메뉴 건너뛰기




Volumn 16, Issue 3, 2011, Pages 256-271

The ribonucleotide reductase R1 subunits of herpes simplex virus types 1 and 2 protect cells against TNFα- and FasL-induced apoptosis by interacting with caspase-8

Author keywords

Caspase 8; FasL; ICP10; ICP6; Viral inhibitor of apoptosis

Indexed keywords

APOPTOSIS REGULATORY PROTEIN; CASPASE 8; FAS ASSOCIATED DEATH DOMAIN PROTEIN; FAS LIGAND; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE B; RIBONUCLEOTIDE REDUCTASE; STRESS ACTIVATED PROTEIN KINASE; TUMOR NECROSIS FACTOR ALPHA ANTIBODY;

EID: 79952194140     PISSN: 13608185     EISSN: 1573675X     Source Type: Journal    
DOI: 10.1007/s10495-010-0560-2     Document Type: Article
Times cited : (73)

References (71)
  • 1
    • 0026474991 scopus 로고
    • Antiviral activity of tumor necrosis factor is signaled through the 55-kDa type i TNF receptor [corrected]
    • 1331233 1:CAS:528:DyaK3sXnvFSnsg%3D%3D
    • GH Wong LA Tartaglia MS Lee DV Goeddel 1992 Antiviral activity of tumor necrosis factor is signaled through the 55-kDa type I TNF receptor [corrected] J Immunol 149 3350 3353 1331233 1:CAS:528:DyaK3sXnvFSnsg%3D%3D
    • (1992) J Immunol , vol.149 , pp. 3350-3353
    • Wong, G.H.1    Tartaglia, L.A.2    Lee, M.S.3    Goeddel, D.V.4
  • 2
    • 0037790592 scopus 로고    scopus 로고
    • Apoptosis and interferons: Role of interferon-stimulated genes as mediators of apoptosis
    • DOI 10.1023/A:1023668705040
    • M Chawla-Sarkar DJ Lindner YF Liu BR Williams GC Sen RH Silverman EC Borden 2003 Apoptosis and interferons: role of interferon-stimulated genes as mediators of apoptosis Apoptosis 8 237 249 12766484 10.1023/A:1023668705040 1:CAS:528:DC%2BD3sXjsF2nt70%3D (Pubitemid 36749609)
    • (2003) Apoptosis , vol.8 , Issue.3 , pp. 237-249
    • Chawla-Sarkar, M.1    Lindner, D.J.2    Liu, Y.-F.3    Williams, B.R.4    Sen, G.C.5    Silverman, R.H.6    Borden, E.C.7
  • 3
    • 70350314350 scopus 로고    scopus 로고
    • Protective role of Fas-FasL signaling in lethal infection with herpes simplex virus type 2 in mice
    • 19740996 10.1128/JVI.01006-09 1:CAS:528:DC%2BC3cXksFKqtLw%3D
    • T Ishikawa H Yamada A Oyamada F Goshima Y Nishiyama Y Yoshikai 2009 Protective role of Fas-FasL signaling in lethal infection with herpes simplex virus type 2 in mice J Virol 83 11777 11783 19740996 10.1128/JVI.01006-09 1:CAS:528:DC%2BC3cXksFKqtLw%3D
    • (2009) J Virol , vol.83 , pp. 11777-11783
    • Ishikawa, T.1    Yamada, H.2    Oyamada, A.3    Goshima, F.4    Nishiyama, Y.5    Yoshikai, Y.6
  • 4
    • 0034922931 scopus 로고    scopus 로고
    • Robust expression of TNF-α, IL-1β, RANTES, and IP-10 by human microglial cells during nonproductive infection with herpes simplex virus
    • DOI 10.1080/13550280152403254
    • JR Lokensgard S Hu W Sheng M van Oijen D Cox MC Cheeran PK Peterson 2001 Robust expression of TNF-alpha, IL-1beta, RANTES, and IP-10 by human microglial cells during nonproductive infection with herpes simplex virus J Neurovirol 7 208 219 11517395 10.1080/13550280152403254 1:CAS:528:DC%2BD3MXlvFaisLg%3D (Pubitemid 32685255)
    • (2001) Journal of NeuroVirology , vol.7 , Issue.3 , pp. 208-219
    • Lokensgard, J.R.1    Hu, S.2    Sheng, W.3    Van Oijen, M.4    Cox, D.5    Cheeran, M.C.-J.6    Peterson, P.K.7
  • 5
    • 0028071790 scopus 로고
    • Synergistic anti-herpes effect of TNF-α and IFN-γ in human corneal epithelial cells compared with that in corneal fibroblasts
    • DOI 10.1016/0166-3542(94)90004-3
    • SH Chen JE Oakes RN Lausch 1994 Synergistic anti-herpes effect of TNF-alpha and IFN-gamma in human corneal epithelial cells compared with that in corneal fibroblasts Antiviral Res 25 201 213 7710269 10.1016/0166-3542(94)90004- 3 1:CAS:528:DyaK2MXitlWmurk%3D (Pubitemid 24371525)
    • (1994) Antiviral Research , vol.25 , Issue.3-4 , pp. 201-213
    • Chen, S.-H.1    Oakes, J.E.2    Lausch, R.N.3
  • 6
    • 34548490485 scopus 로고    scopus 로고
    • Tumor necrosis factor-α and interleukin-1β play a critical role in the resistance against lethal herpes simplex virus encephalitis
    • DOI 10.1086/520094
    • Y Sergerie S Rivest G Boivin 2007 Tumor necrosis factor-alpha and interleukin-1 beta play a critical role in the resistance against lethal herpes simplex virus encephalitis J Infect Dis 196 853 860 17703415 10.1086/520094 1:CAS:528:DC%2BD2sXhtFanu7rL (Pubitemid 47378934)
    • (2007) Journal of Infectious Diseases , vol.196 , Issue.6 , pp. 853-860
    • Sergerie, Y.1    Rivest, S.2    Boivin, G.3
  • 8
    • 33746210101 scopus 로고    scopus 로고
    • Herpes simplex virus 1 precludes replenishment of the short-lived receptor of tumor necrosis factor alpha by virion host shutoff-dependent degradation of its mRNA
    • DOI 10.1128/JVI.00587-06
    • L Liang B Roizman 2006 Herpes simplex virus 1 precludes replenishment of the short-lived receptor of tumor necrosis factor alpha by virion host shutoff-dependent degradation of its mRNA J Virol 80 7756 7759 16840355 10.1128/JVI.00587-06 1:CAS:528:DC%2BD28XnsVWgurY%3D (Pubitemid 44092595)
