Chem. 277:1864-1871.
    • (2002) J. Biol. Chem. , vol.277 , pp. 1864-1871
    • Bean, L.J.1    Stark, G.R.2
  • 7
    • 0022457155 scopus 로고
    • Herpes simplex virus immediate early infected-cell polypeptide 4 binds to DNA and promotes transcription
    • Beard, P., S. Faber, K. W. Wilcox, and L. I. Pizer. 1986. Herpes simplex virus immediate early infected-cell polypeptide 4 binds to DNA and promotes transcription. Proc. Natl. Acad. Sci. USA 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
  • 8
    • 0035794541 scopus 로고    scopus 로고
    • COP9 signalosome-specific phosphorylation targets p53 to degradation by the ubiquitin system
    • Bech-Otschir, D., R. Kraft, X. Huang, P. Henklein, B. Kapelari, C. Pollmann, and W. Dubiel. 2001. COP9 signalosome-specific phosphorylation targets p53 to degradation by the ubiquitin system. EMBO J. 20:1630-1639.
    • (2001) EMBO J. , vol.20 , pp. 1630-1639
    • Bech-Otschir, D.1    Kraft, R.2    Huang, X.3    Henklein, P.4    Kapelari, B.5    Pollmann, C.6    Dubiel, W.7
  • 9
    • 0141704201 scopus 로고    scopus 로고
    • The herpes simplex virus type 1 (HSV-1) regulatory protein ICP0 interacts with and ubiquitinates p53
    • Boutell, C., and R. D. Everett. 2003. The herpes simplex virus type 1 (HSV-1) regulatory protein ICP0 interacts with and ubiquitinates p53. J. Biol. Chem. 278:36596-36602.
    • (2003) J. Biol. Chem. , vol.278 , pp. 36596-36602
    • Boutell, C.1    Everett, R.D.2
  • 10
    • 0042709466 scopus 로고    scopus 로고
    • PML residue lysine 160 is required for the degradation of PML induced by herpes simplex virus type 1 regulatory protein ICP0
    • Boutell, C., A. Orr, and R. D. Everett. 2003. PML residue lysine 160 is required for the degradation of PML induced by herpes simplex virus type 1 regulatory protein ICP0. J. Virol. 77:8686-8694.
    • (2003) J. Virol. , vol.77 , pp. 8686-8694
    • Boutell, C.1    Orr, A.2    Everett, R.D.3
  • 11
    • 0036138854 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 immediate-early protein ICP1 and its isolated RING finger domain act as ubiquitin E3 ligases in vitro
    • Boutell, C., S. Sadis, and R. D. Everett. 2002. Herpes simplex virus type 1 immediate-early protein ICP1 and its isolated RING finger domain act as ubiquitin E3 ligases in vitro. J. Virol. 76:841-850.
    • (2002) J. Virol. , vol.76 , pp. 841-850
    • Boutell, C.1    Sadis, S.2    Everett, R.D.3
  • 12
    • 0037377060 scopus 로고    scopus 로고
    • Ubiquitination, phosphorylation and acetylation: The molecular basis for p53 regulation
    • Brooks, C. L., and W. Gu. 2003. Ubiquitination, phosphorylation and acetylation: the molecular basis for p53 regulation. Curr. Opin. Cell Biol. 15: 164-171.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 164-171
    • Brooks, C.L.1    Gu, W.2
  • 13
    • 0033611590 scopus 로고    scopus 로고
    • Herpes virus induced proteasome-dependent degradation of the nuclear bodies-associated PML and Sp100 proteins
    • Chelbi-Alix, M. K., and H. de The. 1999. Herpes virus induced proteasome-dependent degradation of the nuclear bodies-associated PML and Sp100 proteins. Oncogene 18:935-941.
    • (1999) Oncogene , vol.18 , pp. 935-941
    • Chelbi-Alix, M.K.1    De The, H.2
  • 14
    • 0022358365 scopus 로고
    • Isolation and characterization of deletion mutants of herpes simplex virus type 1 in the gene encoding immediate-early regulatory protein ICP4
    • DeLuca, N. A., A. M. McCarthy, and P. A. Schaffer. 1985. Isolation and characterization of deletion mutants of herpes simplex virus type 1 in the gene encoding immediate-early regulatory protein ICP4. J. Virol. 56:558-570.
