메뉴 건너뛰기




Volumn 87, Issue 15, 2013, Pages 8675-8686

Pyrrolidine dithiocarbamate inhibits herpes simplex virus 1 and 2 replication, and its activity may be mediated through dysregulation of the ubiquitin-proteasome system

Author keywords

[No Author keywords available]

Indexed keywords

26S PROTEASOME; CELL PROTEIN; I KAPPA B ALPHA; IMMEDIATE EARLY PROTEIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; PROMYELOCYTIC LEUKEMIA PROTEIN; PROTEASOME; PYRROLIDINE DITHIOCARBAMATE; REACTIVE OXYGEN METABOLITE; UBIQUITIN; UNCLASSIFIED DRUG; ZINC ION;

EID: 84880600373     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00869-13     Document Type: Article
Times cited : (21)

References (80)
  • 1
    • 84880608075 scopus 로고    scopus 로고
    • Herpesviruses
    • In Ryan KJ, Ray CG , 5th ed McGraw Hill Medical, New York, NY
    • Ahmad N, Ray CG, Drew WL. 2011. Chapter 14. Herpesviruses, p 247-270. In Ryan KJ, Ray CG (ed), Sherris medical microbiology, 5th ed.McGraw Hill Medical, New York, NY.
    • (2011) Sherris medical microbiology , pp. 247-270
    • Ahmad, N.1    Ray, C.G.2    Drew, W.L.3
  • 2
    • 34247479968 scopus 로고    scopus 로고
    • The role of herpes simplex virus type 2 and other genital infections in the acquisition of HIV-1 among high-risk women in northern Tanzania
    • Kapiga SH, Sam NE, Bang H, Ni Q, Ao TTH, Kiwelu I, Chiduo S, Ndibe U, Seage G, Coplan P. 2007. The role of herpes simplex virus type 2 and other genital infections in the acquisition of HIV-1 among high-risk women in northern Tanzania. J. Infect. Dis. 195:1260-1269.
    • (2007) J. Infect. Dis. , vol.195 , pp. 1260-1269
    • Kapiga, S.H.1    Sam, N.E.2    Bang, H.3    Ni, Q.4    Ao, T.T.H.5    Kiwelu, I.6    Chiduo, S.7    Ndibe, U.8    Seage, G.9    Coplan, P.10
  • 4
    • 47849119723 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 in Alzheimer's disease: the enemy within
    • Itzhaki RF, Wozniak MA. 2008. Herpes simplex virus type 1 in Alzheimer's disease: the enemy within. J. Alzheimers Dis. 13:393-405.
    • (2008) J. Alzheimers Dis. , vol.13 , pp. 393-405
    • Itzhaki, R.F.1    Wozniak, M.A.2
  • 5
    • 71449097274 scopus 로고    scopus 로고
    • Role of infection in the pathogenesis of Alzheimers disease: implications for treatment
    • Holmes C, Cotterell D. 2009. Role of infection in the pathogenesis of Alzheimers disease: implications for treatment. CNS Drugs 23:993-1002.
    • (2009) CNS Drugs , vol.23 , pp. 993-1002
    • Holmes, C.1    Cotterell, D.2
  • 6
    • 0037232666 scopus 로고    scopus 로고
    • Redox-regulated mechanisms of IL-4-induced MCP-1 expression in human vascular endothelial cells.
    • Lee YW, Hennig B, Toborek M. 2003. Redox-regulated mechanisms of IL-4-induced MCP-1 expression in human vascular endothelial cells. Am.J. Physiol. Heart Circ. Physiol. 284:H185-H192.
    • (2003) Am.J. Physiol. Heart Circ. Physiol , vol.284
    • Lee, Y.W.1    Hennig, B.2    Toborek, M.3
  • 7
    • 20744441360 scopus 로고    scopus 로고
    • Pyrrolidine dithiocarbamate reduces coxsackievirus B3 replication through inhibition of the ubiquitin-proteasome pathway
    • Si X, McManus BM, Zhang J, Yuan J, Cheung C, Esfandiarei M, Suarez A, Morgan A, Luo H. 2005. Pyrrolidine dithiocarbamate reduces coxsackievirus B3 replication through inhibition of the ubiquitin-proteasome pathway. J. Virol. 79:8014-8023.