    • (2006) Journal of Virology , vol.80 , Issue.15 , pp. 7756-7759
    • Liang, L.1    Roizman, B.2
  • 9
    • 62849093368 scopus 로고    scopus 로고
    • Death receptor signal transducers: Nodes of coordination in immune signaling networks
    • 19295631 10.1038/ni.1714 1:CAS:528:DC%2BD1MXjtlymsLw%3D
    • NS Wilson V Dixit A Ashkenazi 2009 Death receptor signal transducers: nodes of coordination in immune signaling networks Nat Immunol 10 348 355 19295631 10.1038/ni.1714 1:CAS:528:DC%2BD1MXjtlymsLw%3D
    • (2009) Nat Immunol , vol.10 , pp. 348-355
    • Wilson, N.S.1    Dixit, V.2    Ashkenazi, A.3
  • 10
    • 0034744033 scopus 로고    scopus 로고
    • NF-κB inducers upregulate cFLIP, a cycloheximide-sensitive inhibitor of death receptor signaling
    • DOI 10.1128/MCB.21.12.3964-3973.2001
    • S Kreuz D Siegmund P Scheurich H Wajant 2001 NF-kappaB inducers upregulate cFLIP, a cycloheximide-sensitive inhibitor of death receptor signaling Mol Cell Biol 21 3964 3973 11359904 10.1128/MCB.21.12.3964-3973.2001 1:CAS:528:DC%2BD3MXktFWgt7k%3D (Pubitemid 32476458)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.12 , pp. 3964-3973
    • Kreuz, S.1    Siegmund, D.2    Scheurich, P.3    Wajant, H.4
  • 11
    • 0035827569 scopus 로고    scopus 로고
    • Cellular FLICE-inhibitory protein splice variants inhibit different steps of caspase-8 activation at the CD95 death-inducing signaling complex
    • 11279218 10.1074/jbc.M101780200 1:CAS:528:DC%2BD3MXktlKnurc%3D
    • A Krueger I Schmitz S Baumann PH Krammer S Kirchhoff 2001 Cellular FLICE-inhibitory protein splice variants inhibit different steps of caspase-8 activation at the CD95 death-inducing signaling complex J Biol Chem 276 20633 20640 11279218 10.1074/jbc.M101780200 1:CAS:528:DC%2BD3MXktlKnurc%3D
    • (2001) J Biol Chem , vol.276 , pp. 20633-20640
    • Krueger, A.1    Schmitz, I.2    Baumann, S.3    Krammer, P.H.4    Kirchhoff, S.5
  • 12
    • 44449125603 scopus 로고    scopus 로고
    • Crystal Structure of a vFlip-IKKγ Complex: Insights into Viral Activation of the IKK Signalosome
    • DOI 10.1016/j.molcel.2008.04.029, PII S1097276508003602
    • C Bagneris AV Ageichik N Cronin B Wallace M Collins C Boshoff G Waksman T Barrett 2008 Crystal structure of a vFlip-IKKgamma complex: insights into viral activation of the IKK signalosome Mol Cell 30 620 631 18538660 10.1016/j.molcel.2008.04.029 1:CAS:528:DC%2BD1cXntlWmsLk%3D (Pubitemid 351755065)
    • (2008) Molecular Cell , vol.30 , Issue.5 , pp. 620-631
    • Bagneris, C.1    Ageichik, A.V.2    Cronin, N.3    Wallace, B.4    Collins, M.5    Boshoff, C.6    Waksman, G.7    Barrett, T.8
  • 13
    • 0041853690 scopus 로고    scopus 로고
    • Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes
    • DOI 10.1016/S0092-8674(03)00521-X
    • O Micheau J Tschopp 2003 Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes Cell 114 181 190 12887920 10.1016/S0092-8674(03)00521-X 1:CAS:528:DC%2BD3sXlvFCgu7Y%3D (Pubitemid 36936912)
    • (2003) Cell , vol.114 , Issue.2 , pp. 181-190
    • Micheau, O.1    Tschopp, J.2
  • 14
    • 0037815277 scopus 로고    scopus 로고
    • Fas-associated death domain protein and caspase-8 are not recruited to the tumor necrosis factor receptor I signaling complex during tumor necrosis factor-induced apoptosis
    • DOI 10.1074/jbc.M303399200
    • N Harper M Hughes M MacFarlane GM Cohen 2003 Fas-associated death domain protein and caspase-8 are not recruited to the tumor necrosis factor receptor 1 signaling complex during tumor necrosis factor-induced apoptosis J Biol Chem 278 25534 25541 12721308 10.1074/jbc.M303399200 1:CAS:528:DC%2BD3sXlt1Cmuro%3D (Pubitemid 36835305)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.28 , pp. 25534-25541
    • Harper, N.1    Hughes, M.2    MacFarlane, M.3    Cohen, G.M.4
  • 15
    • 0242656497 scopus 로고    scopus 로고
    • Death receptor-induced cell killing
    • DOI 10.1016/j.cellsig.2003.08.007
    • A Thorburn 2004 Death receptor-induced cell killing Cell Signal 16 139 144 14636884 10.1016/j.cellsig.2003.08.007 1:CAS:528:DC%2BD3sXptVWmtr4%3D (Pubitemid 37431163)
    • (2004) Cellular Signalling , vol.16 , Issue.2 , pp. 139-144
    • Thorburn, A.1
  • 16
    • 0037276438 scopus 로고    scopus 로고
    • Tumor necrosis factor signaling
    • DOI 10.1038/sj.cdd.4401189
    • H Wajant K Pfizenmaier P Scheurich 2003 Tumor necrosis factor signaling Cell Death Differ 10 45 65 12655295 10.1038/sj.cdd.4401189 1:CAS:528: DC%2BD3sXit12mu7s%3D (Pubitemid 36511832)
    • (2003) Cell Death and Differentiation , vol.10 , Issue.1 , pp. 45-65
    • Wajant, H.1    Pfizenmaier, K.2    Scheurich, P.3
  • 17
    • 5644222552 scopus 로고    scopus 로고
    • Life and death decisions: Secondary complexes and lipid rafts in TNF receptor family signal transduction
    • DOI 10.1016/j.immuni.2004.10.001, PII S1074761304002808
