메뉴 건너뛰기




Volumn 28, Issue 8, 2003, Pages 452-459

Viruses and the 26S proteasome: Hacking into destruction

Author keywords

[No Author keywords available]

Indexed keywords

ONCOPROTEIN; PROTEASOME; PROTEIN KINASE; PROTEIN P53; UBIQUITIN PROTEIN LIGASE; VIRUS ENZYME; VIRUS PROTEIN;

EID: 0042157103     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0004(03)00141-5     Document Type: Review
Times cited : (101)

References (79)
  • 1
    • 0035945349 scopus 로고    scopus 로고
    • A novel class of herpesvirus-encoded membrane-bound E3 ubiquitin ligases regulates endocytosis of proteins involved in immune recognition
    • Coscoy L., et al. A novel class of herpesvirus-encoded membrane-bound E3 ubiquitin ligases regulates endocytosis of proteins involved in immune recognition. J. Cell Biol. 155:2001;1265-1273.
    • (2001) J. Cell Biol. , vol.155 , pp. 1265-1273
    • Coscoy, L.1
  • 2
    • 0034754443 scopus 로고    scopus 로고
    • Rhabdoviruses and the cellular ubiquitin-proteasome system: A budding interaction
    • Harty R.N., et al. Rhabdoviruses and the cellular ubiquitin-proteasome system: a budding interaction. J. Virol. 75:2001;10623-10629.
    • (2001) J. Virol. , vol.75 , pp. 10623-10629
    • Harty, R.N.1
  • 3
    • 0033756590 scopus 로고    scopus 로고
    • Latent membrane protein 2A of Epstein-Barr virus binds WW domain E3 protein-ubiquitin ligases that ubiquitinate B-cell tyrosine kinases
    • Winberg G., et al. Latent membrane protein 2A of Epstein-Barr virus binds WW domain E3 protein-ubiquitin ligases that ubiquitinate B-cell tyrosine kinases. Mol. Cell. Biol. 20:2000;8526-8535.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8526-8535
    • Winberg, G.1
  • 4
    • 0037016045 scopus 로고    scopus 로고
    • Adenovirus protein involved in virus internalisation recruits ubiquitin-protein ligases
    • Galinier R., et al. Adenovirus protein involved in virus internalisation recruits ubiquitin-protein ligases. Biochemistry. 41:2002;14299-14305.
    • (2002) Biochemistry , vol.41 , pp. 14299-14305
    • Galinier, R.1
  • 5
    • 0034231287 scopus 로고    scopus 로고
    • Role of P30 in replication and spread of TMV
    • Beachy R.N., Heinlein M. Role of P30 in replication and spread of TMV. Traffic. 1:2000;540-544.
    • (2000) Traffic , vol.1 , pp. 540-544
    • Beachy, R.N.1    Heinlein, M.2
  • 6
    • 0037221535 scopus 로고    scopus 로고
    • Transferring substrates to the 26S proteasome
    • Petersen H., et al. Transferring substrates to the 26S proteasome. Trends Biochem. Sci. 28:2003;26-31.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 26-31
    • Petersen, H.1
  • 7
    • 0032143446 scopus 로고    scopus 로고
    • Nuclear domain 10, the site of DNA virus transcription and replication
    • Maul G.G. Nuclear domain 10, the site of DNA virus transcription and replication. Bioessays. 20:1998;660-667.
    • (1998) Bioessays , vol.20 , pp. 660-667
    • Maul, G.G.1
  • 8
    • 0029862620 scopus 로고    scopus 로고
    • Nuclear domain 10 as pre-existing potential replication start sites of herpes simplex virus type 1
    • Maul G.G., et al. Nuclear domain 10 as pre-existing potential replication start sites of herpes simplex virus type 1. Virology. 217:1996;67-75.
    • (1996) Virology , vol.217 , pp. 67-75
    • Maul, G.G.1
  • 9
    • 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., et al. The disruption of ND10 during herpes simplex virus infection correlates with the Vmw110- and proteasome-dependent loss of several PML isoforms. J. Virol. 72:1998;6581-6591.
    • (1998) J. Virol. , vol.72 , pp. 6581-6591
    • Everett, R.D.1
  • 10
    • 0033611590 scopus 로고    scopus 로고
    • Herpes virus induced proteasome-dependent degradation of the nuclear bodies-associated PML and Sp100 proteins
    • Chelbi-Alix M.K., de The H. Herpes virus induced proteasome-dependent degradation of the nuclear bodies-associated PML and Sp100 proteins. Oncogene. 18:1999;935-941.