    • (1985) J. Virol. , vol.56 , pp. 558-570
    • DeLuca, N.A.1    McCarthy, A.M.2    Schaffer, P.A.3
  • 15
    • 0034649503 scopus 로고    scopus 로고
    • ATM complexes with HDM2 and promotes its rapid phosphorylation in a p53-independent manner in normal and tumor human cells exposed to ionizing radiation
    • de Toledo, S. M., E. I. Azzam, W. K. Dahlberg, T. B. Gooding, and J. B. Little. 2000. ATM complexes with HDM2 and promotes its rapid phosphorylation in a p53-independent manner in normal and tumor human cells exposed to ionizing radiation. Oncogene 19:6185-6193.
    • (2000) Oncogene , vol.19 , pp. 6185-6193
    • De Toledo, S.M.1    Azzam, E.I.2    Dahlberg, W.K.3    Gooding, T.B.4    Little, J.B.5
  • 16
    • 0027258003 scopus 로고
    • An epitope within the DNA-binding domain of the herpes simplex virus immediate early protein Vmw175 is conserved in the varicella-zoster virus gene 62 protein
    • Everett, R., A. Cross, J. Tyler, and A. Orr. 1993. An epitope within the DNA-binding domain of the herpes simplex virus immediate early protein Vmw175 is conserved in the varicella-zoster virus gene 62 protein. J. Gen. Virol. 74:1955-1958.
    • (1993) J. Gen. Virol. , vol.74 , pp. 1955-1958
    • Everett, R.1    Cross, A.2    Tyler, J.3    Orr, A.4
  • 17
    • 0023759594 scopus 로고
    • Analysis of the functional domains of herpes simplex virus type 1 immediate-early polypeptide Vmw110
    • Everett, R. D. 1988. Analysis of the functional domains of herpes simplex virus type 1 immediate-early polypeptide Vmw110. J. Mol. Biol. 202:87-96.
    • (1988) J. Mol. Biol. , vol.202 , pp. 87-96
    • Everett, R.D.1
  • 18
    • 0024512466 scopus 로고
    • Construction and characterization of herpes simplex virus type 1 mutants with defined lesions in immediate early gene 1
    • Everett, R. D. 1989. Construction and characterization of herpes simplex virus type 1 mutants with defined lesions in immediate early gene 1. J. Gen. Virol. 70:1185-1202.
    • (1989) J. Gen. Virol. , vol.70 , pp. 1185-1202
    • Everett, R.D.1
  • 19
    • 0033779119 scopus 로고    scopus 로고
    • ICP0 induces the accumulation of colocalizing conjugated ubiquitin
    • Everett, R. D. 2000. ICP0 induces the accumulation of colocalizing conjugated ubiquitin. J. Virol. 74:9994-10005.
    • (2000) J. Virol. , vol.74 , pp. 9994-10005
    • Everett, R.D.1
  • 20
    • 0033624137 scopus 로고    scopus 로고
    • ICP0, a regulator of herpes simplex virus during lytic and latent infection
    • Everett, R. D. 2000. ICP0, a regulator of herpes simplex virus during lytic and latent infection. Bioessays 22:761-770.
    • (2000) Bioessays , vol.22 , pp. 761-770
    • Everett, R.D.1
  • 21
    • 0842347715 scopus 로고    scopus 로고
    • Phenotype of a herpes simplex virus type 1 mutant that fails to express immediate-early regulatory protein ICP0
    • Everett, R. D., C. Boutell, and A. Orr. 2004. Phenotype of a herpes simplex virus type 1 mutant that fails to express immediate-early regulatory protein ICP0. J. Virol. 78:1763-1774.
    • (2004) J. Virol. , vol.78 , pp. 1763-1774
    • Everett, R.D.1    Boutell, C.2    Orr, A.3
  • 22
    • 0033559253 scopus 로고    scopus 로고
    • Specific destruction of kinetochore protein CENP-C and disruption of cell division by herpes simplex virus immediate-early protein Vmw110
    • Everett, R. D., W. C. Earnshaw, J. Findlay, and P. Lomonte. 1999. Specific destruction of kinetochore protein CENP-C and disruption of cell division by herpes simplex virus immediate-early protein Vmw110. EMBO J. 18:1526-1538.