    • JR Muppidi J Tschopp RM Siegel 2004 Life and death decisions: secondary complexes and lipid rafts in TNF receptor family signal transduction Immunity 21 461 465 15485624 10.1016/j.immuni.2004.10.001 1:CAS:528:DC%2BD2cXpvVygt7g%3D (Pubitemid 39370502)
    • (2004) Immunity , vol.21 , Issue.4 , pp. 461-465
    • Muppidi, J.R.1    Tschopp, J.2    Siegel, R.M.3
  • 18
    • 0032508414 scopus 로고    scopus 로고
    • NF-≃B antiapoptosis: Induction of TRAF1 and TRAF2 and c-IAP1 and c- IAP2 to suppress caspase-8 activation
    • DOI 10.1126/science.281.5383.1680
    • CY Wang MW Mayo RG Korneluk DV Goeddel AS Baldwin Jr 1998 NF-kappaB antiapoptosis: induction of TRAF1 and TRAF2 and c-IAP1 and c-IAP2 to suppress caspase-8 activation Science 281 1680 1683 9733516 10.1126/science.281.5383.1680 1:CAS:528:DyaK1cXmtVWhurk%3D (Pubitemid 28435585)
    • (1998) Science , vol.281 , Issue.5383 , pp. 1680-1683
    • Wang, C.-Y.1    Mayo, M.W.2    Korneluk, R.G.3    Goeddel, D.V.4    Baldwin Jr., A.S.5
  • 19
    • 0023695728 scopus 로고
    • Factor(s) present in herpes simplex virus type 1-infected cells can compensate for the loss of the large subunit of the viral ribonucleotide reductase: Characterization of an ICP6 deletion mutant
    • 2842955 10.1016/0042-6822(88)90144-4 1:CAS:528:DyaL1cXlvVCmsrw%3D
    • DJ Goldstein SK Weller 1988 Factor(s) present in herpes simplex virus type 1-infected cells can compensate for the loss of the large subunit of the viral ribonucleotide reductase: characterization of an ICP6 deletion mutant Virology 166 41 51 2842955 10.1016/0042-6822(88)90144-4 1:CAS:528: DyaL1cXlvVCmsrw%3D
    • (1988) Virology , vol.166 , pp. 41-51
    • Goldstein, D.J.1    Weller, S.K.2
  • 20
    • 0023124838 scopus 로고
    • 2 composed of 40K and 140K proteins, of which the latter shows multiple forms due to proteolysis
    • DOI 10.1016/0042-6822(87)90422-3
    • R Ingemarson H Lankinen 1987 The herpes simplex virus type 1 ribonucleotide reductase is a tight complex of the type alpha 2 beta 2 composed of 40 K and 140 K proteins, of which the latter shows multiple forms due to proteolysis Virology 156 417 422 3027985 10.1016/0042-6822(87)90422-3 1:CAS:528:DyaL2sXhvFWktLw%3D (Pubitemid 17021037)
    • (1987) Virology , vol.156 , Issue.2 , pp. 417-422
    • Ingemarson, R.1    Lankinin, H.2
  • 21
    • 0022646555 scopus 로고
    • Herpes simplex virus specifies two subunits of ribonucleotide reductase encoded by 3'-coterminal transcripts
    • MA Swain DA Galloway 1986 Herpes simplex virus specifies two subunits of ribonucleotide reductase encoded by 3′-coterminal transcripts J Virol 57 802 808 2419588 1:CAS:528:DyaL28Xhs1altLs%3D (Pubitemid 16143959)
    • (1986) Journal of Virology , vol.57 , Issue.3 , pp. 802-808
    • Swain, M.A.1    Galloway, D.A.2
  • 22
    • 0036145517 scopus 로고    scopus 로고
    • The herpes simplex virus type 2 r1 protein kinase (ICP10 PK) blocks apoptosis in hippocampal neurons, involving activation of the MEK/MAPK survival pathway
    • D Perkins EF Pereira M Gober PJ Yarowsky L Aurelian 2002 The herpes simplex virus type 2 R1 protein kinase (ICP10 PK) blocks apoptosis in hippocampal neurons, involving activation of the MEK/MAPK survival pathway J Virol 76 1435 1449 11773417 10.1128/JVI.76.3.1435-1449.2002 1:CAS:528: DC%2BD38XnvFCqtg%3D%3D (Pubitemid 34066444)
    • (2002) Journal of Virology , vol.76 , Issue.3 , pp. 1435-1449
    • Perkins, D.1    Pereira, E.F.R.2    Gober, M.3    Yarowsky, P.J.4    Aurelian, L.5
  • 23
    • 0033015933 scopus 로고    scopus 로고
    • The unique N terminus of herpes simplex virus type 1 ribonucleotide reductase large subunit is phosphorylated by casein kinase 2, which may have a homologue in Escherichia coli
    • J Conner 1999 The unique N terminus of herpes simplex virus type 1 ribonucleotide reductase large subunit is phosphorylated by casein kinase 2, which may have a homologue in Escherichia coli J Gen Virol 80 Pt 6 1471 1476 10374965 1:CAS:528:DyaK1MXjs1Omtbc%3D (Pubitemid 29261478)
    • (1999) Journal of General Virology , vol.80 , Issue.6 , pp. 1471-1476
    • Conner, J.1
  • 24
    • 0031916707 scopus 로고    scopus 로고
    • The R1 subunit of herpes simplex virus ribonucleotide reductase is a good substrate for host cell protein kinases but is not itself a protein kinase
    • DOI 10.1074/jbc.273.3.1435
    • Y Langelier L Champoux M Hamel C Guilbault N Lamarche P Gaudreau B Massie 1998 The R1 subunit of herpes simplex virus ribonucleotide reductase is a good substrate for host cell protein kinases but is not itself a protein kinase J Biol Chem 273 1435 1443 9430680 10.1074/jbc.273.3.1435 1:CAS:528: DyaK1cXktFGisw%3D%3D (Pubitemid 28133664)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.3 , pp. 1435-1443
    • Langelier, Y.1    Champoux, L.2    Hamel, M.3    Guilbault, C.4    Lamarche, N.5    Gaudreau, P.6    Massie, B.7
  • 25
    • 21344465226 scopus 로고    scopus 로고
    • Herpes simplex virus type 2 encodes a heat shock protein homologue with apoptosis regulatory functions