    • (1999) Oncogene , vol.18 , pp. 935-941
    • Chelbi-Alix, M.K.1    De The, H.2
  • 11
    • 0033624137 scopus 로고    scopus 로고
    • ICP0, a regulator of herpes simplex virus during lytic and latent infection
    • Everett R.D. ICP0, a regulator of herpes simplex virus during lytic and latent infection. Bioessays. 22:2000;761-770.
    • (2000) Bioessays , vol.22 , pp. 761-770
    • Everett, R.D.1
  • 12
    • 0034266806 scopus 로고    scopus 로고
    • RING finger proteins: Mediators of ubiquitin ligase activity
    • Joazeiro C.A., Weissman A.M. RING finger proteins: mediators of ubiquitin ligase activity. Cell. 102:2000;549-552.
    • (2000) Cell , vol.102 , pp. 549-552
    • Joazeiro, C.A.1    Weissman, A.M.2
  • 13
    • 0036138854 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 immediate-early protein ICP0 and its isolated RING finger domain act as ubiquitin E3 ligases in vitro
    • Boutell C., et al. Herpes simplex virus type 1 immediate-early protein ICP0 and its isolated RING finger domain act as ubiquitin E3 ligases in vitro. J. Virol. 76:2002;841-850.
    • (2002) J. Virol. , vol.76 , pp. 841-850
    • Boutell, C.1
  • 14
    • 0030043724 scopus 로고    scopus 로고
    • Cloning of human Ub-conjugating enzymes UbcH6 and UbcH7 (E2-F1) and characterisation of their interaction with E6-AP and RSP5
    • Nuber U., et al. Cloning of human Ub-conjugating enzymes UbcH6 and UbcH7 (E2-F1) and characterisation of their interaction with E6-AP and RSP5. J. Biol. Chem. 271:1996;2795-2800.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2795-2800
    • Nuber, U.1
  • 15
    • 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., et al. 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. 73:1999;650-657.
    • (1999) J. Virol. , vol.73 , pp. 650-657
    • Parkinson, J.1
  • 16
    • 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., et al. Specific destruction of kinetochore protein CENP-C and disruption of cell division by herpes simplex virus immediate-early protein Vmw110. EMBO J. 18:1999;1526-1538.
    • (1999) EMBO J. , vol.18 , pp. 1526-1538
    • Everett, R.D.1
  • 17
    • 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., et al. Degradation of nucleosome-associated centromeric histone H3-like protein CENP-A induced by herpes simplex virus type 1 protein ICP0. J. Biol. Chem. 276:2001;5829-5835.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5829-5835
    • Lomonte, P.1
  • 18
    • 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., et al. 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. 73:1999;417-426.
    • (1999) J. Virol. , vol.73 , pp. 417-426
    • Everett, R.D.1
  • 19
    • 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., et al. A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory protein. EMBO J. 16:1997;566-577.
    • (1997) EMBO J. , vol.16 , pp. 566-577
    • Everett, R.D.1
  • 20
    • 0037061508 scopus 로고    scopus 로고
    • De-ubiquitination of p53 by HAUSP is an important pathway for p53 stabilisation
    • Li M., et al. De-ubiquitination of p53 by HAUSP is an important pathway for p53 stabilisation. Nature. 416:2002;648-653.
    • (2002) Nature , vol.416 , pp. 648-653
    • Li, M.1
  • 21
    • 0035133052 scopus 로고    scopus 로고
    • Role of Cyclin D3 in the biology of Herpes simplex virus 1 ICP0
    • Van Sant C., et al. Role of Cyclin D3 in the biology of Herpes simplex virus 1 ICP0. J. Virol. 75:2001;1888-1898.
    • (2001) J. Virol. , vol.75 , pp. 1888-1898
    • Van Sant, C.1
  • 22
    • 0026541641 scopus 로고
    • Herpesvirus saimiri encodes homologues of G protein-coupled receptor and cyclins
    • Nicholas J., et al. Herpesvirus saimiri encodes homologues of G protein-coupled receptor and cyclins. Nature. 355:1992;362-365.