    • (1999) EMBO J. , vol.18 , pp. 1526-1538
    • Everett, R.D.1    Earnshaw, W.C.2    Findlay, J.3    Lomonte, P.4
  • 23
    • 0031878851 scopus 로고    scopus 로고
    • The disruption of ND10 during herpes simplex virus infection correlates with the Vmw110- and proteasome-dependent loss of several PML isoforms
    • Everett, R. D., P. Freemont, H. Saitoh, M. Dasso, A. Orr, M. Kathoria, and J. Parkinson. 1998. The disruption of ND10 during herpes simplex virus infection correlates with the Vmw110- and proteasome-dependent loss of several PML isoforms. J. Virol. 72:6581-6591.
    • (1998) J. Virol. , vol.72 , pp. 6581-6591
    • Everett, R.D.1    Freemont, P.2    Saitoh, H.3    Dasso, M.4    Orr, A.5    Kathoria, M.6    Parkinson, J.7
  • 24
    • 0032889557 scopus 로고    scopus 로고
    • The ability of herpes simplex virus type 1 immediate-early protein Vmw110 to bind to a ubiquitin-specific protease contributes to its roles in the activation of gene expression and stimulation of virus replication
    • Everett, R. D., M. Meredith, and A. Orr. 1999. The ability of herpes simplex virus type 1 immediate-early protein Vmw110 to bind to a ubiquitin-specific protease contributes to its roles in the activation of gene expression and stimulation of virus replication. J. Virol. 73:417-426.
    • (1999) J. Virol. , vol.73 , pp. 417-426
    • Everett, R.D.1    Meredith, M.2    Orr, A.3
  • 25
    • 0031023690 scopus 로고    scopus 로고
    • A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory protein
    • Everett, R. D., M. Meredith, A. Orr, A. Cross, M. Kathoria, and J. Parkinson. 1997. A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory protein. EMBO J. 16:1519-1530.
    • (1997) EMBO J. , vol.16 , pp. 1519-1530
    • Everett, R.D.1    Meredith, M.2    Orr, A.3    Cross, A.4    Kathoria, M.5    Parkinson, J.6
  • 26
    • 0025946814 scopus 로고
    • High level expression and purification of herpes simplex virus type 1 immediate early polypeptide Vmw110
    • Everett, R. D., A. Orr, and M. Elliott. 1991. High level expression and purification of herpes simplex virus type 1 immediate early polypeptide Vmw110. Nucleic Acids Res. 19:6155-6161.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 6155-6161
    • Everett, R.D.1    Orr, A.2    Elliott, M.3
  • 27
    • 0032534802 scopus 로고    scopus 로고
    • A viral activator of gene expression functions via the ubiquitin-proteasome pathway
    • Everett, R. D., A. Orr, and C. M. Preston. 1998. A viral activator of gene expression functions via the ubiquitin-proteasome pathway. EMBO J. 17: 7161-7169.
    • (1998) EMBO J. , vol.17 , pp. 7161-7169
    • Everett, R.D.1    Orr, A.2    Preston, C.M.3
  • 28
    • 0031951650 scopus 로고    scopus 로고
    • p53 and RPA are sequestered in viral replication centers in the nuclei of cells infected with human cytomegalovirus
    • Fortunato, E. A., and D. H. Spector. 1998. p53 and RPA are sequestered in viral replication centers in the nuclei of cells infected with human cytomegalovirus. J. Virol. 72:2033-2039.
    • (1998) J. Virol. , vol.72 , pp. 2033-2039
    • Fortunato, E.A.1    Spector, D.H.2
  • 29
    • 0037241129 scopus 로고    scopus 로고
    • Viral induction of site-specific chromosome damage
    • Fortunato, E. A., and D. H. Spector. 2003. Viral induction of site-specific chromosome damage. Rev. Med. Virol. 13:21-37.
    • (2003) Rev. Med. Virol. , vol.13 , pp. 21-37
    • Fortunato, E.A.1    Spector, D.H.2
  • 30
    • 0033599006 scopus 로고    scopus 로고
    • p53 inhibition by the LANA protein of KSHV protects against cell death
    • Friborg, J., Jr., W. Kong, M. O. Hottiger, and G. J. Nabel. 1999. p53 inhibition by the LANA protein of KSHV protects against cell death. Nature 402:889-894.
    • (1999) Nature , vol.402 , pp. 889-894
    • Friborg Jr., J.1    Kong, W.2    Hottiger, M.O.3    Nabel, G.J.4
  • 31
    • 0032512057 scopus 로고    scopus 로고
    • Mdm2 association with p53 targets its ubiquitination
    • Fuchs, S. Y., V. Adler, T. Buschmann, X. Wu, and Z. Ronal. 1998. Mdm2 association with p53 targets its ubiquitination. Oncogene 17:2543-2547.