    • MD Gober SQ Wales L Aurelian 2005 Herpes simplex virus type 2 encodes a heat shock protein homologue with apoptosis regulatory functions Front Biosci 10 2788 2803 15970534 10.2741/1736 1:CAS:528:DC%2BD2MXntFGisb4%3D (Pubitemid 40905275)
    • (2005) Frontiers in Bioscience , vol.10 , Issue.SUPPL. 2 , pp. 2788-2803
    • Gober, M.D.1    Wales, S.Q.2    Aurelian, L.3
  • 26
    • 0037526521 scopus 로고    scopus 로고
    • The R1 subunit of herpes simplex virus ribonucleotide reductase has chaperone-like activity similar to Hsp27
    • DOI 10.1016/S0014-5793(03)00547-7
    • S Chabaud H Lambert AM Sasseville H Lavoie C Guilbault B Massie J Landry Y Langelier 2003 The R1 subunit of herpes simplex virus ribonucleotide reductase has chaperone-like activity similar to Hsp27 FEBS Lett 545 213 218 12804778 10.1016/S0014-5793(03)00547-7 1:CAS:528:DC%2BD3sXksVOktro%3D (Pubitemid 36694704)
    • (2003) FEBS Letters , vol.545 , Issue.2-3 , pp. 213-218
    • Chabaud, S.1    Lambert, H.2    Sasseville, A.M.-J.3    Lavoie, H.4    Guilbault, C.5    Massie, B.6    Landry, J.7    Langelier, Y.8
  • 27
    • 32644444260 scopus 로고    scopus 로고
    • Assembly of an active translation initiation factor complex by a viral protein
    • DOI 10.1101/gad.1375006
    • D Walsh I Mohr 2006 Assembly of an active translation initiation factor complex by a viral protein Genes Dev 20 461 472 16481474 10.1101/gad.1375006 1:CAS:528:DC%2BD28Xhslaqu70%3D (Pubitemid 43244400)
    • (2006) Genes and Development , vol.20 , Issue.4 , pp. 461-472
    • Walsh, D.1    Mohr, I.2
  • 28
    • 33846794626 scopus 로고    scopus 로고
    • The ribonucleotide reductase domain of the R1 subunit of herpes simplex virus type 2 ribonucleotide reductase is esential for R1 antiapoptotic function
    • DOI 10.1099/vir.0.82383-0
    • S Chabaud AM Sasseville SM Elahi A Caron F Dufour B Massie Y Langelier 2007 The ribonucleotide reductase domain of the R1 subunit of herpes simplex virus type 2 ribonucleotide reductase is essential for R1 antiapoptotic function J Gen Virol 88 384 394 17251554 10.1099/vir.0.82383-0 1:CAS:528: DC%2BD2sXhsFakur8%3D (Pubitemid 46210875)
    • (2007) Journal of General Virology , vol.88 , Issue.2 , pp. 384-394
    • Chabaud, S.1    Sasseville, A.M.-J.2    Elahi, S.M.3    Caron, A.4    Dufour, F.5    Massie, B.6    Langelier, Y.7
  • 29
    • 66149133220 scopus 로고    scopus 로고
    • The EBV deubiquitinating enzyme, BPLF1, reduces EBV ribonucleotide reductase activity
    • 19244336 10.1128/JVI.02195-08 1:CAS:528:DC%2BD1MXlt1Kqu74%3D
    • CB Whitehurst S Ning GL Bentz F Dufour E Gershburg J Shackelford Y Langelier JS Pagano 2009 The EBV deubiquitinating enzyme, BPLF1, reduces EBV ribonucleotide reductase activity J Virol 83 4345 4353 19244336 10.1128/JVI.02195-08 1:CAS:528:DC%2BD1MXlt1Kqu74%3D
    • (2009) J Virol , vol.83 , pp. 4345-4353
    • Whitehurst, C.B.1    Ning, S.2    Bentz, G.L.3    Dufour, F.4    Gershburg, E.5    Shackelford, J.6    Langelier, Y.7    Pagano, J.S.8
  • 30
    • 0032101371 scopus 로고    scopus 로고
    • Death-effector filaments: Novel cytoplasmic structures that recruit caspases and trigger apoptosis
    • DOI 10.1083/jcb.141.5.1243
    • RM Siegel DA Martin L Zheng SY Ng J Bertin J Cohen MJ Lenardo 1998 Death-effector filaments: novel cytoplasmic structures that recruit caspases and trigger apoptosis J Cell Biol 141 1243 1253 9606215 10.1083/jcb.141.5.1243 1:CAS:528:DyaK1cXjs12ntbw%3D (Pubitemid 28265617)
    • (1998) Journal of Cell Biology , vol.141 , Issue.5 , pp. 1243-1253
    • Siegel, R.M.1    Martin, D.A.2    Zheng, L.3    Ng, S.Y.4    Bertin, J.5    Cohen, J.6    Lenardo, M.J.7
  • 31
    • 34247221517 scopus 로고    scopus 로고
    • The scaffolding adapter Gab1 mediates vascular endothelial growth factor signaling and is required for endothelial cell migration and capillary formation
    • DOI 10.1074/jbc.M611327200
    • M Laramee C Chabot M Cloutier R Stenne M Holgado-Madruga AJ Wong I Royal 2007 The scaffolding adapter Gab1 mediates vascular endothelial growth factor signaling and is required for endothelial cell migration and capillary formation J Biol Chem 282 7758 7769 17178724 10.1074/jbc.M611327200 1:CAS:528: DC%2BD2sXis1KgsL4%3D (Pubitemid 47093597)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.11 , pp. 7758-7769
    • Larame, M.1    Chabot, C.2    Cloutier, M.3    Stenne, R.4    Holgado-Madruga, M.5    Wong, A.J.6    Royal, I.7
  • 33
    • 0030826338 scopus 로고    scopus 로고
    • FLICE is predominantly expressed as two functionally active isoforms, caspase-8/a and caspase-8/b
    • DOI 10.1074/jbc.272.43.26953
    • C Scaffidi JP Medema PH Krammer ME Peter 1997 FLICE is predominantly expressed as two functionally active isoforms, caspase-8/a and caspase-8/b J Biol Chem 272 26953 26958 9341131 10.1074/jbc.272.43.26953 1:CAS:528: DyaK2sXmvFyrsLw%3D (Pubitemid 27452647)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.43 , pp. 26953-26958
    • Scaffidi, C.1    Medema, J.P.2    Krammer, P.H.3    Peter, M.E.4