    • (1992) Nature , vol.355 , pp. 362-365
    • Nicholas, J.1
  • 23
    • 0001651446 scopus 로고    scopus 로고
    • Cyclin encoded by KS herpesvirus
    • Chang Y., et al. Cyclin encoded by KS herpesvirus. Nature. 382:1996;410.
    • (1996) Nature , vol.382 , pp. 410
    • Chang, Y.1
  • 24
    • 0035902533 scopus 로고    scopus 로고
    • The infected cell protein 0 of herpes simplex virus 1 dynamically interacts with proteasomes, binds and activates the cdc34 E2 ubiquitin conjugating enzyme, and possesses in vitro E3 ubiquitin ligase activity
    • Van Sant C., et al. The infected cell protein 0 of herpes simplex virus 1 dynamically interacts with proteasomes, binds and activates the cdc34 E2 ubiquitin conjugating enzyme, and possesses in vitro E3 ubiquitin ligase activity. Proc. Natl. Acad. Sci. U. S. A. 98:2001;8815-8820.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 8815-8820
    • Van Sant, C.1
  • 25
    • 0032530151 scopus 로고    scopus 로고
    • Human CUL-1 associates with the SKP1/SKP2 complex and regulates p21 (CIP1/WAF1) and cyclin D proteins
    • Yu Z.K., et al. Human CUL-1 associates with the SKP1/SKP2 complex and regulates p21 (CIP1/WAF1) and cyclin D proteins. Proc. Natl. Acad. Sci. U. S. A. 95:1998;11324-11329.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 11324-11329
    • Yu, Z.K.1
  • 26
    • 0028352769 scopus 로고
    • The nuclear location of PML, a cellular member of the C3HC4 zinc-binding domain protein family, is rearranged during herpes simplex virus infection by the C3HC4 protein ICP0
    • Maul G.G., Everett R.D. The nuclear location of PML, a cellular member of the C3HC4 zinc-binding domain protein family, is rearranged during herpes simplex virus infection by the C3HC4 protein ICP0. J. Gen. Virol. 75:1994;1223-1233.
    • (1994) J. Gen. Virol. , vol.75 , pp. 1223-1233
    • Maul, G.G.1    Everett, R.D.2
  • 27
    • 0026560315 scopus 로고
    • Inhibition of p53 transactivation required for transformation by adenovirus early 1B protein
    • Yew P.R., Berk A.J. Inhibition of p53 transactivation required for transformation by adenovirus early 1B protein. Nature. 357:1992;82-85.
    • (1992) Nature , vol.357 , pp. 82-85
    • Yew, P.R.1    Berk, A.J.2
  • 28
    • 0029907816 scopus 로고    scopus 로고
    • Oncogenic potential of the adenovirus E4orf6 protein
    • Moore M., et al. Oncogenic potential of the adenovirus E4orf6 protein. Proc. Natl. Acad. Sci. U. S. A. 93:1996;11295-11301.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 11295-11301
    • Moore, M.1
  • 29
    • 0020079972 scopus 로고
    • Adenovirus E1B 58 kD tumor antigen and SV40 large tumour antigen are physically associated with the same 54 kD cellular protein in transformed cells
    • Sarnow P., et al. Adenovirus E1B 58 kD tumor antigen and SV40 large tumour antigen are physically associated with the same 54 kD cellular protein in transformed cells. Cell. 28:1982;387-394.
    • (1982) Cell , vol.28 , pp. 387-394
    • Sarnow, P.1
  • 30
    • 0030001373 scopus 로고    scopus 로고
    • Blockage by adenovirus E4orf6 of transcriptional activation by the p53 tumor suppressor
    • Dobner T., et al. Blockage by adenovirus E4orf6 of transcriptional activation by the p53 tumor suppressor. Science. 272:1996;1470-1473.
    • (1996) Science , vol.272 , pp. 1470-1473
    • Dobner, T.1
  • 31
    • 0025251915 scopus 로고
    • Domains required for in vitro association between the cellular p53 and the adenovirus 2 E1B 55K proteins
    • Kao C.C., et al. Domains required for in vitro association between the cellular p53 and the adenovirus 2 E1B 55K proteins. Virology. 179:1990;806-814.