    • (2005) J. Virol , vol.79 , pp. 8014-8023
    • Si, X.1    McManus, B.M.2    Zhang, J.3    Yuan, J.4    Cheung, C.5    Esfandiarei, M.6    Suarez, A.7    Morgan, A.8    Luo, H.9
  • 8
    • 0036111639 scopus 로고    scopus 로고
    • Antiviral effects of pyrrolidine dithiocarbamate on human rhinoviruses
    • Gaudernak E, Seipelt J, Triendl A, Grassauer A, Kuechler E. 2002.Antiviral effects of pyrrolidine dithiocarbamate on human rhinoviruses. J.Virol. 76:6004-6015.
    • (2002) J.Virol , vol.76 , pp. 6004-6015
    • Gaudernak, E.1    Seipelt, J.2    Triendl, A.3    Grassauer, A.4    Kuechler, E.5
  • 10
    • 0026590541 scopus 로고
    • Dithiocarbamates as potent inhibitors of nuclear factor kappa B activation in intact cells
    • Schreck R, Meier B, Männel DN, Dräge W, Baeuerle PA. 1992. Dithiocarbamates as potent inhibitors of nuclear factor kappa B activation in intact cells. J. Exp. Med. 175:1181-1194.
    • (1992) J. Exp. Med. , vol.175 , pp. 1181-1194
    • Schreck, R.1    Meier, B.2    Männel, D.N.3    Dräge, W.4    Baeuerle, P.A.5
  • 14
    • 0242718916 scopus 로고    scopus 로고
    • Novel biphasic effect of pyrrolidine dithiocarbamate on neuronal cell viability is mediated by the differential regulation of intracellular zinc and copper ion levels, NFΚb, and MAP kinases.
    • Chung KC, Park JH, Kim CH, Lee HW, Sato N, Uchiyama Y, Ahn YS.2000. Novel biphasic effect of pyrrolidine dithiocarbamate on neuronal cell viability is mediated by the differential regulation of intracellular zinc and copper ion levels, NFΚ b, and MAP kinases. J. Neurosci. Res. 59:117-125.
    • (2000) J. Neurosci. Res. , vol.59 , pp. 117-125
    • Chung, K.C.1    Park, J.H.2    Kim, C.H.3    Lee, H.W.4    Sato, N.5    Uchiyama, Y.6    Ahn, Y.S.7
  • 16
    • 0028234770 scopus 로고
    • Distinct 19 S and 20 S subcomplexes of the 26 S proteasome and their distribution in the nucleus and the cytoplasm.
    • Peters J, Franke W, Kleinschmidt J. 1994. Distinct 19 S and 20 S subcomplexes of the 26 S proteasome and their distribution in the nucleus and the cytoplasm. J. Biol. Chem. 269:7709-7718.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7709-7718
    • Peters, J.1    Franke, W.2    Kleinschmidt, J.3
  • 17
    • 33847066706 scopus 로고    scopus 로고
    • Functions of the proteasome: from protein degradation and immune surveillance to cancer therapy
    • Goldberg A. 2007. Functions of the proteasome: from protein degradation and immune surveillance to cancer therapy. Biochem. Soc. Trans.35:12-17.
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 12-17
    • Goldberg, A.1
  • 18
    • 0842303313 scopus 로고    scopus 로고
    • Back to the future with ubiquitin
    • Pickart CM. 2004. Back to the future with ubiquitin. Cell 116:181-190.
    • (2004) Cell , vol.116 , pp. 181-190
    • Pickart, C.M.1
  • 19
    • 0042157103 scopus 로고    scopus 로고
    • Viruses and the 26S proteasome:hacking into destruction
    • Banks L, Pim D, Thomas M. 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    Pim, D.2    Thomas, M.3
  • 20
    • 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, Sadis S, Everett RD. 2002. Herpes simplex virus type 1 immediate-early protein ICP0 and its isolated RING finger domain act as ubiquitin E3 ligases in vitro. J. Virol. 76:841-850.
    • (2002) J. Virol. , vol.76 , pp. 841-850
    • Boutell, C.1    Sadis, S.2    Everett, R.D.3
  • 21
    • 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
    • U.S.A
    • Van Sant C, Hagglund R, Lopez P, Roizman B. 2001. 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. 98:8815-8820.
    • (2001) Proc. Natl. Acad. Sci. , vol.98 , pp. 8815-8820
    • Van Sant, C.1    Hagglund, R.2    Lopez, P.3    Roizman, B.4
  • 22
    • 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, Orr A, Everett RD. 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
  • 23
    • 33746827706 scopus 로고    scopus 로고
    • PML contributes to a cellular mechanism of repression of herpes simplex virus type 1 infection that is inactivated by ICP0
    • Everett RD, Rechter S, Papior P, Tavalai N, Stamminger T, Orr A. 2006.PML contributes to a cellular mechanism of repression of herpes simplex virus type 1 infection that is inactivated by ICP0. J. Virol. 80:7995-8005.
