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Volumn 267, Issue 5, 2010, Pages 526-542

Viral strategies for the evasion of immunogenic cell death: Symposium

Author keywords

BAP31; Bax; Calreticulin; Caspases; Eif2 ; PERK

Indexed keywords

ADENOSINE DEAMINASE; CALNEXIN; CALRETICULIN; DOUBLE STRANDED RNA; INITIATION FACTOR 2ALPHA; MITOCHONDRIAL PERMEABILITY TRANSITION PORE; PHOSPHOPROTEIN PHOSPHATASE; POLYADENYLIC ACID BINDING PROTEIN; PROTEIN KINASE; RNA BINDING PROTEIN; SYNAPTOBREVIN 1; VIRUS PROTEIN;

EID: 77950499409     PISSN: 09546820     EISSN: 13652796     Source Type: Journal    
DOI: 10.1111/j.1365-2796.2010.02223.x     Document Type: Conference Paper
Times cited : (54)

References (168)
  • 1
    • 32944462309 scopus 로고    scopus 로고
    • Anti-immunology: Evasion of the host immune system by bacterial and viral pathogens
    • DOI 10.1016/j.cell.2006.01.034, PII S0092867406001322
    • Finlay BB, McFadden G. Anti-immunology: evasion of the host immune system by bacterial and viral pathogens. Cell 2006 124 : 767 782. (Pubitemid 43261451)
    • (2006) Cell , vol.124 , Issue.4 , pp. 767-782
    • Finlay, B.B.1    McFadden, G.2
  • 3
    • 33845977959 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization in cell death
    • DOI 10.1152/physrev.00013.2006
    • Kroemer G, Galluzzi L, Brenner C. Mitochondrial membrane permeabilization in cell death. Physiol Rev 2007 87 : 99 163. (Pubitemid 46209992)
    • (2007) Physiological Reviews , vol.87 , Issue.1 , pp. 99-163
    • Kroemer, G.1    Galluzzi, L.2    Brenner, C.3
  • 4
    • 57649149333 scopus 로고    scopus 로고
    • Classification of cell death: Recommendations of the Nomenclature Committee on Cell Death 2009
    • Kroemer G, Galluzzi L, Vandenabeele P et al. Classification of cell death: recommendations of the Nomenclature Committee on Cell Death 2009. Cell Death Differ 2009 16 : 3 11.
    • (2009) Cell Death Differ , vol.16 , pp. 3-11
    • Kroemer, G.1    Galluzzi, L.2    Vandenabeele, P.3
  • 5
    • 57649167477 scopus 로고    scopus 로고
    • Necroptosis: A specialized pathway of programmed necrosis
    • Galluzzi L, Kroemer G. Necroptosis: a specialized pathway of programmed necrosis. Cell 2008 135 : 1161 1163.
    • (2008) Cell , vol.135 , pp. 1161-1163
    • Galluzzi, L.1    Kroemer, G.2
  • 6
    • 33846018602 scopus 로고    scopus 로고
    • Cell death by necrosis: towards a molecular definition
    • DOI 10.1016/j.tibs.2006.11.001, PII S0968000406003185
    • Golstein P, Kroemer G. Cell death by necrosis: towards a molecular definition. Trends Biochem Sci 2007 32 : 37 43. (Pubitemid 46043552)
    • (2007) Trends in Biochemical Sciences , vol.32 , Issue.1 , pp. 37-43
    • Golstein, P.1    Kroemer, G.2
  • 12
    • 75749147533 scopus 로고    scopus 로고
    • Immunogenic death of colon cancer cells treated with oxaliplatin
    • Tesniere A, Schlemmer F, Kepp O et al. Immunogenic death of colon cancer cells treated with oxaliplatin. Oncogene 2010 29 : 482 491.
    • (2010) Oncogene , vol.29 , pp. 482-491
    • Tesniere, A.1    Schlemmer, F.2    Kepp, O.3
  • 13
    • 70350569295 scopus 로고    scopus 로고
    • Activation of the NLRP3 inflammasome in dendritic cells induces IL-1beta-dependent adaptive immunity against tumors
    • Ghiringhelli F, Apetoh L, Tesniere A et al. Activation of the NLRP3 inflammasome in dendritic cells induces IL-1beta-dependent adaptive immunity against tumors. Nat Med 2009 15 : 1170 1178.
    • (2009) Nat Med , vol.15 , pp. 1170-1178
    • Ghiringhelli, F.1    Apetoh, L.2    Tesniere, A.3
  • 14
    • 62449131194 scopus 로고    scopus 로고
    • Immunogenic cell death modalities and their impact on cancer treatment
    • Kepp O, Tesniere A, Schlemmer F et al. Immunogenic cell death modalities and their impact on cancer treatment. Apoptosis 2009 14 : 364 375.