    • (1990) Virology , vol.179 , pp. 806-814
    • Kao, C.C.1
  • 32
    • 0032556920 scopus 로고    scopus 로고
    • The large E1B protein together with the E4orf6 protein target p53 for active degradation in adenovirus infected cells
    • Steegenga W.T., et al. The large E1B protein together with the E4orf6 protein target p53 for active degradation in adenovirus infected cells. Oncogene. 16:1998;349-357.
    • (1998) Oncogene , vol.16 , pp. 349-357
    • Steegenga, W.T.1
  • 33
    • 0032926836 scopus 로고    scopus 로고
    • Analysis of synthesis, stability, phosphorylation, and interacting polypeptides of the 34-kilodalton product of open reading frame 6 of the early region 4 protein of human adenovirus type 5
    • Boivin D., et al. Analysis of synthesis, stability, phosphorylation, and interacting polypeptides of the 34-kilodalton product of open reading frame 6 of the early region 4 protein of human adenovirus type 5. J. Virol. 73:1999;1245-1253.
    • (1999) J. Virol. , vol.73 , pp. 1245-1253
    • Boivin, D.1
  • 34
    • 0035577765 scopus 로고    scopus 로고
    • Degradation of p53 by adenovirus E4orf6 and E1B55k proteins occurs via a novel mechanism involving a Cullin-containing complex
    • Querido E., et al. degradation of p53 by adenovirus E4orf6 and E1B55k proteins occurs via a novel mechanism involving a Cullin-containing complex. Genes Dev. 15:2001;3104-3117.
    • (2001) Genes Dev. , vol.15 , pp. 3104-3117
    • Querido, E.1
  • 35
    • 0036720983 scopus 로고    scopus 로고
    • Analysis of the adenovirus E1B-55k-anchored proteome reveals its link to ubiquitination machinery
    • Harada J.N., et al. Analysis of the adenovirus E1B-55k-anchored proteome reveals its link to ubiquitination machinery. J. Virol. 76:2002;9194-9206.
    • (2002) J. Virol. , vol.76 , pp. 9194-9206
    • Harada, J.N.1
  • 36
    • 0033565672 scopus 로고    scopus 로고
    • The von Hippel-Lindau tumour suppressor protein is a component of an E3 ubiquitin-protein ligase activity
    • Lisztwan J., et al. The von Hippel-Lindau tumour suppressor protein is a component of an E3 ubiquitin-protein ligase activity. Genes Dev. 13:1999;1822-1833.
    • (1999) Genes Dev. , vol.13 , pp. 1822-1833
    • Lisztwan, J.1
  • 37
    • 0034641615 scopus 로고    scopus 로고
    • Activation of HIF1α ubiquitination by a reconstituted von Hippel-Lindau (VHL) tumour suppressor complex
    • Kamura T., et al. Activation of HIF1α ubiquitination by a reconstituted von Hippel-Lindau (VHL) tumour suppressor complex. Proc. Natl. Acad. Sci. U. S. A. 97:2000;10430-10435.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 10430-10435
    • Kamura, T.1
  • 38
    • 0031831274 scopus 로고    scopus 로고
    • Combinatorial control in ubiquitin-dependent proteolysis: Don't skp the F-box hypothesis
    • Patton E.E., et al. Combinatorial control in ubiquitin-dependent proteolysis: Don't skp the F-box hypothesis. Trends Genet. 14:1998;236-243.
    • (1998) Trends Genet. , vol.14 , pp. 236-243
    • Patton, E.E.1
  • 39
    • 0036195134 scopus 로고    scopus 로고
    • An intact NEDD8 pathway is required for Cullin-dependent ubiquitylation in mammalian cells
    • Ohh M., et al. An intact NEDD8 pathway is required for Cullin-dependent ubiquitylation in mammalian cells. EMBO Rep. 3:2002;177-182.
    • (2002) EMBO Rep. , vol.3 , pp. 177-182
    • Ohh, M.1
  • 40
    • 0033552585 scopus 로고    scopus 로고
    • The role of the E6-p53 interaction in the molecular pathogenesis of the HPV
    • Thomas M., et al. The role of the E6-p53 interaction in the molecular pathogenesis of the HPV. Oncogene. 18:1999;7690-7700.
    • (1999) Oncogene , vol.18 , pp. 7690-7700
    • Thomas, M.1
  • 41
    • 0037328861 scopus 로고    scopus 로고
    • Angelman syndrome: A review of the clinical and genetic aspects
    • Clayton-Smith J., Laan L. Angelman syndrome: a review of the clinical and genetic aspects. J. Med. Genet. 40:2003;87-95.