    • (2006) J. Virol. , vol.80 , pp. 7995-8005
    • Everett, R.D.1    Rechter, S.2    Papior, P.3    Tavalai, N.4    Stamminger, T.5    Orr, A.6
  • 24
    • 0033611590 scopus 로고    scopus 로고
    • Herpes virus induced proteasome-dependent degradation of the nuclear bodies-associated PML and Sp100 proteins
    • Chelbi-Alix MK. 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
  • 25
    • 33846881608 scopus 로고    scopus 로고
    • Centromeric protein CENP-B proteasomal degradation induced by the viral protein ICP0
    • Lomonte P, Morency E. 2007. Centromeric protein CENP-B proteasomal degradation induced by the viral protein ICP0. FEBS Lett. 581:658-662.
    • (2007) FEBS Lett. , vol.581 , pp. 658-662
    • Lomonte, P.1    Morency, E.2
  • 26
    • 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 RD, Earnshaw WC, Findlay J, Lomonte P. 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
  • 27
    • 0035937114 scopus 로고    scopus 로고
    • Degradation of nucleosomeassociated centromeric histone H3-like protein CENP-A induced by herpes simplex virus type 1 protein ICP0
    • Lomonte P, Sullivan KF, Everett RD. 2001. Degradation of nucleosomeassociated 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
  • 28
    • 79952584958 scopus 로고    scopus 로고
    • The herpes simplex virus immediate-early ubiquitin ligase ICP0 induces degradation of the ICP0 repressor protein E2FBP1
    • Fukuyo Y, Horikoshi N, Ishov AM, Silverstein SJ, Nakajima T. 2011.The herpes simplex virus immediate-early ubiquitin ligase ICP0 induces degradation of the ICP0 repressor protein E2FBP1. J. Virol. 85:3356-3366.
    • (2011) J. Virol , vol.85 , pp. 3356-3366
    • Fukuyo, Y.1    Horikoshi, N.2    Ishov, A.M.3    Silverstein, S.J.4    Nakajima, T.5
  • 29
    • 41149153281 scopus 로고    scopus 로고
    • Cellular proteasome activity facilitates herpes simplex virus entry at a postpenetration step
    • Delboy MG, Roller DG, Nicola AV. 2008. Cellular proteasome activity facilitates herpes simplex virus entry at a postpenetration step. J. Virol.82:3381-3390.
    • (2008) J. Virol. , vol.82 , pp. 3381-3390
    • Delboy, M.G.1    Roller, D.G.2    Nicola, A.V.3
  • 30
    • 79958126321 scopus 로고    scopus 로고
    • A pre-immediate-early role for tegument ICP0 in the proteasome-dependent entry of herpes simplex virus
    • Delboy MG, Nicola AV. 2011. A pre-immediate-early role for tegument ICP0 in the proteasome-dependent entry of herpes simplex virus. J. Virol.85:5910-5918.
    • (2011) J. Virol. , vol.85 , pp. 5910-5918
    • Delboy, M.G.1    Nicola, A.V.2
  • 31
    • 0036888327 scopus 로고    scopus 로고
    • Effect of antioxidants on apoptosis induced by influenza virus infection: inhibition of viral gene replication and transcription with pyrrolidine dithiocarbamate
    • Uchide N, Ohyama K, Bessho T, Yuan B, Yamakawa T. 2002. Effect of antioxidants on apoptosis induced by influenza virus infection: inhibition of viral gene replication and transcription with pyrrolidine dithiocarbamate.Antiviral Res. 56:207-217.
    • (2002) Antiviral Res. , vol.56 , pp. 207-217
    • Uchide, N.1    Ohyama, K.2    Bessho, T.3    Yuan, B.4    Yamakawa, T.5
  • 32
    • 27644479061 scopus 로고    scopus 로고
    • Inhibition of polyprotein processing and RNA replication of human rhinovirus by pyrrolidine dithiocarbamate involves metal ions
    • Krenn B, Holzer B, Gaudernak E, Triendl A, Van Kuppeveld F, Seipelt J. 2005. Inhibition of polyprotein processing and RNA replication of human rhinovirus by pyrrolidine dithiocarbamate involves metal ions. J. Virol. 79:13892-13899.