    • (2009) Apoptosis , vol.14 , pp. 364-375
    • Kepp, O.1    Tesniere, A.2    Schlemmer, F.3
  • 15
    • 49949115791 scopus 로고    scopus 로고
    • The co-translocation of ERp57 and calreticulin determines the immunogenicity of cell death
    • Panaretakis T, Joza N, Modjtahedi N et al. The co-translocation of ERp57 and calreticulin determines the immunogenicity of cell death. Cell Death Differ 2008 15 : 1499 1509.
    • (2008) Cell Death Differ , vol.15 , pp. 1499-1509
    • Panaretakis, T.1    Joza, N.2    Modjtahedi, N.3
  • 16
    • 62049085194 scopus 로고    scopus 로고
    • Mechanisms of pre-apoptotic calreticulin exposure in immunogenic cell death
    • Panaretakis T, Kepp O, Brockmeier U et al. Mechanisms of pre-apoptotic calreticulin exposure in immunogenic cell death. EMBO J 2009 28 : 578 590.
    • (2009) EMBO J , vol.28 , pp. 578-590
    • Panaretakis, T.1    Kepp, O.2    Brockmeier, U.3
  • 17
    • 42449121506 scopus 로고    scopus 로고
    • PKR in innate immunity, cancer, and viral oncolysis
    • Balachandran S, Barber GN. PKR in innate immunity, cancer, and viral oncolysis. Methods Mol Biol 2007 383 : 277 301.
    • (2007) Methods Mol Biol , vol.383 , pp. 277-301
    • Balachandran, S.1    Barber, G.N.2
  • 19
    • 33644609471 scopus 로고    scopus 로고
    • PKR-dependent autophagic degradation of herpes simplex virus type 1
    • Talloczy Z, Virgin HWt, Levine B. PKR-dependent autophagic degradation of herpes simplex virus type 1. Autophagy 2006 2 : 24 9. (Pubitemid 43310359)
    • (2006) Autophagy , vol.2 , Issue.1 , pp. 24-29
    • Talloczy, Z.1    Virgin IV, H.W.2    Levine, B.3
  • 20
    • 34347225099 scopus 로고    scopus 로고
    • The dsRNA protein kinase PKR: Virus and cell control
    • Garcia MA, Meurs EF, Esteban M. The dsRNA protein kinase PKR: virus and cell control. Biochimie 2007 89 : 799 811.
    • (2007) Biochimie , vol.89 , pp. 799-811
    • Garcia, M.A.1    Meurs, E.F.2    Esteban, M.3
  • 21
    • 44349125754 scopus 로고    scopus 로고
    • PERK and PKR: Old kinases learn new tricks
    • Raven JF, Koromilas AE. PERK and PKR: old kinases learn new tricks. Cell Cycle 2008 7 : 1146 1150.
    • (2008) Cell Cycle , vol.7 , pp. 1146-1150
    • Raven, J.F.1    Koromilas, A.E.2
  • 22
    • 0030992545 scopus 로고    scopus 로고
    • A double-stranded RNA-activated protein kinase-dependent pathway mediating stress-induced apoptosis
    • Der SD, Yang YL, Weissmann C, Williams BR. A double-stranded RNA-activated protein kinase-dependent pathway mediating stress-induced apoptosis. Proc Natl Acad Sci USA 1997 94 : 3279 3283.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 3279-3283
    • Der, S.D.1    Yang, Y.L.2    Weissmann, C.3    Williams, B.R.4
  • 23
    • 32544446451 scopus 로고    scopus 로고
    • Coping with stress: EIF2 kinases and translational control
    • Wek RC, Jiang HY, Anthony TG. Coping with stress: eIF2 kinases and translational control. Biochem Soc Trans 2006 34 : 7 11.
    • (2006) Biochem Soc Trans , vol.34 , pp. 7-11
    • Wek, R.C.1    Jiang, H.Y.2    Anthony, T.G.3
  • 24
    • 35748977389 scopus 로고    scopus 로고
    • Nck-1 selectively modulates eIF2αSer51 phosphorylation by a subset of eIF2α-kinases
    • DOI 10.1111/j.1742-4658.2007.06110.x
    • Cardin E, Latreille M, Khoury C, Greenwood MT, Larose L. Nck-1 selectively modulates eIF2alphaSer51 phosphorylation by a subset of eIF2alpha-kinases. FEBS J 2007 274 : 5865 5875. (Pubitemid 350045800)
    • (2007) FEBS Journal , vol.274 , Issue.22 , pp. 5865-5875
    • Cardin, E.1    Latreille, M.2    Khoury, C.3    Greenwood, M.T.4    Larose, L.5
  • 25
    • 33645142635 scopus 로고    scopus 로고
    • Viruses, endoplasmic reticulum stress, and interferon responses
    • He B. Viruses, endoplasmic reticulum stress, and interferon responses. Cell Death Differ 2006 13 : 393 403.