    • (2003) J. Med. Genet. , vol.40 , pp. 87-95
    • Clayton-Smith, J.1    Laan, L.2
  • 42
    • 0028898424 scopus 로고
    • Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade
    • Scheffner M., et al. Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade. Nature. 373:1995;81-83.
    • (1995) Nature , vol.373 , pp. 81-83
    • Scheffner, M.1
  • 43
    • 0028907874 scopus 로고
    • A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase
    • Huibregtse J.M., et al. A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase. Proc. Natl. Acad. Sci. U. S. A. 92:1995;2563-2567.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 2563-2567
    • Huibregtse, J.M.1
  • 44
    • 0032741446 scopus 로고    scopus 로고
    • Structure of an E6AP-UbcH7 complex: Insights into ubiquitination by the E2-E3 enzyme cascade
    • Huang L., et al. Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade. Science. 286:1999;1321-1326.
    • (1999) Science , vol.286 , pp. 1321-1326
    • Huang, L.1
  • 45
    • 0030908874 scopus 로고    scopus 로고
    • Physical interaction between specific E2 and Hect E3 enzymes determines functional cooperativity
    • Kumar S., et al. Physical interaction between specific E2 and Hect E3 enzymes determines functional cooperativity. J. Biol. Chem. 272:1997;13548-13554.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13548-13554
    • Kumar, S.1
  • 46
    • 0031984523 scopus 로고    scopus 로고
    • The identification of a conserved binding motif within human papillomavirus type 16 E6 binding peptides, E6AP and E6BP
    • Elston R.C., et al. The identification of a conserved binding motif within human papillomavirus type 16 E6 binding peptides, E6AP and E6BP. J. Gen. Virol. 79:1998;371-374.
    • (1998) J. Gen. Virol. , vol.79 , pp. 371-374
    • Elston, R.C.1
  • 47
    • 0031058283 scopus 로고    scopus 로고
    • Antisense targeting of E6-AP elevates p53 in HPV-infected cells but not in normal cells
    • Beer-Romero P., et al. Antisense targeting of E6-AP elevates p53 in HPV-infected cells but not in normal cells. Oncogene. 14:1997;595-602.
    • (1997) Oncogene , vol.14 , pp. 595-602
    • Beer-Romero, P.1
  • 48
    • 0032513114 scopus 로고    scopus 로고
    • The role of E6AP in the regulation of p53 protein levels in human papillomavirus (HPV)-positive and HPV-negative cells
    • Talis A.L., et al. The role of E6AP in the regulation of p53 protein levels in human papillomavirus (HPV)-positive and HPV-negative cells. J. Biol. Chem. 273:1998;6439-6445.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6439-6445
    • Talis, A.L.1
  • 49
    • 0034612296 scopus 로고    scopus 로고
    • Induction of apoptosis in human papillomavirus-positive cancer cells by peptide aptamers targeting the viral E6 oncoprotein
    • Butz K., et al. Induction of apoptosis in human papillomavirus-positive cancer cells by peptide aptamers targeting the viral E6 oncoprotein. Proc. Natl. Acad. Sci. U. S. A. 97:2000;6693-6697.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 6693-6697
    • Butz, K.1
  • 50
    • 0031583962 scopus 로고    scopus 로고
    • Oncoprotein MDM2 is a ubiquitin ligase E3 for tumour suppressor p53
    • Honda R., et al. Oncoprotein MDM2 is a ubiquitin ligase E3 for tumour suppressor p53. FEBS Lett. 420:1997;25-27.
    • (1997) FEBS Lett. , vol.420 , pp. 25-27
    • Honda, R.1
  • 51
    • 0035970025 scopus 로고    scopus 로고
    • Complete switch from Mdm2 to human papillomavirus E6-mediated degradation of p53 in cervical cancer cells
    • Hengstermann A., et al. Complete switch from Mdm2 to human papillomavirus E6-mediated degradation of p53 in cervical cancer cells. Proc. Natl. Acad. Sci. U. S. A. 98:2001;1218-1223.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 1218-1223
    • Hengstermann, A.1
  • 52
    • 0035794541 scopus 로고    scopus 로고
    • COP9 signalosome-specific phosphorylation targets p53 to degradation by the ubiquitin system
    • Bech-Otschir D., et al. COP9 signalosome-specific phosphorylation targets p53 to degradation by the ubiquitin system. EMBO J. 20:2001;1630-1639.