    • (2005) J.Virol. , vol.79 , pp. 13892-13899
    • Krenn, B.1    Holzer, B.2    Gaudernak, E.3    Triendl, A.4    Van Kuppeveld, F.5    Seipelt, J.6
  • 33
    • 34047100343 scopus 로고    scopus 로고
    • PDTC inhibits picornavirus polyprotein processing and RNA replication by transporting zinc ions into cells
    • Lanke K, Krenn B, Melchers W, Seipelt J, van Kuppeveld F. 2007. PDTC inhibits picornavirus polyprotein processing and RNA replication by transporting zinc ions into cells. J. Gen. Virol. 88:1206-1217.
    • (2007) J. Gen. Virol , vol.88 , pp. 1206-1217
    • Lanke, K.1    Krenn, B.2    Melchers, W.3    Seipelt, J.4    van Kuppeveld, F.5
  • 34
    • 0036683674 scopus 로고    scopus 로고
    • Copper uptake is required for pyrrolidine dithiocarbamate-mediated oxidation and protein level increase of p53 in cells
    • Furuta S, Ortiz F, Sun XZ, Wu HH, Mason A, Momand J. 2002. Copper uptake is required for pyrrolidine dithiocarbamate-mediated oxidation and protein level increase of p53 in cells. Biochem. J. 365:639-648.
    • (2002) Biochem. J , vol.365 , pp. 639-648
    • Furuta, S.1    Ortiz, F.2    Sun, X.Z.3    Wu, H.H.4    Mason, A.5    Momand, J.6
  • 35
    • 0032908620 scopus 로고    scopus 로고
    • Zinc is required in pyrrolidine dithiocarbamate inhibition of NFΚB activation
    • Kim CH, Kim JH, Hsu CY, Ahn YS. 1999. Zinc is required in pyrrolidine dithiocarbamate inhibition of NFΚB activation. FEBS Lett. 449:28-32.
    • (1999) FEBS Lett. , vol.449 , pp. 28-32
    • Kim, C.H.1    Kim, J.H.2    Hsu, C.Y.3    Ahn, Y.S.4
  • 36
    • 0021767941 scopus 로고
    • Trans activation of transcription by herpes virus products: requirement for two HSV-1 immediate-early polypeptides for maximum activity
    • Everett R. 1984. Trans activation of transcription by herpes virus products: requirement for two HSV-1 immediate-early polypeptides for maximum activity. EMBO J. 3:3135-3141.
    • (1984) EMBO J , vol.3 , pp. 3135-3141
    • Everett, R.1
  • 37
    • 0021760248 scopus 로고
    • A detailed analysis of an HSV-1 early promoter: sequences involved in trans-activation by viral immediate-early gene products are not early-gene specific
    • Everett R. 1984. A detailed analysis of an HSV-1 early promoter: sequences involved in trans-activation by viral immediate-early gene products are not early-gene specific. Nucleic Acids Res. 12:3037-3056.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 3037-3056
    • Everett, R.1
  • 38
    • 0021984653 scopus 로고
    • Evidence for a direct role for both the 175,000-and 110,000-molecular-weight immediate-early proteins of herpes simplex virus in the transactivation of delayed-early promoters
    • O'Hare P, Hayward GS. 1985. Evidence for a direct role for both the 175,000-and 110,000-molecular-weight immediate-early proteins of herpes simplex virus in the transactivation of delayed-early promoters. J. Virol. 53:751-760.
    • (1985) J. Virol. , vol.53 , pp. 751-760
    • O'Hare, P.1    Hayward, G.S.2
  • 39
    • 0022393681 scopus 로고
    • Three trans-acting regulatory proteins of herpes simplex virus modulate immediate-early gene expression in a pathway involving positive and negative feedback regulation
    • O'Hare P, Hayward GS. 1985. Three trans-acting regulatory proteins of herpes simplex virus modulate immediate-early gene expression in a pathway involving positive and negative feedback regulation. J. Virol. 56:723-733.
    • (1985) J. Virol. , vol.56 , pp. 723733
    • O'Hare, P.1    Hayward, G.S.2
  • 40
    • 0023378322 scopus 로고
    • A detailed mutational analysis of Vmw110, a trans-acting transcriptional activator encoded by herpes simplex virus type 1
    • Everett R. 1987. A detailed mutational analysis of Vmw110, a trans-acting transcriptional activator encoded by herpes simplex virus type 1. EMBO J. 6:2069-2076.