  • 34
    • 0036848194 scopus 로고    scopus 로고
    • HIV-1 protease processes procaspase 8 to cause mitochondrial release of cytochrome c, caspase cleavage and nuclear fragmentation
    • DOI 10.1038/sj.cdd.4401094
    • Z Nie BN Phenix JJ Lum A Alam DH Lynch B Beckett PH Krammer RP Sekaly AD Badley 2002 HIV-1 protease processes procaspase 8 to cause mitochondrial release of cytochrome c, caspase cleavage and nuclear fragmentation Cell Death Differ 9 1172 1184 12404116 10.1038/sj.cdd.4401094 1:CAS:528:DC%2BD38XotFOrsb8%3D (Pubitemid 35331764)
    • (2002) Cell Death and Differentiation , vol.9 , Issue.11 , pp. 1172-1184
    • Nie, Z.1    Phenix, B.N.2    Lum, J.J.3    Alam, A.4    Lynch, D.H.5    Beckett, B.6    Krammer, P.H.7    Sekaly, R.P.8    Badley, A.D.9
  • 35
    • 0032488664 scopus 로고    scopus 로고
    • Bcl-x(L) acts downstream of caspase-8 activation by the CD95 death- inducing signaling complex
    • DOI 10.1074/jbc.273.6.3388
    • JP Medema C Scaffidi PH Krammer ME Peter 1998 Bcl-xL acts downstream of caspase-8 activation by the CD95 death-inducing signaling complex J Biol Chem 273 3388 3393 9452459 10.1074/jbc.273.6.3388 1:CAS:528:DyaK1cXhtVynur8%3D (Pubitemid 28109756)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.6 , pp. 3388-3393
    • Medema, J.P.1    Scaffidi, C.2    Krammer, P.H.3    Peter, M.E.4
  • 36
    • 65449163494 scopus 로고    scopus 로고
    • Over-expression of IkappaB-kinase-epsilon (IKKepsilon/IKKi) induces secretion of inflammatory cytokines in prostate cancer cell lines
    • 19170126 10.1002/pros.20912 1:CAS:528:DC%2BD1MXmtFelsbo%3D
    • B Peant JS Diallo F Dufour C Le Page N Delvoye F Saad AM Mes-Masson 2009 Over-expression of IkappaB-kinase-epsilon (IKKepsilon/IKKi) induces secretion of inflammatory cytokines in prostate cancer cell lines Prostate 69 706 718 19170126 10.1002/pros.20912 1:CAS:528:DC%2BD1MXmtFelsbo%3D
    • (2009) Prostate , vol.69 , pp. 706-718
    • Peant, B.1    Diallo, J.S.2    Dufour, F.3    Le Page, C.4    Delvoye, N.5    Saad, F.6    Mes-Masson, A.M.7
  • 37
    • 0029796520 scopus 로고    scopus 로고
    • Production of the R2 subunit of ribonucleotide reductase from herpes simplex virus with prokaryotic and eukaryotic expression systems: Higher activity of R2 produced by eukaryotic cells related to higher iron-binding capacity
    • 8947477 1:CAS:528:DyaK28Xnt12rsbk%3D
    • N Lamarche G Matton B Massie M Fontecave M Atta F Dumas P Gaudreau Y Langelier 1996 Production of the R2 subunit of ribonucleotide reductase from herpes simplex virus with prokaryotic and eukaryotic expression systems: higher activity of R2 produced by eukaryotic cells related to higher iron-binding capacity Biochem J 320 Pt 1 129 135 8947477 1:CAS:528:DyaK28Xnt12rsbk%3D
    • (1996) Biochem J , vol.320 , Issue.PART 1 , pp. 129-135
    • Lamarche, N.1    Matton, G.2    Massie, B.3    Fontecave, M.4    Atta, M.5    Dumas, F.6    Gaudreau, P.7    Langelier, Y.8
  • 38
    • 0023000475 scopus 로고
    • Neutralization of herpes simplex virus ribonucleotide reductase activity by an oligopeptide-induced antiserum directed against subunit H2
    • EA Cohen P Gaudreau P Brazeau Y Langelier 1986 Neutralization of herpes simplex virus ribonucleotide reductase activity by an oligopeptide-induced antiserum directed against subunit H2 J Virol 60 1130 1133 2431161 1:CAS:528:DyaL2sXivFansQ%3D%3D (Pubitemid 17179291)
    • (1986) Journal of Virology , vol.60 , Issue.3 , pp. 1130-1133
    • Cohen, E.A.1    Gaudreau, P.2    Brazeau, P.3    Langelier, Y.4
  • 39
    • 0035066383 scopus 로고    scopus 로고
    • Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation
    • JM Kyriakis J Avruch 2001 Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation Physiol Rev 81 807 869 11274345 1:CAS:528:DC%2BD3MXislCrsb8%3D (Pubitemid 32267078)
    • (2001) Physiological Reviews , vol.81 , Issue.2 , pp. 807-869
    • Kyriakis, J.M.1    Avruch, J.2
  • 40
    • 13844273087 scopus 로고    scopus 로고
    • PI3K-Akt pathway: Its functions and alterations in human cancer
    • DOI 10.1023/B:APPT.0000045801.15585.dd
    • M Osaki M Oshimura H Ito 2004 PI3K-Akt pathway: its functions and alterations in human cancer Apoptosis 9 667 676 15505410 10.1023/B:APPT. 0000045801.15585.dd 1:CAS:528:DC%2BD2cXovVKqu70%3D (Pubitemid 40941196)
    • (2004) Apoptosis , vol.9 , Issue.6 , pp. 667-676
    • Osaki, M.1    Oshimura, M.2    Ito, H.3
  • 41
    • 52049088263 scopus 로고    scopus 로고
    • Resistance to TRAIL-induced apoptosis caused by constitutional phosphorylation of Akt and PTEN in acute lymphoblastic leukemia cells
    • 18599181 10.1016/j.exphem.2008.04.011 1:CAS:528:DC%2BD1cXhtFylsLnK
    • F Dida Y Li A Iwao T Deguchi E Azuma Y Komada 2008 Resistance to TRAIL-induced apoptosis caused by constitutional phosphorylation of Akt and PTEN in acute lymphoblastic leukemia cells Exp Hematol 36 1343 1353 18599181 10.1016/j.exphem.2008.04.011 1:CAS:528:DC%2BD1cXhtFylsLnK