    • (2001) EMBO J. , vol.20 , pp. 1630-1639
    • Bech-Otschir, D.1
  • 53
    • 0033919402 scopus 로고    scopus 로고
    • Human papillomavirus type 16 E6 induces self-ubiquitination of the E6-AP ubiquitin protein ligase
    • Kao W.H., et al. Human papillomavirus type 16 E6 induces self-ubiquitination of the E6-AP ubiquitin protein ligase. J. Virol. 74:2000;6408-6417.
    • (2000) J. Virol. , vol.74 , pp. 6408-6417
    • Kao, W.H.1
  • 54
    • 0032506698 scopus 로고    scopus 로고
    • Inhibition of Bak-induced apoptosis by HPV-18 E6
    • Thomas M., Banks L. Inhibition of Bak-induced apoptosis by HPV-18 E6. Oncogene. 17:1998;2943-2954.
    • (1998) Oncogene , vol.17 , pp. 2943-2954
    • Thomas, M.1    Banks, L.2
  • 55
    • 0036606329 scopus 로고    scopus 로고
    • Human papillomavirus E6-induced degradation of E6TP1 is mediated by E6AP ubiquitin ligase
    • Gao Q., et al. Human papillomavirus E6-induced degradation of E6TP1 is mediated by E6AP ubiquitin ligase. Cancer Res. 62:2002;3315-3321.
    • (2002) Cancer Res. , vol.62 , pp. 3315-3321
    • Gao, Q.1
  • 56
    • 0033776810 scopus 로고    scopus 로고
    • Human scribble (Vartul) is targeted for ubiquitin-mediated degradation by the high-risk papillomavirus E6 proteins and the E6AP ubiquitin-protein ligase
    • Nakagawa S., Huibregtse J.M. Human scribble (Vartul) is targeted for ubiquitin-mediated degradation by the high-risk papillomavirus E6 proteins and the E6AP ubiquitin-protein ligase. Mol. Cell. Biol. 20:2000;8244-8253.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8244-8253
    • Nakagawa, S.1    Huibregtse, J.M.2
  • 57
    • 0037194597 scopus 로고    scopus 로고
    • The DNA repair protein, O(6)-methylguanine-DNA methyltransferase is a proteolytic target for the E6 human papillomavirus oncoprotein
    • Srivenugopal K.S., Ali-Osman F. The DNA repair protein, O(6)-methylguanine-DNA methyltransferase is a proteolytic target for the E6 human papillomavirus oncoprotein. Oncogene. 21:2002;5940-5945.
    • (2002) Oncogene , vol.21 , pp. 5940-5945
    • Srivenugopal, K.S.1    Ali-Osman, F.2
  • 58
    • 0033578418 scopus 로고    scopus 로고
    • Regulation of the Src family tyrosine kinase Blk through E6AP-mediated degradation
    • Oda H., et al. Regulation of the Src family tyrosine kinase Blk through E6AP-mediated degradation. Proc. Natl. Acad. Sci. U. S. A. 96:1999;9557-9562.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 9557-9562
    • Oda, H.1
  • 59
    • 0033603339 scopus 로고    scopus 로고
    • Identification of HHR23A as a substrate for E6-associated protein-mediated ubiquitination
    • Kumar S., et al. Identification of HHR23A as a substrate for E6-associated protein-mediated ubiquitination. J. Biol. Chem. 274:1999;18785-18792.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18785-18792
    • Kumar, S.1
  • 60
    • 0028358885 scopus 로고
    • Mutational analysis of HPV-18 E6 identifies domains required for p53 degradation in vitro, abolition of p53 transactivation in vivo and immortalisation of primary BMK cells
    • Pim D., et al. Mutational analysis of HPV-18 E6 identifies domains required for p53 degradation in vitro, abolition of p53 transactivation in vivo and immortalisation of primary BMK cells. Oncogene. 9:1994;1869-1876.
    • (1994) Oncogene , vol.9 , pp. 1869-1876
    • Pim, D.1
  • 61
    • 0036891825 scopus 로고    scopus 로고
    • A mutant of human papillomavirus type 16 E6 deficient in binding α-helix partners displays reduced oncogenic potential in vivo
    • Nguyen M., et al. A mutant of human papillomavirus type 16 E6 deficient in binding α-helix partners displays reduced oncogenic potential in vivo. J. Virol. 76:2002;13039-13048.