    • (1987) EMBO J , vol.6 , pp. 2069-2076
    • Everett, R.1
  • 41
    • 0021847819 scopus 로고
    • Identification of immediate early genes from herpes simplex virus that transactivate the virus thymidine kinase gene
    • U.S.A
    • Gelman IH, Silverstein S. 1985. Identification of immediate early genes from herpes simplex virus that transactivate the virus thymidine kinase gene. Proc. Natl. Acad. Sci. U. S. A. 82:5265-5269.
    • (1985) Proc. Natl. Acad. Sci. , vol.82 , pp. 5265-5269
    • Gelman, I.H.1    Silverstein, S.2
  • 42
    • 0035082275 scopus 로고    scopus 로고
    • Requirements for the nuclearcytoplasmic translocation of infected-cell protein 0 of herpes simplex virus 1
    • Lopez P, Van Sant C, Roizman B. 2001. Requirements for the nuclearcytoplasmic translocation of infected-cell protein 0 of herpes simplex virus 1. J. Virol. 75:3832-3840.
    • (2001) J. Virol. , vol.75 , pp. 3832-3840
    • Lopez, P.1    Van Sant, C.2    Roizman, B.3
  • 43
    • 0032822610 scopus 로고    scopus 로고
    • Activation of cJUN N-terminal kinase by herpes simplex virus type 1 enhances viral replication
    • McLean T, Bachenheimer S. 1999. Activation of cJUN N-terminal kinase by herpes simplex virus type 1 enhances viral replication. J. Virol.73:8415-8426.
    • (1999) J. Virol. , vol.73 , pp. 8415-8426
    • McLean, T.1    Bachenheimer, S.2
  • 44
    • 0033582476 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 infection stimulates p38/c-Jun N-terminal mitogen-activated protein kinase pathways and activates transcription factor AP-1
    • Zachos G, Clements B, Conner J. 1999. Herpes simplex virus type 1 infection stimulates p38/c-Jun N-terminal mitogen-activated protein kinase pathways and activates transcription factor AP-1. J. Biol. Chem. 274:5097-5103.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5097-5103
    • Zachos, G.1    Clements, B.2    Conner, J.3
  • 45
    • 5144231404 scopus 로고    scopus 로고
    • Inhibition of the stress-activated kinase, p38, does not affect the virus transcriptional program of herpes simplex virus type 1
    • Karaca G, Hargett D, McLean TI, Aguilar J, Ghazal P, Wagner EK, Bachenheimer SL. 2004. Inhibition of the stress-activated kinase, p38, does not affect the virus transcriptional program of herpes simplex virus type 1. Virology 329:142-156.
    • (2004) Virology , vol.329 , pp. 142-156
    • Karaca, G.1    Hargett, D.2    McLean, T.I.3    Aguilar, J.4    Ghazal, P.5    Wagner, E.K.6    Bachenheimer, S.L.7
  • 46
    • 1542379821 scopus 로고    scopus 로고
    • Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway
    • Mehle A, Strack B, Ancuta P, Zhang C, McPike M, Gabuzda D. 2004. Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway. J. Biol. Chem. 279:7792-7798.
    • (2004) J. Biol. Chem. , vol.279 , pp. 7792-7798
    • Mehle, A.1    Strack, B.2    Ancuta, P.3    Zhang, C.4    McPike, M.5    Gabuzda, D.6
  • 47
    • 0035167960 scopus 로고    scopus 로고
    • Polyubiquitination is required for US11-dependent movement of MHC class I heavy chain from endoplasmic reticulum into cytosol
    • Shamu CE, Flierman D, Ploegh HL, Rapoport TA, Chau V. 2001. Polyubiquitination is required for US11-dependent movement of MHC class I heavy chain from endoplasmic reticulum into cytosol. Mol. Biol. Cell 12:2546-2555.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2546-2555
    • Shamu, C.E.1    Flierman, D.2    Ploegh, H.L.3    Rapoport, T.A.4    Chau, V.5
  • 48
    • 0031935031 scopus 로고    scopus 로고
    • CD4 glycoprotein degradation induced by human immunodeficiency virus type 1 Vpu protein requires the function of proteasomes and the ubiquitin-conjugating pathway
    • Schubert U, Antón LC, Bacčík I, Cox JH, Bour S, Bennink JR, Orlowski M, Strebel K, Yewdell JW. 1998. CD4 glycoprotein degradation induced by human immunodeficiency virus type 1 Vpu protein requires the function of proteasomes and the ubiquitin-conjugating pathway. J. Virol. 72:2280-2288.