    • (2008) Exp Hematol , vol.36 , pp. 1343-1353
    • Dida, F.1    Li, Y.2    Iwao, A.3    Deguchi, T.4    Azuma, E.5    Komada, Y.6
  • 43
    • 0029095455 scopus 로고
    • Intracellular internalization and signaling pathways triggered by the large subunit of HSV-2 ribonucleotide reductase (ICP10)
    • 7618272 10.1006/viro.1995.1351 1:CAS:528:DyaK2MXmvFWksbk%3D
    • JC Hunter CC Smith D Bose M Kulka R Broderick L Aurelian 1995 Intracellular internalization and signaling pathways triggered by the large subunit of HSV-2 ribonucleotide reductase (ICP10) Virology 210 345 360 7618272 10.1006/viro.1995.1351 1:CAS:528:DyaK2MXmvFWksbk%3D
    • (1995) Virology , vol.210 , pp. 345-360
    • Hunter, J.C.1    Smith, C.C.2    Bose, D.3    Kulka, M.4    Broderick, R.5    Aurelian, L.6
  • 44
    • 25844490942 scopus 로고    scopus 로고
    • The Fas-associated death domain protein/caspase-8/c-FLIP signaling pathway is involved in TNF-induced activation of ERK
    • DOI 10.1016/j.yexcr.2005.07.022, PII S0014482705003241
    • S Luschen M Falk G Scherer S Ussat M Paulsen S Adam-Klages 2005 The Fas-associated death domain protein/caspase-8/c-FLIP signaling pathway is involved in TNF-induced activation of ERK Exp Cell Res 310 33 42 16129431 10.1016/j.yexcr.2005.07.022 (Pubitemid 41393685)
    • (2005) Experimental Cell Research , vol.310 , Issue.1 , pp. 33-42
    • Luschen, S.1    Falk, M.2    Scherer, G.3    Ussat, S.4    Paulsen, M.5    Adam-Klages, S.6
  • 45
    • 0028884033 scopus 로고
    • PD 098059 is a specific inhibitor of the activation of mitogen-activated protein kinase kinase in vitro and in vivo
    • 7499206 10.1074/jbc.270.46.27489 1:CAS:528:DyaK2MXpsFShsLg%3D
    • DR Alessi A Cuenda P Cohen DT Dudley AR Saltiel 1995 PD 098059 is a specific inhibitor of the activation of mitogen-activated protein kinase kinase in vitro and in vivo J Biol Chem 270 27489 27494 7499206 10.1074/jbc.270.46. 27489 1:CAS:528:DyaK2MXpsFShsLg%3D
    • (1995) J Biol Chem , vol.270 , pp. 27489-27494
    • Alessi, D.R.1    Cuenda, A.2    Cohen, P.3    Dudley, D.T.4    Saltiel, A.R.5
  • 46
    • 0028170210 scopus 로고
    • A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002)
    • 8106507 1:CAS:528:DyaK2cXjtFGit78%3D
    • CJ Vlahos WF Matter KY Hui RF Brown 1994 A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002) J Biol Chem 269 5241 5248 8106507 1:CAS:528:DyaK2cXjtFGit78%3D
    • (1994) J Biol Chem , vol.269 , pp. 5241-5248
    • Vlahos, C.J.1    Matter, W.F.2    Hui, K.Y.3    Brown, R.F.4
  • 47
    • 16844387124 scopus 로고    scopus 로고
    • Role of JNK activation in apoptosis: A double-edged sword
    • DOI 10.1038/sj.cr.7290262
    • J Liu A Lin 2005 Role of JNK activation in apoptosis: a double-edged sword Cell Res 15 36 42 15686625 10.1038/sj.cr.7290262 (Pubitemid 41653963)
    • (2005) Cell Research , vol.15 , Issue.1 , pp. 36-42
    • Liu, J.1    Lin, A.2
  • 48
    • 0036289047 scopus 로고    scopus 로고
    • A time to kill: Viral manipulation of the cell death program
    • S Hay G Kannourakis 2002 A time to kill: viral manipulation of the cell death program J Gen Virol 83 1547 1564 12075073 1:CAS:528:DC%2BD38Xlt1Wgu74%3D (Pubitemid 34716260)
    • (2002) Journal of General Virology , vol.83 , Issue.7 , pp. 1547-1564
    • Hay, S.1    Kannourakis, G.2
  • 52
    • 0037184928 scopus 로고    scopus 로고
    • Activation of initiator caspases through a stable dimeric intermediate
    • DOI 10.1074/jbc.M210356200
    • M Chen A Orozco DM Spencer J Wang 2002 Activation of initiator caspases through a stable dimeric intermediate J Biol Chem 277 50761 50767 12399450 10.1074/jbc.M210356200 1:CAS:528:DC%2BD38Xps12ntLo%3D (Pubitemid 36042239)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.52 , pp. 50761-50767
    • Chen, M.1    Orozco, A.2    Spencer, D.M.3    Wang, J.4
  • 53
    • 17644399432 scopus 로고    scopus 로고
    • Two mechanisms of caspase 9 processing in double-stranded RNA- and virus-triggered apoptosis
    • DOI 10.1007/s10495-005-6070-y
    • MS Iordanov OP Ryabinina P Schneider BE Magun 2005 Two mechanisms of caspase 9 processing in double-stranded RNA- and virus-triggered apoptosis Apoptosis 10 153 166 15711931 10.1007/s10495-005-6070-y 1:CAS:528: DC%2BD2MXhsVWmsLk%3D (Pubitemid 40558123)
    • (2005) Apoptosis , vol.10 , Issue.1 , pp. 153-166
    • Iordanov, M.S.1    Ryabinina, O.P.2    Schneider, P.3    Magun, B.E.4
  • 54
    • 0036774155 scopus 로고    scopus 로고
    • Unstable receptors disappear from cell surface during poliovirus infection
    • 12388911 1:CAS:528:DC%2BD38XptVOns7s%3D
    • N Neznanov KP Chumakov A Ullrich VI Agol AV Gudkov 2002 Unstable receptors disappear from cell surface during poliovirus infection Med Sci Monit 8 BR391 BR396 12388911 1:CAS:528:DC%2BD38XptVOns7s%3D
    • (2002) Med Sci Monit , vol.8
    • Neznanov, N.1    Chumakov, K.P.2    Ullrich, A.3    Agol, V.I.4    Gudkov, A.V.5
  • 55
    • 0028873964 scopus 로고