    • (1998) Oncogene , vol.17 , pp. 2543-2547
    • Fuchs, S.Y.1    Adler, V.2    Buschmann, T.3    Wu, X.4    Ronal, Z.5
  • 33
    • 0042808481 scopus 로고    scopus 로고
    • The degradation of promyelocytic leukemia and Sp100 proteins by herpes simplex virus 1 is mediated by the ubiquitin-conjugating enzyme UbcH5a
    • Gu, H., and B. Roizman. 2003. The degradation of promyelocytic leukemia and Sp100 proteins by herpes simplex virus 1 is mediated by the ubiquitin-conjugating enzyme UbcH5a. Proc. Natl. Acad. Sci. USA 100:8963-8968.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 8963-8968
    • Gu, H.1    Roizman, B.2
  • 34
    • 0037154225 scopus 로고    scopus 로고
    • Herpes simplex virus 1-infected cell protein 0 contains two E3 ubiquitin ligase sites specific for different E2 ubiquitin-conjugating enzymes
    • Hagglund, R., C. Van Sant, P. Lopez, and B. Roizman. 2002. Herpes simplex virus 1-infected cell protein 0 contains two E3 ubiquitin ligase sites specific for different E2 ubiquitin-conjugating enzymes. Proc. Natl. Acad. Sci. USA 99:631-636.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 631-636
    • Hagglund, R.1    Van Sant, C.2    Lopez, P.3    Roizman, B.4
  • 35
    • 0034726060 scopus 로고    scopus 로고
    • Multiple sites of in vivo phosphorylation in the MDM2 oncoprotein cluster within two important functional domains
    • Hay, T. J., and D. W. Meek. 2000. Multiple sites of in vivo phosphorylation in the MDM2 oncoprotein cluster within two important functional domains. FEBS Lett. 478:183-186.
    • (2000) FEBS Lett. , vol.478 , pp. 183-186
    • Hay, T.J.1    Meek, D.W.2
  • 36
    • 0344995285 scopus 로고    scopus 로고
    • Perturbation of cell cycle progression and cellular gene expression as a function of herpes simplex virus ICP0
    • Hobbs, W. E., II, and N. A. DeLuca. 1999. Perturbation of cell cycle progression and cellular gene expression as a function of herpes simplex virus ICP0. J. Virol. 73:8245-8255.
    • (1999) J. Virol. , vol.73 , pp. 8245-8255
    • Hobbs II, W.E.1    DeLuca, N.A.2
  • 37
    • 0031583962 scopus 로고    scopus 로고
    • Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53
    • Honda, R., H. Tanaka, and H. Yasuda. 1997. Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53. FEBS Lett. 420:25-27.
    • (1997) FEBS Lett. , vol.420 , pp. 25-27
    • Honda, R.1    Tanaka, H.2    Yasuda, H.3
  • 39
    • 0033963335 scopus 로고    scopus 로고
    • MdmX protects p53 from Mdm2-mediated degradation
    • Jackson, M. W., and S. J. Berberich. 2000. MdmX protects p53 from Mdm2-mediated degradation. Mol. Cell. Biol. 20:1001-1007.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1001-1007
    • Jackson, M.W.1    Berberich, S.J.2
  • 41
    • 0034688263 scopus 로고    scopus 로고
    • Cooperative phosphorylation at multiple sites is required to activate p53 in response to UV radiation
    • Kapoor, M., R. Hamm, W. Yan, Y. Taya, and G. Lozano. 2000. Cooperative phosphorylation at multiple sites is required to activate p53 in response to UV radiation. Oncogene 19:358-364.
    • (2000) Oncogene , vol.19 , pp. 358-364
    • Kapoor, M.1    Hamm, R.2    Yan, W.3    Taya, Y.4    Lozano, G.5
  • 42
    • 0033592868 scopus 로고    scopus 로고
    • Rapid ATM-dependent phosphorylation of MDM2 precedes p53 accumulation in response to DNA damage
    • Khosravi, R., R. Maya, T. Gottlieb, M. Oren, Y. Shiloh, and D. Shkedy. 1999. Rapid ATM-dependent phosphorylation of MDM2 precedes p53 accumulation in response to DNA damage. Proc. Natl. Acad. Sci. USA 96:14973-14977.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14973-14977
    • Khosravi, R.1    Maya, R.2    Gottlieb, T.3    Oren, M.4    Shiloh, Y.5    Shkedy, D.6
  • 43
    • 0033552595 scopus 로고    scopus 로고
    • Regulation of p53 in response to DNA damage
    • Lakin, N. D., and S. P. Jackson. 1999. Regulation of p53 in response to DNA damage. Oncogene 18:7644-7655.