    • (1998) J. Virol , vol.72 , pp. 2280-2288
    • Schubert, U.1    Antón, L.C.2    Bacčík, I.3    Cox, J.H.4    Bour, S.5    Bennink, J.R.6    Orlowski, M.7    Strebel, K.8    Yewdell, J.W.9
  • 50
    • 0041344358 scopus 로고    scopus 로고
    • Proteasome inhibition reduces coxsackievirus B3 replication in murine cardiomyocytes
    • Luo H, Zhang J, Cheung C, Suarez A, McManus BM, Yang D. 2003.Proteasome inhibition reduces coxsackievirus B3 replication in murine cardiomyocytes. Am. J. Pathol. 163:381-385.
    • (2003) Am. J. Pathol , vol.163 , pp. 381-385
    • Luo, H.1    Zhang, J.2    Cheung, C.3    Suarez, A.4    McManus, B.M.5    Yang, D.6
  • 51
    • 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 RD, Freemont P, Saitoh H, Dasso M, Orr A, Kathoria M,Parkinson J. 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.
    • 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
  • 52
    • 0035146502 scopus 로고    scopus 로고
    • Proteasome inhibitor induces nucleolar translocation of Epstein-Barr virus-encoded EBNA-5
    • Pokrovskaja K, Mattsson K, Kashuba E, Klein G, Szekely L. 2001.Proteasome inhibitor induces nucleolar translocation of Epstein-Barr virus-encoded EBNA-5. J. Gen. Virol. 82:345-358.
    • (2001) J. Gen. Virol. , vol.82 , pp. 345-358
    • Pokrovskaja, K.1    Mattsson, K.2    Kashuba, E.3    Klein, G.4    Szekely, L.5
  • 53
    • 62749192159 scopus 로고    scopus 로고
    • Inhibition of the ubiquitin-proteasome system prevents vaccinia virus DNA replication and expression of intermediate and late genes
    • Satheshkumar P, Anton LC, Sanz P, Moss B. 2009. Inhibition of the ubiquitin-proteasome system prevents vaccinia virus DNA replication and expression of intermediate and late genes. J. Virol. 83:2469-2479.
    • (2009) J. Virol. , vol.83 , pp. 2469-2479
    • Satheshkumar, P.1    Anton, L.C.2    Sanz, P.3    Moss, B.4
  • 54
    • 84863703068 scopus 로고    scopus 로고
    • The ubiquitin/proteasome system mediates entry and endosomal trafficking of Kaposi's sarcoma-associated herpesvirus in endothelial cells
    • Greene W, Zhang W, He M, Witt C, Ye F, Gao SJ. 2012. The ubiquitin/proteasome system mediates entry and endosomal trafficking of Kaposi's sarcoma-associated herpesvirus in endothelial cells. PLoS Pathog.8:e1002703. doi:10.1371/journal.ppat.1002703.
    • (2012) PLoS Pathog. , vol.8
    • Greene, W.1    Zhang, W.2    He, M.3    Witt, C.4    Ye, F.5    Gao, S.J.6
  • 55
    • 84861309346 scopus 로고    scopus 로고
    • Hepatitis E virus replication requires an active ubiquitin-proteasome system
    • Karpe YA, Meng XJ. 2012. Hepatitis E virus replication requires an active ubiquitin-proteasome system. J. Virol. 86:5948-5952.
    • (2012) J. Virol. , vol.86 , pp. 5948-5952
    • Karpe, Y.A.1    Meng, X.J.2
  • 57
    • 0032129268 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 induction of persistent NFΚB nuclear translocation increases the efficiency of virus replication
    • Patel A, Hanson J, McLean TI, Olgiate J, Hilton M, Miller WE, Bachenheimer SL. 1998. Herpes simplex virus type 1 induction of persistent NFΚB nuclear translocation increases the efficiency of virus replication.Virology 247:212-222.
    • (1998) Virology , vol.247 , pp. 212-222
    • Patel, A.1    Hanson, J.2    McLean, T.I.3    Olgiate, J.4    Hilton, M.5    Miller, W.E.6    Bachenheimer, S.L.7
  • 58
    • 10044241988 scopus 로고    scopus 로고
    • Efficient replication by herpes simplex virus type 1 involves activation of the IΚB kinase-IΚB-p65 pathway
    • Gregory D, Hargett D, Holmes D, Money E, Bachenheimer S. 2004.Efficient replication by herpes simplex virus type 1 involves activation of the IΚB kinase-IΚB-p65 pathway. J. Virol. 78:13582-13590.