    • Fas- and tumor necrosis factor-induced apoptosis is inhibited by the poxvirus crmA gene product
    • 7531702 10.1074/jbc.270.28.16526 1:CAS:528:DyaK2MXjslahu7s%3D
    • M Tewari VM Dixit 1995 Fas- and tumor necrosis factor-induced apoptosis is inhibited by the poxvirus crmA gene product J Biol Chem 270 3255 3260 7531702 10.1074/jbc.270.28.16526 1:CAS:528:DyaK2MXjslahu7s%3D
    • (1995) J Biol Chem , vol.270 , pp. 3255-3260
    • Tewari, M.1    Dixit, V.M.2
  • 57
    • 33646166625 scopus 로고    scopus 로고
    • Hepatitis C virus core protein inhibits tumor necrosis factor alpha-mediated apoptosis by a protective effect involving cellular FLICE inhibitory protein
    • 16611896 10.1128/JVI.80.9.4372-4379.2006 1:CAS:528:DC%2BD28Xkt1Orsrw%3D
    • K Saito K Meyer R Warner A Basu RB Ray R Ray 2006 Hepatitis C virus core protein inhibits tumor necrosis factor alpha-mediated apoptosis by a protective effect involving cellular FLICE inhibitory protein J Virol 80 4372 4379 16611896 10.1128/JVI.80.9.4372-4379.2006 1:CAS:528:DC%2BD28Xkt1Orsrw%3D
    • (2006) J Virol , vol.80 , pp. 4372-4379
    • Saito, K.1    Meyer, K.2    Warner, R.3    Basu, A.4    Ray, R.B.5    Ray, R.6
  • 58
    • 1642430634 scopus 로고    scopus 로고
    • Herpes simplex virus infection and apoptosis
    • ML Goodkin ER Morton JA Blaho 2004 Herpes simplex virus infection and apoptosis Int Rev Immunol 23 141 172 14690858 10.1080/08830180490265574 1:CAS:528:DC%2BD3sXpvV2lsLw%3D (Pubitemid 38121750)
    • (2004) International Reviews of Immunology , vol.23 , Issue.1-2 , pp. 141-172
    • Goodkin, M.L.1    Morton, E.R.2    Blaho, J.A.3
  • 59
    • 34548644394 scopus 로고    scopus 로고
    • The herpes simplex virus type 2 gene ICP10PK protects from apoptosis caused by nerve growth factor deprivation through inhibition of caspase-3 activation and XIAP up-regulation
    • DOI 10.1111/j.1471-4159.2007.04745.x
    • SQ Wales B Li JM Laing L Aurelian 2007 The herpes simplex virus type 2 gene ICP10PK protects from apoptosis caused by nerve growth factor deprivation through inhibition of caspase-3 activation and XIAP up-regulation J Neurochem 103 365 379 17877640 1:CAS:528:DC%2BD2sXht1Sjsr7N (Pubitemid 47404212)
    • (2007) Journal of Neurochemistry , vol.103 , Issue.1 , pp. 365-379
    • Wales, S.Q.1    Li, B.2    Laing, J.M.3    Aurelian, L.4
  • 60
    • 17144421545 scopus 로고    scopus 로고
    • Oleate promotes the proliferation of breast cancer cells via the G protein-coupled receptor GPR40
    • DOI 10.1074/jbc.M410922200
    • S Hardy GG St-Onge E Joly Y Langelier M Prentki 2005 Oleate promotes the proliferation of breast cancer cells via the G protein-coupled receptor GPR40 J Biol Chem 280 13285 13291 15695516 10.1074/jbc.M410922200 1:CAS:528: DC%2BD2MXivV2ksL4%3D (Pubitemid 40517213)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.14 , pp. 13285-13291
    • Hardy, S.1    St-Onge, G.G.2    Joly, E.3    Langelier, Y.4    Prentki, M.5
  • 61
    • 34247165442 scopus 로고    scopus 로고
    • The large and small isoforms of human papillomaviras type 16 E6 bind to and differentially affect procaspase 8 stability and activity
    • DOI 10.1128/JVI.01924-06
    • M Filippova MM Johnson M Bautista V Filippov N Fodor SS Tungteakkhun K Williams PJ Duerksen-Hughes 2007 The large and small isoforms of human papillomavirus type 16 E6 bind to and differentially affect procaspase 8 stability and activity J Virol 81 4116 4129 17267478 10.1128/JVI.01924-06 1:CAS:528:DC%2BD2sXksVKksL8%3D (Pubitemid 46586906)
    • (2007) Journal of Virology , vol.81 , Issue.8 , pp. 4116-4129
    • Filippova, M.1    Johnson, M.M.2    Bautista, M.3    Filippov, V.4    Fodor, N.5    Tungteakkhun, S.S.6    Williams, K.7    Duerksen-Hughes, P.J.8
  • 62
    • 2942525121 scopus 로고    scopus 로고
    • The human papillomavirus 16 E6 protein binds to Fas-associated death domain and protects cells from Fas-triggered apoptosis
    • DOI 10.1074/jbc.M401172200
    • M Filippova L Parkhurst PJ Duerksen-Hughes 2004 The human papillomavirus 16 E6 protein binds to Fas-associated death domain and protects cells from Fas-triggered apoptosis J Biol Chem 279 25729 25744 15073179 10.1074/jbc.M401172200 1:CAS:528:DC%2BD2cXksFygtL0%3D (Pubitemid 38756837)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.24 , pp. 25729-25744
    • Filippova, M.1    Parkhurst, L.2    Duerksen-Hughes, P.J.3
  • 64
    • 0032584081 scopus 로고    scopus 로고
    • Herpes simplex virus 1 induces and blocks apoptosis at multiple steps during infection and protects cells from exogenous inducers in a cell-type- dependent manner
    • DOI 10.1073/pnas.95.7.3931
    • V Galvan B Roizman 1998 Herpes simplex virus 1 induces and blocks apoptosis at multiple steps during infection and protects cells from exogenous inducers in a cell-type-dependent manner Proc Natl Acad Sci USA 95 3931 3936 9520470 10.1073/pnas.95.7.3931 1:CAS:528:DyaK1cXitlKjurY%3D (Pubitemid 28173231)
    • (1998) Proceedings of the National Academy of Sciences of the United States of America , vol.95 , Issue.7 , pp. 3931-3936