    • (1999) Oncogene , vol.18 , pp. 7644-7655
    • Lakin, N.D.1    Jackson, S.P.2
  • 44
    • 0029798373 scopus 로고    scopus 로고
    • Attenuation of DNA-dependent protein kinase activity and its catalytic subunit by the herpes simplex virus type 1 transactivator ICP0
    • Lees-Miller, S. P., M. C. Long, M. A. Kilvert, V. Lam, S. A. Rice, and C. A. Spencer. 1996. Attenuation of DNA-dependent protein kinase activity and its catalytic subunit by the herpes simplex virus type 1 transactivator ICP0. J. Virol. 70:7471-7477.
    • (1996) J. Virol. , vol.70 , pp. 7471-7477
    • Lees-Miller, S.P.1    Long, M.C.2    Kilvert, M.A.3    Lam, V.4    Rice, S.A.5    Spencer, C.A.6
  • 46
    • 0037061508 scopus 로고    scopus 로고
    • Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization
    • Li, M., D. Chen, A. Shiloh, J. Luo, A. Y. Nikolaev, J. Qin, and W. Gu. 2002. Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization. Nature 416:648-653.
    • (2002) Nature , vol.416 , pp. 648-653
    • Li, M.1    Chen, D.2    Shiloh, A.3    Luo, J.4    Nikolaev, A.Y.5    Qin, J.6    Gu, W.7
  • 47
    • 0037184969 scopus 로고    scopus 로고
    • Acetylation of p53 inhibits its ubiquitination by Mdm2
    • Li, M., J. Luo, C. L. Brooks, and W. Gu. 2002. Acetylation of p53 inhibits its ubiquitination by Mdm2. J. Biol. Chem. 277:50607-50611.
    • (2002) J. Biol. Chem. , vol.277 , pp. 50607-50611
    • Li, M.1    Luo, J.2    Brooks, C.L.3    Gu, W.4
  • 48
    • 0035043465 scopus 로고    scopus 로고
    • Multiple immediate-early gene-deficient herpes simplex virus vectors allowing efficient gene delivery to neurons in culture and widespread gene delivery to the central nervous system in vivo
    • Lilley, C. E., F. Groutsi, Z. Han, J. A. Palmer, P. N. Anderson, D. S. Latchman, and R. S. Coffin. 2001. Multiple immediate-early gene-deficient herpes simplex virus vectors allowing efficient gene delivery to neurons in culture and widespread gene delivery to the central nervous system in vivo. J. Virol. 75:4343-4356.
    • (2001) J. Virol. , vol.75 , pp. 4343-4356
    • Lilley, C.E.1    Groutsi, F.2    Han, Z.3    Palmer, J.A.4    Anderson, P.N.5    Latchman, D.S.6    Coffin, R.S.7
  • 50
    • 0035937114 scopus 로고    scopus 로고
    • Degradation of nucleosome-associated centromeric histone H3-like protein CENP-A induced by herpes simplex virus type 1 protein ICP0
    • Lomonte, P., K. F. Sullivan, and R. D. Everett. 2001. Degradation of nucleosome-associated centromeric histone H3-like protein CENP-A induced by herpes simplex virus type 1 protein ICP0. J. Biol. Chem. 276:5829-5835.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5829-5835
    • Lomonte, P.1    Sullivan, K.F.2    Everett, R.D.3
  • 51
    • 0029952441 scopus 로고    scopus 로고
    • In vivo ubiquitination and proteasome-mediated degradation of p53(1)
    • Maki, C. G., J. M. Huibregtse, and P. M. Howley. 1996. In vivo ubiquitination and proteasome-mediated degradation of p53(1). Cancer Res. 56:2649-2654.
    • (1996) Cancer Res. , vol.56 , pp. 2649-2654
    • Maki, C.G.1    Huibregtse, J.M.2    Howley, P.M.3
  • 52
    • 0036893162 scopus 로고    scopus 로고
    • The Epstein-Barr virus immediate-early protein BZLF1 regulates p53 function through multiple mechanisms
    • Mauser, A., S. Saito, E. Appella, C. W. Anderson, W. T. Seaman, and S. Kenney. 2002. The Epstein-Barr virus immediate-early protein BZLF1 regulates p53 function through multiple mechanisms. J. Virol. 76:12503-12512.