    • (2004) J. Virol , vol.78 , pp. 13582-13590
    • Gregory, D.1    Hargett, D.2    Holmes, D.3    Money, E.4    Bachenheimer, S.5
  • 59
    • 0035969127 scopus 로고    scopus 로고
    • Role and fate of PML nuclear bodies in response to interferon and viral infections
    • Regad T, Chelbi-Alix MK. 2001. Role and fate of PML nuclear bodies in response to interferon and viral infections. Oncogene 20:7274-7286.
    • (2001) Oncogene , vol.20 , pp. 7274-7286
    • Regad, T.1    Chelbi-Alix, M.K.2
  • 60
    • 34347348272 scopus 로고    scopus 로고
    • PML and PML nuclear bodies: implications in antiviral defence
    • Everett RD, Chelbi-Alix MK. 2007. PML and PML nuclear bodies: implications in antiviral defence. Biochimie 89:819-830.
    • (2007) Biochimie , vol.89 , pp. 819-830
    • Everett, R.D.1    Chelbi-Alix, M.K.2
  • 61
    • 44149083798 scopus 로고    scopus 로고
    • Promyelocytic leukemia-nuclear body proteins:herpesvirus enemies, accomplices, or both
    • Saffert RT, Kalejta RF. 2008. Promyelocytic leukemia-nuclear body proteins:herpesvirus enemies, accomplices, or both? Future Virol. 3:265-277.
    • (2008) Future Virol. , vol.3 , pp. 265-277
    • Saffert, R.T.1    Kalejta, R.F.2
  • 62
    • 79960360968 scopus 로고    scopus 로고
    • Protein cross-linking as a novel mechanism of action of a ubiquitin-activating enzyme inhibitor with anti-tumor activity
    • Kapuria V, Peterson LF, Showalter H, Kirchhoff PD, Talpaz M, Donato NJ. 2011. Protein cross-linking as a novel mechanism of action of a ubiquitin-activating enzyme inhibitor with anti-tumor activity. Biochem.Pharmacol. 82:341-349.
    • (2011) Biochem Pharmacol , vol.82 , pp. 341-349
    • Kapuria, V.1    Peterson, L.F.2    Showalter, H.3    Kirchhoff, P.D.4    Talpaz, M.5    Donato, N.J.6
  • 64
    • 0035933837 scopus 로고    scopus 로고
    • Nonstructural 3 protein of hepatitis C virus triggers an oxidative burst in human monocytes via activation of NADPH oxidase
    • Bureau C, Bernad J, Chaouche N, Orfila C, Béraud M, Gonindard C,Alric L, Vinel JP, Pipy B. 2001. Nonstructural 3 protein of hepatitis C virus triggers an oxidative burst in human monocytes via activation of NADPH oxidase. J. Biol. Chem. 276:23077-23083.
    • J. Biol. Chem , vol.276 , pp. 23077-23083
    • Bureau, C.1    Bernad, J.2    Chaouche, N.3    Orfila, C.4    Béraud, M.5    Gonindard, C.6    Alric, L.7    Vinel, J.P.8    Pipy, B.9
  • 65
    • 0031435786 scopus 로고    scopus 로고
    • Oxidative stress in human immunodeficiency virus infection
    • Israel N, Gougerot-Pocidalo MA. 1997. Oxidative stress in human immunodeficiency virus infection. Cell. Mol. Life Sci. 53:864-870.
    • (1997) Cell. Mol. Life Sci. , vol.53 , pp. 864-870
    • Israel, N.1    Gougerot-Pocidalo, M.A.2
  • 66
    • 0029162485 scopus 로고
    • The role of oxidative stress in HIV disease
    • Pace GW, Leaf CD. 1995. The role of oxidative stress in HIV disease. Free Radic. Biol. Med. 19:523-528.
    • (1995) Free Radic. Biol. Med. , vol.19 , pp. 523-528
    • Pace, G.W.1    Leaf, C.D.2
  • 67
    • 77953947353 scopus 로고    scopus 로고
    • Herpes simplex virus induces neural oxidative damage via microglial cell Toll-like receptor-2
    • Schachtele SJ, Hu S, Little MR, Lokensgard JR. 2010. Herpes simplex virus induces neural oxidative damage via microglial cell Toll-like receptor-2. J. Neuroinflamm. 7:35. doi:10.1186/1742-2094-7-35.
    • (2010) J. Neuroinflamm , vol.7 , pp. 35
    • Schachtele, S.J.1    Hu, S.2    Little, M.R.3    Lokensgard, J.R.4
  • 68
    • 80053456294 scopus 로고    scopus 로고
    • HSV infection induces production of ROS, which potentiate signaling from pattern recognition receptors: role for S-glutathionylation of TRAF3 and 6
    • Gonzalez-Dosal R, Horan KA, Rahbek SH, Ichijo H, Chen ZJ, Mieyal JJ, Hartmann R, Paludan SR. 2011. HSV infection induces production of ROS, which potentiate signaling from pattern recognition receptors: role for S-glutathionylation of TRAF3 and 6. PLoS Pathog. 7:e1002250. doi:10.1371/journal.ppat.1002250.