    • Galvan, V.1    Roizman, B.2
  • 65
    • 0344982847 scopus 로고    scopus 로고
    • Differential function and expression of the viral inhibitor of caspase 8-induced apoptosis (vICA) and the viral mitochondria-localized inhibitor of apoptosis (vMIA) cell death suppressors conserved in primate and rodent cytomegaloviruses
    • DOI 10.1016/j.virol.2003.07.003
    • AL McCormick A Skaletskaya PA Barry ES Mocarski VS Goldmacher 2003 Differential function and expression of the viral inhibitor of caspase 8-induced apoptosis (vICA) and the viral mitochondria-localized inhibitor of apoptosis (vMIA) cell death suppressors conserved in primate and rodent cytomegaloviruses Virology 316 221 233 14644605 10.1016/j.virol.2003.07.003 1:CAS:528: DC%2BD3sXpsVSlsb8%3D (Pubitemid 37468526)
    • (2003) Virology , vol.316 , Issue.2 , pp. 221-233
    • McCormick, A.L.1    Skaletskaya, A.2    Barry, P.A.3    Mocarski, E.S.4    Goldmacher, V.S.5
  • 66
    • 61449175831 scopus 로고    scopus 로고
    • Structural and biochemical studies on procaspase-8: New insights on initiator caspase activation
    • 19278658 10.1016/j.str.2008.12.019 1:CAS:528:DC%2BD1MXivVKisbY%3D
    • N Keller J Mares O Zerbe MG Grutter 2009 Structural and biochemical studies on procaspase-8: new insights on initiator caspase activation Structure 17 438 448 19278658 10.1016/j.str.2008.12.019 1:CAS:528:DC%2BD1MXivVKisbY%3D
    • (2009) Structure , vol.17 , pp. 438-448
    • Keller, N.1    Mares, J.2    Zerbe, O.3    Grutter, M.G.4
  • 67
    • 33744539048 scopus 로고    scopus 로고
    • The Structure of FADD and Its Mode of Interaction with Procaspase-8
    • DOI 10.1016/j.molcel.2006.04.018, PII S1097276506002668
    • PE Carrington C Sandu Y Wei JM Hill G Morisawa T Huang E Gavathiotis Y Wei MH Werner 2006 The structure of FADD and its mode of interaction with procaspase-8 Mol Cell 22 599 610 16762833 10.1016/j.molcel.2006.04.018 1:CAS:528:DC%2BD28XmtFSrurk%3D (Pubitemid 43817600)
    • (2006) Molecular Cell , vol.22 , Issue.5 , pp. 599-610
    • Carrington, P.E.1    Sandu, C.2    Wei, Y.3    Hill, J.M.4    Morisawa, G.5    Huang, T.6    Gavathiotis, E.7    Wei, Y.8    Werner, M.H.9
  • 68
    • 58149279459 scopus 로고    scopus 로고
    • Tinkering with a viral ribonucleotide reductase
    • 18990579 10.1016/j.tibs.2008.09.008 1:CAS:528:DC%2BD1MXktl2gsQ%3D%3D
    • D Lembo W Brune 2009 Tinkering with a viral ribonucleotide reductase Trends Biochem Sci 34 25 32 18990579 10.1016/j.tibs.2008.09.008 1:CAS:528:DC%2BD1MXktl2gsQ%3D%3D
    • (2009) Trends Biochem Sci , vol.34 , pp. 25-32
    • Lembo, D.1    Brune, W.2
  • 69
    • 77950499409 scopus 로고    scopus 로고
    • Viral strategies for the evasion of immunogenic cell death
    • 20433579 10.1111/j.1365-2796.2010.02223.x 1:CAS:528:DC%2BC3cXmsleqt7o%3D
    • L Galluzzi O Kepp E Morselli I Vitale L Senovilla M Pinti L Zitvogel G Kroemer 2010 Viral strategies for the evasion of immunogenic cell death J Intern Med 267 526 542 20433579 10.1111/j.1365-2796.2010.02223.x 1:CAS:528: DC%2BC3cXmsleqt7o%3D
    • (2010) J Intern Med , vol.267 , pp. 526-542
    • Galluzzi, L.1    Kepp, O.2    Morselli, E.3    Vitale, I.4    Senovilla, L.5    Pinti, M.6    Zitvogel, L.7    Kroemer, G.8
  • 70
    • 73849104260 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 (HSV-1)-induced apoptosis in human dendritic cells as a result of downregulation of cellular FLICE-inhibitory protein and reduced expression of HSV-1 antiapoptotic latency-associated transcript sequences
    • 19906927 10.1128/JVI.01409-09 1:CAS:528:DC%2BC3cXisFyksrk%3D
    • A Kather MJ Raftery G Devi-Rao J Lippmann T Giese RM Sandri-Goldin G Schonrich 2010 Herpes simplex virus type 1 (HSV-1)-induced apoptosis in human dendritic cells as a result of downregulation of cellular FLICE-inhibitory protein and reduced expression of HSV-1 antiapoptotic latency-associated transcript sequences J Virol 84 1034 1046 19906927 10.1128/JVI.01409-09 1:CAS:528:DC%2BC3cXisFyksrk%3D
    • (2010) J Virol , vol.84 , pp. 1034-1046
    • Kather, A.1    Raftery, M.J.2    Devi-Rao, G.3    Lippmann, J.4    Giese, T.5    Sandri-Goldin, R.M.6    Schonrich, G.7
  • 71
    • 33846476600 scopus 로고    scopus 로고
    • Tumor necrosis factor (TNF) protects resistant C57BL/6 mice against herpes simplex virus-induced encephalitis independently of signaling via TNF receptor 1 or 2
    • DOI 10.1128/JVI.02243-06
    • P Lundberg PV Welander CK Edwards 3rd N van Rooijen E Cantin 2007 Tumor necrosis factor (TNF) protects resistant C57BL/6 mice against herpes simplex virus-induced encephalitis independently of signaling via TNF receptor 1 or 2 J Virol 81 1451 1460 17108044 10.1128/JVI.02243-06 1:CAS:528:DC%2BD2sXhtFCnsrY%3D (Pubitemid 46167866)
    • (2007) Journal of Virology , vol.81 , Issue.3 , pp. 1451-1460
    • Lundberg, P.1    Welander, P.V.2    Edwards III, C.K.3    Van Rooijen, N.4    Cantin, E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.