    • (2006) Cell Death Differ , vol.13 , pp. 393-403
    • He, B.1
  • 26
    • 65349092744 scopus 로고    scopus 로고
    • Viral subversion of immunogenic cell death
    • Kepp O, Senovilla L, Galluzzi L et al. Viral subversion of immunogenic cell death. Cell Cycle 2009 8 : 860 869.
    • (2009) Cell Cycle , vol.8 , pp. 860-869
    • Kepp, O.1    Senovilla, L.2    Galluzzi, L.3
  • 27
    • 0035947778 scopus 로고    scopus 로고
    • Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2α
    • DOI 10.1083/jcb.153.5.1011
    • Novoa I, Zeng H, Harding HP, Ron D. Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2alpha. J Cell Biol 2001 153 : 1011 1022. (Pubitemid 34289240)
    • (2001) Journal of Cell Biology , vol.153 , Issue.5 , pp. 1011-1021
    • Novoa, I.1    Zeng, H.2    Harding, H.P.3    Ron, D.4
  • 28
    • 0034715581 scopus 로고    scopus 로고
    • Pseudosubstrate inhibition of protein kinase PKR by swine pox virus C8L gene product
    • Kawagishi-Kobayashi M, Cao C, Lu J, Ozato K, Dever TE. Pseudosubstrate inhibition of protein kinase PKR by swine pox virus C8L gene product. Virology 2000 276 : 424 434.
    • (2000) Virology , vol.276 , pp. 424-434
    • Kawagishi-Kobayashi, M.1    Cao, C.2    Lu, J.3    Ozato, K.4    Dever, T.E.5
  • 29
    • 0037333913 scopus 로고    scopus 로고
    • Protein synthesis and endoplasmic reticulum stress can be modulated by the hepatitis C virus envelope protein E2 through the eukaryotic initiation factor 2α kinase PERK
    • DOI 10.1128/JVI.77.6.3578-3585.2003
    • Pavio N, Romano PR, Graczyk TM, Feinstone SM, Taylor DR. Protein synthesis and endoplasmic reticulum stress can be modulated by the hepatitis C virus envelope protein E2 through the eukaryotic initiation factor 2alpha kinase PERK. J Virol 2003 77 : 3578 3585. (Pubitemid 36297277)
    • (2003) Journal of Virology , vol.77 , Issue.6 , pp. 3578-3585
    • Pavio, N.1    Romano, P.R.2    Graczyk, T.M.3    Feinstone, S.M.4    Taylor, D.R.5
  • 30
    • 0036670396 scopus 로고    scopus 로고
    • X-ray crystal structure and functional analysis of vaccinia virus K3L reveals molecular determinants for PKR subversion and substrate recognition
    • DOI 10.1016/S1097-2765(02)00590-7
    • Dar AC, Sicheri F. X-ray crystal structure and functional analysis of vaccinia virus K3L reveals molecular determinants for PKR subversion and substrate recognition. Mol Cell 2002 10 : 295 305. (Pubitemid 35007344)
    • (2002) Molecular Cell , vol.10 , Issue.2 , pp. 295-305
    • Dar, A.C.1    Sicheri, F.2
  • 31
    • 0036409394 scopus 로고    scopus 로고
    • Myxoma virus immunomodulatory protein M156R is a structural mimic of eukaryotic translation initiation factor eIF2alpha
    • Ramelot TA, Cort JR, Yee AA et al. Myxoma virus immunomodulatory protein M156R is a structural mimic of eukaryotic translation initiation factor eIF2alpha. J Mol Biol 2002 322 : 943 954.