    • (2002) J. Virol. , vol.76 , pp. 13039-13048
    • Nguyen, M.1
  • 62
    • 0030950410 scopus 로고    scopus 로고
    • Binding of human virus oncoproteins to hDlg/SAP97, a mammalian homolog of the Drosophila discs large tumor suppressor protein
    • Lee S.S., et al. Binding of human virus oncoproteins to hDlg/SAP97, a mammalian homolog of the Drosophila discs large tumor suppressor protein. Proc. Natl. Acad. Sci. U. S. A. 94:1997;6670-6675.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 6670-6675
    • Lee, S.S.1
  • 63
    • 0033619139 scopus 로고    scopus 로고
    • Oncogenic human papillomavirus E6 proteins target the discs large tumour suppressor for proteasome-mediated degradation
    • Gardiol D., et al. Oncogenic human papillomavirus E6 proteins target the discs large tumour suppressor for proteasome-mediated degradation. Oncogene. 18:1999;5487-5496.
    • (1999) Oncogene , vol.18 , pp. 5487-5496
    • Gardiol, D.1
  • 64
    • 0034597533 scopus 로고    scopus 로고
    • Interactions of the PDZ-protein MAGI-1 with adenovirus E4-ORF1 and high-risk papillomavirus E6 oncoproteins
    • Glaunsinger B., et al. Interactions of the PDZ-protein MAGI-1 with adenovirus E4-ORF1 and high-risk papillomavirus E6 oncoproteins. Oncogene. 19:2000;1093-1098.
    • (2000) Oncogene , vol.19 , pp. 1093-1098
    • Glaunsinger, B.1
  • 65
    • 0036676836 scopus 로고    scopus 로고
    • Oncogenic human papillomavirus E6 proteins target the MAGI-2 and MAGI-3 proteins for degradation
    • Thomas M., et al. Oncogenic human papillomavirus E6 proteins target the MAGI-2 and MAGI-3 proteins for degradation. Oncogene. 21:2002;5088-5096.
    • (2002) Oncogene , vol.21 , pp. 5088-5096
    • Thomas, M.1
  • 66
    • 0036369804 scopus 로고    scopus 로고
    • Genetic studies define MAGUK proteins as regulators of epithelial cell polarity
    • Caruana G. Genetic studies define MAGUK proteins as regulators of epithelial cell polarity. Int. J. Dev. Biol. 46:2002;511-518.
    • (2002) Int. J. Dev. Biol. , vol.46 , pp. 511-518
    • Caruana, G.1
  • 67
    • 0034617129 scopus 로고    scopus 로고
    • Cooperative regulation of cell polarity and growth by Drosophila tumor suppressors
    • Bilder D., et al. Cooperative regulation of cell polarity and growth by Drosophila tumor suppressors. Science. 289:2000;113-116.
    • (2000) Science , vol.289 , pp. 113-116
    • Bilder, D.1
  • 68
    • 0034628567 scopus 로고    scopus 로고
    • HPV E6 targeted degradation of the discs large protein: Evidence for the involvement of a novel ubiquitin ligase
    • Pim D., et al. HPV E6 targeted degradation of the discs large protein: evidence for the involvement of a novel ubiquitin ligase. Oncogene. 19:2000;719-725.
    • (2000) Oncogene , vol.19 , pp. 719-725
    • Pim, D.1
  • 69
    • 0037153381 scopus 로고    scopus 로고
    • Chimaeric HPV E6 proteins allow dissection of the proteolytic pathways regulating different E6 cellular target proteins
    • Pim D., et al. Chimaeric HPV E6 proteins allow dissection of the proteolytic pathways regulating different E6 cellular target proteins. Oncogene. 21:2002;8140-8148.
    • (2002) Oncogene , vol.21 , pp. 8140-8148
    • Pim, D.1
  • 70
    • 0035956258 scopus 로고    scopus 로고
    • Biological activities and molecular targets of the human papillomavirus E7 oncoprotein
    • Münger K., et al. Biological activities and molecular targets of the human papillomavirus E7 oncoprotein. Oncogene. 20:2001;7888-7898.