    • (2002) J. Virol. , vol.76 , pp. 12503-12512
    • Mauser, A.1    Saito, S.2    Appella, E.3    Anderson, C.W.4    Seaman, W.T.5    Kenney, S.6
  • 53
    • 0030665146 scopus 로고    scopus 로고
    • Mdm-2 phosphorylation by DNA-dependent protein kinase prevents interaction with p53
    • Mayo, L. D., J. J. Turchi, and S. J. Berberich. 1997. Mdm-2 phosphorylation by DNA-dependent protein kinase prevents interaction with p53. Cancer Res. 57:5013-5016.
    • (1997) Cancer Res. , vol.57 , pp. 5013-5016
    • Mayo, L.D.1    Turchi, J.J.2    Berberich, S.J.3
  • 54
    • 0029013765 scopus 로고
    • Separation of sequence requirements for HSV-1 Vmw110 multimerisation and interaction with a 135-kDa cellular protein
    • Meredith, M., A. Orr, M. Elliott, and R. Everett. 1995. Separation of sequence requirements for HSV-1 Vmw110 multimerisation and interaction with a 135-kDa cellular protein. Virology 209:174-187.
    • (1995) Virology , vol.209 , pp. 174-187
    • Meredith, M.1    Orr, A.2    Elliott, M.3    Everett, R.4
  • 55
    • 0028268666 scopus 로고
    • Herpes simplex virus type 1 immediate-early protein Vmw110 binds strongly and specifically to a 135-kDa cellular protein
    • Meredith, M., A. Orr, and R. Everett. 1994. Herpes simplex virus type 1 immediate-early protein Vmw110 binds strongly and specifically to a 135-kDa cellular protein. Virology 200:457-469.
    • (1994) Virology , vol.200 , pp. 457-469
    • Meredith, M.1    Orr, A.2    Everett, R.3
  • 56
    • 0023150993 scopus 로고
    • Binding of the herpes simplex virus immediate-early gene product ICP4 to its own transcription start site
    • Muller, M. T. 1987. Binding of the herpes simplex virus immediate-early gene product ICP4 to its own transcription start site. J. Virol. 61:858-865.
    • (1987) J. Virol. , vol.61 , pp. 858-865
    • Muller, M.T.1
  • 57
    • 0344299239 scopus 로고    scopus 로고
    • Viral immediate-early proteins abrogate the modification by SUMO-1 of PML and Sp100 proteins, correlating with nuclear body disruption
    • Muller, S., and A. Dejean. 1999. Viral immediate-early proteins abrogate the modification by SUMO-1 of PML and Sp100 proteins, correlating with nuclear body disruption. J. Virol. 73:5137-5143.
    • (1999) J. Virol. , vol.73 , pp. 5137-5143
    • Muller, S.1    Dejean, A.2
  • 59
    • 0033779805 scopus 로고    scopus 로고
    • Alphaherpesvirus proteins related to herpes simplex virus type 1 ICP0 affect cellular structures and proteins
    • Parkinson, J., and R. D. Everett. 2000. Alphaherpesvirus proteins related to herpes simplex virus type 1 ICP0 affect cellular structures and proteins. J. Virol. 74:10006-10017.
    • (2000) J. Virol. , vol.74 , pp. 10006-10017
    • Parkinson, J.1    Everett, R.D.2
  • 60
    • 0032889431 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 immediate-early protein Vmw110 induces the proteasome-dependent degradation of the catalytic subunit of DNA-dependent protein kinase
    • Parkinson, J., S. P. Lees-Miller, and R. D. Everett. 1999. Herpes simplex virus type 1 immediate-early protein Vmw110 induces the proteasome-dependent degradation of the catalytic subunit of DNA-dependent protein kinase. J. Virol. 73:650-657.
    • (1999) J. Virol. , vol.73 , pp. 650-657
    • Parkinson, J.1    Lees-Miller, S.P.2    Everett, R.D.3
  • 62
    • 0018337950 scopus 로고
    • Control of herpes simplex virus type 1 mRNA synthesis in cells infected with wild-type virus or the temperature-sensitive mutant tsK
    • Preston, C. M. 1979. Control of herpes simplex virus type 1 mRNA synthesis in cells infected with wild-type virus or the temperature-sensitive mutant tsK. J. Virol. 29:275-284.