    • (2002) J Mol Biol , vol.322 , pp. 943-954
    • Ramelot, T.A.1    Cort, J.R.2    Yee, A.A.3
  • 32
    • 0030928832 scopus 로고    scopus 로고
    • The Tat protein of human immunodeficiency virus type 1 is a substrate and inhibitor of the interferon-induced, virally activated protein kinase, PKR
    • DOI 10.1074/jbc.272.13.8388
    • Brand SR, Kobayashi R, Mathews MB. The Tat protein of human immunodeficiency virus type 1 is a substrate and inhibitor of the interferon-induced, virally activated protein kinase, PKR. J Biol Chem 1997 272 : 8388 8395. (Pubitemid 27147798)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.13 , pp. 8388-8395
    • Brand, S.R.1    Kobayashi, R.2    Mathews, M.B.3
  • 34
    • 0032566917 scopus 로고    scopus 로고
    • The vaccinia virus E3L gene product interacts with both the regulatory and the substrate binding regions of PKR: Implications for PKR autoregulation
    • DOI 10.1006/viro.1998.9365
    • Sharp TV, Moonan F, Romashko A, Joshi B, Barber GN, Jagus R. The vaccinia virus E3L gene product interacts with both the regulatory and the substrate binding regions of PKR: implications for PKR autoregulation. Virology 1998 250 : 302 315. (Pubitemid 28489630)
    • (1998) Virology , vol.250 , Issue.2 , pp. 302-315
    • Sharp, T.V.1    Moonan, F.2    Romashko, A.3    Joshi, B.4    Barber, G.N.5    Jagus, R.6
  • 35
    • 33947428335 scopus 로고    scopus 로고
    • Maintenance of endoplasmic reticulum (ER) homeostasis in herpes simplex virus type 1-infected cells through the association of a viral glycoprotein with PERK, a cellular ER stress sensor
    • DOI 10.1128/JVI.02191-06
    • Mulvey M, Arias C, Mohr I. Maintenance of endoplasmic reticulum (ER) homeostasis in herpes simplex virus type 1-infected cells through the association of a viral glycoprotein with PERK, a cellular ER stress sensor. J Virol 2007 81 : 3377 3390. (Pubitemid 46456647)
    • (2007) Journal of Virology , vol.81 , Issue.7 , pp. 3377-3390
    • Mulvey, M.1    Arias, C.2    Mohr, I.3
  • 36
    • 21644460103 scopus 로고    scopus 로고
    • Human cytomegalovirus TRS1 and IRS1 gene products block the double-stranded-RNA-activated host protein shutoff response induced by herpes simplex virus type 1 infection
    • Cassady KA. Human cytomegalovirus TRS1 and IRS1 gene products block the double-stranded-RNA-activated host protein shutoff response induced by herpes simplex virus type 1 infection. J Virol 2005 79 : 8707 8715.
    • (2005) J Virol , vol.79 , pp. 8707-8715
    • Cassady, K.A.1
  • 37
    • 33749502236 scopus 로고    scopus 로고
    • Murine cytomegalovirus m142 and m143 are both required to block protein kinase R-mediated shutdown of protein synthesis
    • DOI 10.1128/JVI.00908-06
    • Valchanova RS, Picard-Maureau M, Budt M, Brune W. Murine cytomegalovirus m142 and m143 are both required to block protein kinase R-mediated shutdown of protein synthesis. J Virol 2006 80 : 10181 10190. (Pubitemid 44522611)
    • (2006) Journal of Virology , vol.80 , Issue.20 , pp. 10181-10190
    • Valchanova, R.S.1    Picard-Maureau, M.2    Budt, M.3    Brune, W.4
  • 38
    • 33749492981 scopus 로고    scopus 로고
    • Double-stranded RNA binding by a heterodimeric complex of murine cytomegalovirus m142 and m143 proteins
    • Child SJ, Hanson LK, Brown CE, Janzen DM, Geballe AP. Double-stranded RNA binding by a heterodimeric complex of murine cytomegalovirus m142 and m143 proteins. J Virol 2006 80 : 10173 10180.
    • (2006) J Virol , vol.80 , pp. 10173-10180
    • Child, S.J.1    Hanson, L.K.2    Brown, C.E.3    Janzen, D.M.4    Geballe, A.P.5
  • 39
    • 59649110305 scopus 로고    scopus 로고
    • Binding and relocalization of protein kinase R by murine cytomegalovirus
    • Child SJ, Geballe AP. Binding and relocalization of protein kinase R by murine cytomegalovirus. J Virol 2009 83 : 1790 1799.
    • (2009) J Virol , vol.83 , pp. 1790-1799
    • Child, S.J.1    Geballe, A.P.2
  • 40
    • 33646517711 scopus 로고    scopus 로고
    • Binding of the influenza A virus NS1 protein to PKR mediates the inhibition of its activation by either PACT or double-stranded RNA
    • Li S, Min JY, Krug RM, Sen GC. Binding of the influenza A virus NS1 protein to PKR mediates the inhibition of its activation by either PACT or double-stranded RNA. Virology 2006 349 : 13 21.