    • (2001) Oncogene , vol.20 , pp. 7888-7898
    • Münger, K.1
  • 71
    • 0029834371 scopus 로고    scopus 로고
    • E7 protein of human papillomavirus-16 induces degradation of retinoblastoma protein through the ubiquitin-proteasome pathway
    • Boyer S.N., et al. E7 protein of human papillomavirus-16 induces degradation of retinoblastoma protein through the ubiquitin-proteasome pathway. Cancer Res. 56:1996;4620-4624.
    • (1996) Cancer Res. , vol.56 , pp. 4620-4624
    • Boyer, S.N.1
  • 72
    • 0030728767 scopus 로고    scopus 로고
    • The human papillomavirus E7 oncoprotein functionally interacts with the S4 subunit of the 26S proteasome
    • Berezutskaya E., Bagchi S. The human papillomavirus E7 oncoprotein functionally interacts with the S4 subunit of the 26S proteasome. J. Biol. Chem. 272:1997;30135-30140.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30135-30140
    • Berezutskaya, E.1    Bagchi, S.2
  • 73
    • 0037213921 scopus 로고    scopus 로고
    • Ubiquitin-dependent proteolysis of Cyclin D1 is associated with coxsackievirus-induced cell growth arrest
    • Luo H., et al. Ubiquitin-dependent proteolysis of Cyclin D1 is associated with coxsackievirus-induced cell growth arrest. J. Virol. 77:2003;1-9.
    • (2003) J. Virol. , vol.77 , pp. 1-9
    • Luo, H.1
  • 74
    • 0037373383 scopus 로고    scopus 로고
    • Human cytomegalovirus pp71 stimulates cell cycle progression by inducing the proteasome-dependent degradation of the retinoblastoma family of tumor suppressors
    • Kalejta R.F., et al. Human cytomegalovirus pp71 stimulates cell cycle progression by inducing the proteasome-dependent degradation of the retinoblastoma family of tumor suppressors. Mol. Cell. Biol. 23:2003;1885-1895.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 1885-1895
    • Kalejta, R.F.1
  • 75
    • 0035988010 scopus 로고    scopus 로고
    • The HCMV gene products US2 and US11 target MHC class I molecules for degradation in the cytosol
    • van der Wal F.J., et al. The HCMV gene products US2 and US11 target MHC class I molecules for degradation in the cytosol. Curr. Top. Microbiol. Immunol. 269:2002;37-55.
    • (2002) Curr. Top. Microbiol. Immunol. , vol.269 , pp. 37-55
    • Van der Wal, F.J.1
  • 76
    • 0036847601 scopus 로고    scopus 로고
    • Paramyxovirus strategies for evading the interferon response
    • Gotoh B., et al. Paramyxovirus strategies for evading the interferon response. Rev. Med. Virol. 12:2002;337-357.
    • (2002) Rev. Med. Virol. , vol.12 , pp. 337-357
    • Gotoh, B.1
  • 77
    • 0037228216 scopus 로고    scopus 로고
    • The PHD/LAP-domain protein M153R of myxomavirus is a ubiquitin ligase that induces the rapid internalisation and lysosomal destruction of CD4
    • Mansouri M., et al. The PHD/LAP-domain protein M153R of myxomavirus is a ubiquitin ligase that induces the rapid internalisation and lysosomal destruction of CD4. J. Virol. 77:2003;1427-1440.
    • (2003) J. Virol. , vol.77 , pp. 1427-1440
    • Mansouri, M.1
  • 78
    • 0037303193 scopus 로고    scopus 로고
    • Overlapping motifs (PTAP and PPEY) within the Ebola virus VP40 protein function independently as late budding domains: Involvement of host proteins TSG101 and VPS-4
    • Licata J.M., et al. Overlapping motifs (PTAP and PPEY) within the Ebola virus VP40 protein function independently as late budding domains: involvement of host proteins TSG101 and VPS-4. J. Virol. 77:2003;1812-1819.
    • (2003) J. Virol. , vol.77 , pp. 1812-1819
    • Licata, J.M.1
  • 79
    • 0036023945 scopus 로고    scopus 로고
    • Functional involvement of a novel Nedd4-like ubiquitin ligase on retrovirus budding
    • Yasuda J., et al. Functional involvement of a novel Nedd4-like ubiquitin ligase on retrovirus budding. EMBO Rep. 3:2002;636-640.
    • (2002) EMBO Rep. , vol.3 , pp. 636-640
    • Yasuda, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.