    • (2011) PLoS Pathog , vol.7
    • Gonzalez-Dosal, R.1    Horan, K.A.2    Rahbek, S.H.3    Ichijo, H.4    Chen, Z.J.5    Mieyal, J.J.6    Hartmann, R.7    Paludan, S.R.8
  • 69
    • 0037114944 scopus 로고    scopus 로고
    • Changes in plasma human immunodeficiency virus type 1 RNA associated with herpes simplex virus reactivation and suppression
    • Schacker T, Zeh J, Hu H, Shaughnessy M, Corey L. 2002. Changes in plasma human immunodeficiency virus type 1 RNA associated with herpes simplex virus reactivation and suppression. J. Infect. Dis. 186:1718-1725.
    • (2002) J. Infect. Dis , vol.186 , pp. 1718-1725
    • Schacker, T.1    Zeh, J.2    Hu, H.3    Shaughnessy, M.4    Corey, L.5
  • 70
    • 0033624137 scopus 로고    scopus 로고
    • ICP 0, a regulator of herpes simplex virus during lytic and latent infection
    • Everett RD. 2000. ICP 0, 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
  • 71
    • 0842347715 scopus 로고    scopus 로고
    • Phenotype of a herpes simplex virus type 1 mutant that fails to express immediate-early regulatory protein ICP0
    • Everett RD, Boutell C, Orr A. 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
  • 72
    • 0033552585 scopus 로고    scopus 로고
    • The role of the E6-p53 interaction in the molecular pathogenesis of HPV
    • Thomas M, Pim D, Banks L. 1999. The role of the E6-p53 interaction in the molecular pathogenesis of HPV. Oncogene 18:7690-7700.
    • (1999) Oncogene , vol.18 , pp. 7690-7700
    • Thomas, M.1    Pim, D.2    Banks, L.3
  • 73
    • 14044259999 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system in HIV replication: potential targets for antiretroviral therapy
    • Klinger PP, Schubert U. 2005. The ubiquitin-proteasome system in HIV replication: potential targets for antiretroviral therapy. Expert Rev.Anti Infect. Ther. 3:61-79.
    • (2005) Expert Rev. Anti Infect. Ther. , vol.3 , pp. 61-79
    • Klinger, P.P.1    Schubert, U.2
  • 75
    • 50249083248 scopus 로고    scopus 로고
    • Ubiquitination is required for effective replication of coxsackievirus B3
    • Si X, Gao G, Wong J, Wang Y, Zhang J, Luo H. 2008. Ubiquitination is required for effective replication of coxsackievirus B3. PLoS One 3:e2585. doi:10.1371/journal.pone.0002585.
    • (2008) PLoS One , vol.3
    • Si, X.1    Gao, G.2    Wong, J.3    Wang, Y.4    Zhang, J.5    Luo, H.6
  • 77
    • 77957366917 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway is important for dengue virus infection in primary human endothelial cells
    • Kanlaya R, Pattanakitsakul S, Sinchaikul S, Chen ST, Thongboonkerd V. 2010. The ubiquitin-proteasome pathway is important for dengue virus infection in primary human endothelial cells. J. Proteome Res. 9:4960-4971.
    • (2010) J. Proteome Res , vol.9 , pp. 4960-4971
    • Kanlaya, R.1    Pattanakitsakul, S.2    Sinchaikul, S.3    Chen, S.T.4    Thongboonkerd, V.5
  • 79
    • 0032534802 scopus 로고    scopus 로고
    • A viral activator of gene expression functions via the ubiquitin-proteasome pathway
    • Everett RD, Orr A, Preston CM. 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
  • 80
    • 33845604018 scopus 로고    scopus 로고
    • Antiviral activity of proteasome inhibitors in herpes simplex virus-1 infection: role of nuclear factor-kappaB
    • La Frazia S, Amici C, Santoro MG. 2006. Antiviral activity of proteasome in hibitors in herpes simplex virus-1 infection: role of nuclear factor-kappaB. Antiviral Ther. 11:995-1004.
    • (2006) Antiviral Ther , vol.11 , pp. 995-1004
    • La Frazia, S.1    Amici, C.2    Santoro, M.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.