    • (2006) Virology , vol.349 , pp. 13-21
    • Li, S.1    Min, J.Y.2    Krug, R.M.3    Sen, G.C.4
  • 42
    • 0037213277 scopus 로고    scopus 로고
    • Identification of a lytic-cycle epstein-barr virus gene product that can regulate PKR activation
    • DOI 10.1128/JVI.77.1.228-236.2003
    • Poppers J, Mulvey M, Perez C, Khoo D, Mohr I. Identification of a lytic-cycle Epstein-Barr virus gene product that can regulate PKR activation. J Virol 2003 77 : 228 236. (Pubitemid 36004963)
    • (2003) Journal of Virology , vol.77 , Issue.1 , pp. 228-236
    • Poppers, J.1    Mulvey, M.2    Perez, C.3    Khoo, D.4    Mohr, I.5
  • 43
    • 0141566327 scopus 로고    scopus 로고
    • Regulation of eIF2α phosphorylation by different functions that act during discrete phases in the herpes simplex virus type 1 life cycle
    • DOI 10.1128/JVI.77.20.10917-10928.2003
    • Mulvey M, Poppers J, Sternberg D, Mohr I. Regulation of eIF2alpha phosphorylation by different functions that act during discrete phases in the herpes simplex virus type 1 life cycle. J Virol 2003 77 : 10917 10928. (Pubitemid 37204285)
    • (2003) Journal of Virology , vol.77 , Issue.20 , pp. 10917-10928
    • Mulvey, M.1    Poppers, J.2    Sternberg, D.3    Mohr, I.4
  • 44
    • 0035125267 scopus 로고    scopus 로고
    • Latently expressed human herpesvirus 8-encoded interferon regulatory factor 2 inhibits double-stranded RNA-activated protein kinase
    • DOI 10.1128/JVI.75.5.2345-2352.2001
    • Burysek L, Pitha PM. Latently expressed human herpesvirus 8-encoded interferon regulatory factor 2 inhibits double-stranded RNA-activated protein kinase. J Virol 2001 75 : 2345 2352. (Pubitemid 32147573)
    • (2001) Journal of Virology , vol.75 , Issue.5 , pp. 2345-2352
    • Burysek, L.1    Pitha, P.M.2
  • 45
    • 69249205651 scopus 로고    scopus 로고
    • Ebola virus VP35 antagonizes PKR activity through its C-terminal interferon inhibitory domain
    • Schumann M, Gantke T, Muhlberger E. Ebola virus VP35 antagonizes PKR activity through its C-terminal interferon inhibitory domain. J Virol 2009 83 : 8993 8997.
    • (2009) J Virol , vol.83 , pp. 8993-8997
    • Schumann, M.1    Gantke, T.2    Muhlberger, E.3
  • 46
    • 33750264663 scopus 로고    scopus 로고
    • Human papillomaviruses target the double-stranded RNA protein kinase pathway
    • DOI 10.1099/vir.0.82098-0
    • Hebner CM, Wilson R, Rader J, Bidder M, Laimins LA. Human papillomaviruses target the double-stranded RNA protein kinase pathway. J Gen Virol 2006 87 : 3183 3193. (Pubitemid 44608353)
    • (2006) Journal of General Virology , vol.87 , Issue.11 , pp. 3183-3193
    • Hebner, C.M.1    Wilson, R.2    Rader, J.3    Bidder, M.4    Laimins, L.A.5
  • 47
    • 33751224189 scopus 로고    scopus 로고
    • Binding and nuclear relocalization of protein kinase R by human cytomegalovirus TRS1
    • Hakki M, Marshall EE, De Niro KL, Geballe AP. Binding and nuclear relocalization of protein kinase R by human cytomegalovirus TRS1. J Virol 2006 80 : 11817 11826.
    • (2006) J Virol , vol.80 , pp. 11817-11826
    • Hakki, M.1    Marshall, E.E.2    De Niro, K.L.3    Geballe, A.P.4
  • 48
    • 53749086902 scopus 로고    scopus 로고
    • Sendai virus C protein plays a role in restricting PKR activation by limiting the generation of intracellular double-stranded RNA
    • Takeuchi K, Komatsu T, Kitagawa Y, Sada K, Gotoh B. Sendai virus C protein plays a role in restricting PKR activation by limiting the generation of intracellular double-stranded RNA. J Virol 2008 82 : 10102 10110.
    • (2008) J Virol , vol.82 , pp. 10102-10110
    • Takeuchi, K.1    Komatsu, T.2    Kitagawa, Y.3    Sada, K.4    Gotoh, B.5
  • 49
    • 0038653477 scopus 로고    scopus 로고
    • Evidence that avian reovirus sigmaA protein is an inhibitor of the double-stranded RNA-dependent protein kinase
    • Gonzalez-Lopez C, Martinez-Costas J, Esteban M, Benavente J. Evidence that avian reovirus sigmaA protein is an inhibitor of the double-stranded RNA-dependent protein kinase. J Gen Virol 2003 84 : 1629 1639.