    • (1979) J. Virol. , vol.29 , pp. 275-284
    • Preston, C.M.1
  • 63
    • 0033767235 scopus 로고    scopus 로고
    • Multiple C-terminal lysine residues target p53 for ubiquitin-proteasome- mediated degradation
    • Rodriguez, M. S., J. M. Desterro, S. Lain, D. P. Lane, and R. T. Hay. 2000. Multiple C-terminal lysine residues target p53 for ubiquitin-proteasome- mediated degradation. Mol. Cell. Biol. 20:8458-8467.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8458-8467
    • Rodriguez, M.S.1    Desterro, J.M.2    Lain, S.3    Lane, D.P.4    Hay, R.T.5
  • 65
    • 0023409198 scopus 로고
    • Abnormal forms of the herpes simplex virus immediate early polypeptide Vmw175 induce the cellular stress response
    • Russell, J., E. C. Stow, N. D. Stow, and C. M. Preston. 1987. Abnormal forms of the herpes simplex virus immediate early polypeptide Vmw175 induce the cellular stress response. J. Gen. Virol. 68:2397-2406.
    • (1987) J. Gen. Virol. , vol.68 , pp. 2397-2406
    • Russell, J.1    Stow, E.C.2    Stow, N.D.3    Preston, C.M.4
  • 66
    • 0027358723 scopus 로고
    • The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53
    • Scheffner, M., J. M. Huibregtse, R. D. Vierstra, and P. M. Howley. 1993. The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53. Cell 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
  • 67
    • 0025639158 scopus 로고
    • The E6 oncoprotein encoded by human papillomavirus types 16 and 18 promotes the degradation of p53
    • Scheffner, M., B. A. Werness, J. M. Huibregtse, A. J. Levine, and P. M. Howley. 1990. The E6 oncoprotein encoded by human papillomavirus types 16 and 18 promotes the degradation of p53. Cell 63:1129-1136.
    • (1990) Cell , vol.63 , pp. 1129-1136
    • Scheffner, M.1    Werness, B.A.2    Huibregtse, J.M.3    Levine, A.J.4    Howley, P.M.5
  • 69
    • 0030667702 scopus 로고    scopus 로고
    • DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2
    • Shieh, S. Y., M. Ikeda, Y. Taya, and C. Prives. 1997. DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2. Cell 91:325-334.
    • (1997) Cell , vol.91 , pp. 325-334
    • Shieh, S.Y.1    Ikeda, M.2    Taya, Y.3    Prives, C.4
  • 71
    • 0141814999 scopus 로고    scopus 로고
    • Oxidative stress induces nuclear loss of DNA repair proteins Ku70 and Ku80 and apoptosis in pancreatic acinar AR42J cells
    • Song, J. Y., J. W. Lim, H. Kim, T. Morio, and K. H. Kim. 2003. Oxidative stress induces nuclear loss of DNA repair proteins Ku70 and Ku80 and apoptosis in pancreatic acinar AR42J cells. J. Biol. Chem. 278:36676-36687.
    • (2003) J. Biol. Chem. , vol.278 , pp. 36676-36687
    • Song, J.Y.1    Lim, J.W.2    Kim, H.3    Morio, T.4    Kim, K.H.5
  • 72
    • 0033771363 scopus 로고    scopus 로고
    • Global analysis of herpes simplex virus type 1 transcription using an oligonucleotide-based DNA microarray
    • Stingley, S. W., J. J. Ramirez, S. A. Aguilar, K. Simmen, R. M. Sandri-Goldin, P. Ghazal, and E. K. Wagner. 2000. Global analysis of herpes simplex virus type 1 transcription using an oligonucleotide-based DNA microarray. J. Virol. 74:9916-9927.
    • (2000) J. Virol. , vol.74 , pp. 9916-9927
    • Stingley, S.W.1    Ramirez, J.J.2    Aguilar, S.A.3    Simmen, K.4    Sandri-Goldin, R.M.5    Ghazal, P.6    Wagner, E.K.7
  • 74
    • 0022978685 scopus 로고
    • Isolation and characterization of a herpes simplex virus type 1 mutant containing a deletion within the gene encoding the immediate early polypeptide Vmw110
    • Stow, N. D., and E. C. Stow. 1986. Isolation and characterization of a herpes simplex virus type 1 mutant containing a deletion within the gene encoding the immediate early polypeptide Vmw110. J. Gen. Virol. 67:2571-2585.