    • (2003) J Gen Virol , vol.84 , pp. 1629-1639
    • Gonzalez-Lopez, C.1    Martinez-Costas, J.2    Esteban, M.3    Benavente, J.4
  • 50
    • 19944372421 scopus 로고    scopus 로고
    • Double-stranded RNA binding by human cytomegalovirus pTRS1
    • Hakki M, Geballe AP. Double-stranded RNA binding by human cytomegalovirus pTRS1. J Virol 2005 79 : 7311 7318.
    • (2005) J Virol , vol.79 , pp. 7311-7318
    • Hakki, M.1    Geballe, A.P.2
  • 52
    • 0031710037 scopus 로고    scopus 로고
    • The herpes simplex virus US11 protein effectively compensates for the gamma1(34.5) gene if present before activation of protein kinase R by precluding its phosphorylation and that of the alpha subunit of eukaryotic translation initiation factor 2
    • Cassady KA, Gross M, Roizman B. The herpes simplex virus US11 protein effectively compensates for the gamma1(34.5) gene if present before activation of protein kinase R by precluding its phosphorylation and that of the alpha subunit of eukaryotic translation initiation factor 2. J Virol 1998 72 : 8620 8626.
    • (1998) J Virol , vol.72 , pp. 8620-8626
    • Cassady, K.A.1    Gross, M.2    Roizman, B.3
  • 54
    • 70349283034 scopus 로고    scopus 로고
    • ADAR1 interacts with PKR during HIV infection of lymphocytes and contributes to viral replication
    • Clerzius G, Gelinas JF, Daher A, Bonnet M, Meurs EF, Gatignol A. ADAR1 interacts with PKR during HIV infection of lymphocytes and contributes to viral replication. J Virol 2009 83 : 10119 10128.
    • (2009) J Virol , vol.83 , pp. 10119-10128
    • Clerzius, G.1    Gelinas, J.F.2    Daher, A.3    Bonnet, M.4    Meurs, E.F.5    Gatignol, A.6
  • 55
    • 58149463628 scopus 로고    scopus 로고
    • TRBP control of PACT-induced phosphorylation of protein kinase R is reversed by stress
    • Daher A, Laraki G, Singh M et al. TRBP control of PACT-induced phosphorylation of protein kinase R is reversed by stress. Mol Cell Biol 2009 29 : 254 265.
    • (2009) Mol Cell Biol , vol.29 , pp. 254-265
    • Daher, A.1    Laraki, G.2    Singh, M.3
  • 56
    • 0036839211 scopus 로고    scopus 로고
    • Inhibition of PACT-mediated activation of PKR by the herpes simplex virus type 1 Us11 protein
    • DOI 10.1128/JVI.76.21.11054-11064.2002
    • Peters GA, Khoo D, Mohr I, Sen GC. Inhibition of PACT-mediated activation of PKR by the herpes simplex virus type 1 Us11 protein. J Virol 2002 76 : 11054 11064. (Pubitemid 35176222)
    • (2002) Journal of Virology , vol.76 , Issue.21 , pp. 11054-11064
    • Peters, G.A.1    Khoo, D.2    Mohr, I.3    Sen, G.C.4
  • 57
    • 47749109063 scopus 로고    scopus 로고
    • Systematic deletion of the adenovirus-associated RNAI terminal stem reveals a surprisingly active RNA inhibitor of double-stranded RNA-activated protein kinase
    • Wahid AM, Coventry VK, Conn GL. Systematic deletion of the adenovirus-associated RNAI terminal stem reveals a surprisingly active RNA inhibitor of double-stranded RNA-activated protein kinase. J Biol Chem 2008 283 : 17485 17493.
    • (2008) J Biol Chem , vol.283 , pp. 17485-17493
    • Wahid, A.M.1    Coventry, V.K.2    Conn, G.L.3
  • 58
    • 0032516518 scopus 로고    scopus 로고
    • 134.5 Protein of herpes simplex virus I has the structural and functional attributes of a protein phosphatase I regulatory subunit and is present in a high molecular weight complex with the enzyme in infected cells
    • DOI 10.1074/jbc.273.33.20737
    • He B, Gross M, Roizman B. The gamma134.5 protein of herpes simplex virus 1 has the structural and functional attributes of a protein phosphatase 1 regulatory subunit and is present in a high molecular weight complex with the enzyme in infected cells. J Biol Chem 1998 273 : 20737 20743. (Pubitemid 28385349)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.33 , pp. 20737-20743
    • He, B.1    Gross, M.2    Roizman, B.3
  • 59
    • 0031017382 scopus 로고    scopus 로고
    • 134.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1α to dephosphorylate the α subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA-activated protein kinase
    • DOI 10.1073/pnas.94.3.843
    • He B, Gross M, Roizman B. The gamma(1)34.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1alpha to dephosphorylate the alpha subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA-activated protein kinase. Proc Natl Acad Sci USA 1997 94 : 843 848. (Pubitemid 27074409)
    • (1997) Proceedings of the National Academy of Sciences of the United States of America , vol.94 , Issue.3 , pp. 843-848
    • He, B.1    Gross, M.2    Roizman, B.3
  • 60
    • 1842505312 scopus 로고    scopus 로고
    • Control of α Subunit of Eukaryotic Translation Initiation Factor 2 (eIF2α) Phosphorylation by the Human Papillomavirus Type 18 E6 Oncoprotein: Implications for eIF2α-Dependent Gene Expression and Cell Death
    • DOI 10.1128/MCB.24.8.3415-3429.2004
    • Kazemi S, Papadopoulou S, Li S et al. Control of alpha subunit of eukaryotic translation initiation factor 2 (eIF2 alpha) phosphorylation by the human papillomavirus type 18 E6 oncoprotein: implications for eIF2 alpha-dependent gene expression and cell death. Mol Cell Biol 2004 24 : 3415 3429. (Pubitemid 38452084)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.8 , pp. 3415-3429
    • Kazemi, S.1    Papadopoulou, S.2    Li, S.3    Su, Q.4    Wang, S.5    Yoshimura, A.6    Matlashewski, G.7    Dever, T.E.8    Koromilas, A.E.9
  • 61
    • 38349138566 scopus 로고    scopus 로고
    • Rotavirus infection induces the phosphorylation of eIF2alpha but prevents the formation of stress granules
    • Montero H, Rojas M, Arias CF, Lopez S. Rotavirus infection induces the phosphorylation of eIF2alpha but prevents the formation of stress granules. J Virol 2008 82 : 1496 1504.
    • (2008) J Virol , vol.82 , pp. 1496-1504
    • Montero, H.1    Rojas, M.2    Arias, C.F.3    Lopez, S.4
  • 62
    • 55949121681 scopus 로고    scopus 로고
    • Protein kinase PKR mutants resistant to the poxvirus pseudosubstrate K3L protein
    • Seo EJ, Liu F, Kawagishi-Kobayashi M et al. Protein kinase PKR mutants resistant to the poxvirus pseudosubstrate K3L protein. Proc Natl Acad Sci USA 2008 105 : 16894 16899.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 16894-16899
    • Seo, E.J.1    Liu, F.2    Kawagishi-Kobayashi, M.3
  • 66
    • 0037279654 scopus 로고    scopus 로고
    • The active caspase-8 heterotetramer is formed at the CD95 DISC
    • Lavrik I, Krueger A, Schmitz I et al. The active caspase-8 heterotetramer is formed at the CD95 DISC. Cell Death Differ 2003 10 : 144 145.
    • (2003) Cell Death Differ , vol.10 , pp. 144-145
    • Lavrik, I.1    Krueger, A.2    Schmitz, I.3
  • 67
    • 53549119055 scopus 로고    scopus 로고
    • Vorinostat and sorafenib increase ER stress, autophagy and apoptosis via ceramide-dependent CD95 and PERK activation
    • Park MA, Zhang G, Martin AP et al. Vorinostat and sorafenib increase ER stress, autophagy and apoptosis via ceramide-dependent CD95 and PERK activation. Cancer Biol Ther 2008 7 : 1648 1662.
    • (2008) Cancer Biol Ther , vol.7 , pp. 1648-1662
    • Park, M.A.1    Zhang, G.2    Martin, A.P.3
  • 68
    • 53049109359 scopus 로고    scopus 로고
    • Vorinostat and sorafenib synergistically kill tumor cells via FLIP suppression and CD95 activation
    • Zhang G, Park MA, Mitchell C et al. Vorinostat and sorafenib synergistically kill tumor cells via FLIP suppression and CD95 activation. Clin Cancer Res 2008 14 : 5385 5399.