    • (1986) J. Gen. Virol. , vol.67 , pp. 2571-2585
    • Stow, N.D.1    Stow, E.C.2
  • 75
    • 0037075898 scopus 로고    scopus 로고
    • Activation of the p53 tumor suppressor protein
    • Vousden, K. H. 2002. Activation of the p53 tumor suppressor protein. Biochim. Biophys. Acta 1602:47-59.
    • (2002) Biochim. Biophys. Acta , vol.1602 , pp. 47-59
    • Vousden, K.H.1
  • 76
    • 0034703742 scopus 로고    scopus 로고
    • p53: Death star
    • Vousden, K. H. 2000. p53: death star. Cell 103:691-694.
    • (2000) Cell , vol.103 , pp. 691-694
    • Vousden, K.H.1
  • 77
    • 0036674617 scopus 로고    scopus 로고
    • Live or let die: The cell's response to p53
    • Vousden, K. H., and X. Lu. 2002. Live or let die: the cell's response to p53. Nat. Rev. Cancer 2:594-604.
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 594-604
    • Vousden, K.H.1    Lu, X.2
  • 78
    • 0026062090 scopus 로고
    • Localization of p53, retinoblastoma and host replication proteins at sites of viral replication in herpes-infected cells
    • Wilcock, D., and D. P. Lane. 1991. Localization of p53, retinoblastoma and host replication proteins at sites of viral replication in herpes-infected cells. Nature 349:429-431.
    • (1991) Nature , vol.349 , pp. 429-431
    • Wilcock, D.1    Lane, D.P.2
  • 79
    • 0035835820 scopus 로고    scopus 로고
    • Regulation of p53 function
    • Woods, D. B., and K. H. Vousden. 2001. Regulation of p53 function. Exp. Cell Res. 264:56-66.
    • (2001) Exp. Cell Res. , vol.264 , pp. 56-66
    • Woods, D.B.1    Vousden, K.H.2
  • 80
    • 0035007774 scopus 로고    scopus 로고
    • p53 stimulates TFIID-TFIIA-promoter complex assembly, and p53-T-antigen complex inhibits TATA binding protein-TATA interaction
    • Xing, J., H. M. Sheppard, S. I. Corneillie, and X. Liu. 2001. p53 stimulates TFIID-TFIIA-promoter complex assembly, and p53-T-antigen complex inhibits TATA binding protein-TATA interaction. Mol. Cell. Biol. 21:3652-3661.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 3652-3661
    • Xing, J.1    Sheppard, H.M.2    Corneillie, S.I.3    Liu, X.4
  • 81
    • 0029102140 scopus 로고
    • An activity specified by the osteosarcoma line U2OS can substitute functionally for ICP0, a major regulatory protein of herpes simplex virus type 1
    • Yao, F., and P. A. Schaffer. 1995. An activity specified by the osteosarcoma line U2OS can substitute functionally for ICP0, a major regulatory protein of herpes simplex virus type 1. J. Virol. 69:6249-6258.
    • (1995) J. Virol. , vol.69 , pp. 6249-6258
    • Yao, F.1    Schaffer, P.A.2
  • 82
    • 0028268278 scopus 로고
    • Functional and physical interaction between p53 and BZLF1: Implications for Epstein-Barr virus latency
    • Zhang, Q., D. Gutsch, and S. Kenney. 1994. Functional and physical interaction between p53 and BZLF1: implications for Epstein-Barr virus latency. Mol. Cell. Biol. 14:1929-1938.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1929-1938
    • Zhang, Q.1    Gutsch, D.2    Kenney, S.3
  • 83
    • 0032549711 scopus 로고    scopus 로고
    • ARF promotes MDM2 degradation and stabilizes p53: ARF-INK4a locus deletion impairs both the Rb and p53 tumor suppression pathways
    • Zhang, Y., Y. Xiong, and W. G. Yarbrough. 1998. ARF promotes MDM2 degradation and stabilizes p53: ARF-INK4a locus deletion impairs both the Rb and p53 tumor suppression pathways. Cell 92:725-734.
    • (1998) Cell , vol.92 , pp. 725-734
    • Zhang, Y.1    Xiong, Y.2    Yarbrough, W.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.