    • (2008) Clin Cancer Res , vol.14 , pp. 5385-5399
    • Zhang, G.1    Park, M.A.2    Mitchell, C.3
  • 69
    • 30044435192 scopus 로고    scopus 로고
    • Unique and overlapping substrate specificities of caspase-8 and caspase-10
    • DOI 10.1038/sj.onc.1209015
    • Fischer U, Stroh C, Schulze-Osthoff K. Unique and overlapping substrate specificities of caspase-8 and caspase-10. Oncogene 2006 25 : 152 159. (Pubitemid 43050014)
    • (2006) Oncogene , vol.25 , Issue.1 , pp. 152-159
    • Fischer, U.1    Stroh, C.2    Schulze-Osthoff, K.3
  • 71
    • 15144345497 scopus 로고    scopus 로고
    • Pro-caspase-3 is a major physiologic target of caspase-8
    • Stennicke HR, Jurgensmeier JM, Shin H et al. Pro-caspase-3 is a major physiologic target of caspase-8. J Biol Chem 1998 273 : 27084 27090.
    • (1998) J Biol Chem , vol.273 , pp. 27084-27090
    • Stennicke, H.R.1    Jurgensmeier, J.M.2    Shin, H.3
  • 72
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • Li H, Zhu H, Xu CJ, Yuan J. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell 1998 94 : 491 501. (Pubitemid 28391865)
    • (1998) Cell , vol.94 , Issue.4 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.-J.3    Yuan, J.4
  • 73
    • 0032488661 scopus 로고    scopus 로고
    • Bcl-XL cooperatively associates with the Bap31 complex in the endoplasmic reticulum, dependent on procaspase-8 and Ced-4 adaptor
    • Ng FW, Shore GC. Bcl-XL cooperatively associates with the Bap31 complex in the endoplasmic reticulum, dependent on procaspase-8 and Ced-4 adaptor. J Biol Chem 1998 273 : 3140 3143.
    • (1998) J Biol Chem , vol.273 , pp. 3140-3143
    • Ng, F.W.1    Shore, G.C.2
  • 74
    • 0030705234 scopus 로고    scopus 로고
    • P28 Bap31, a Bcl-2/Bcl-XL- and procaspase-8-associated protein in the endoplasmic reticulum
    • Ng FW, Nguyen M, Kwan T et al. p28 Bap31, a Bcl-2/Bcl-XL- and procaspase-8-associated protein in the endoplasmic reticulum. J Cell Biol 1997 139 : 327 338.
    • (1997) J Cell Biol , vol.139 , pp. 327-338
    • Ng, F.W.1    Nguyen, M.2    Kwan, T.3
  • 75
    • 0013148718 scopus 로고    scopus 로고
    • Uncleaved BAP31 in association with A4 protein at the endoplasmic reticulum is an inhibitor of Fas-initiated release of cytochrome c from mitochondria
    • DOI 10.1074/jbc.M209684200
    • Wang B, Nguyen M, Breckenridge DG et al. Uncleaved BAP31 in association with A4 protein at the endoplasmic reticulum is an inhibitor of Fas-initiated release of cytochrome c from mitochondria. J Biol Chem 2003 278 : 14461 14468. (Pubitemid 36799999)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.16 , pp. 14461-14468
    • Wang, B.1    Nguyen, M.2    Breckenridge, D.G.3    Stojanovic, M.4    Clemons, P.A.5    Kuppig, S.6    Shore, G.C.7
  • 76
    • 0033816610 scopus 로고    scopus 로고
    • Caspase-resistant BAP31 inhibits Fas-mediated apoptotic membrane fragmentation and release of cytochrome c from mitochondria
    • Nguyen M, Breckenridge DG, Ducret A, Shore GC. Caspase-resistant BAP31 inhibits Fas-mediated apoptotic membrane fragmentation and release of cytochrome c from mitochondria. Mol Cell Biol 2000 20 : 6731 6740.
    • (2000) Mol Cell Biol , vol.20 , pp. 6731-6740
    • Nguyen, M.1    Breckenridge, D.G.2    Ducret, A.3    Shore, G.C.4
  • 77
    • 0037417334 scopus 로고    scopus 로고
    • Caspase cleavage product of BAP31 induces mitochondrial fission through endoplasmic reticulum calcium signals, enhancing cytochrome c release to the cytosol
    • Breckenridge DG, Stojanovic M, Marcellus RC, Shore GC. Caspase cleavage product of BAP31 induces mitochondrial fission through endoplasmic reticulum calcium signals, enhancing cytochrome c release to the cytosol. J Cell Biol 2003 160 : 1115 1127.
    • (2003) J Cell Biol , vol.160 , pp. 1115-1127
    • Breckenridge, D.G.1    Stojanovic, M.2    Marcellus, R.C.3    Shore, G.C.4
  • 78
    • 38049110319 scopus 로고    scopus 로고
    • 2+ levels favors plasma membrane surface exposure of calreticulin
    • 2+ levels favors plasma membrane surface exposure of calreticulin. Cell Death Differ 2008 15 : 274 282.
    • (2008) Cell Death Differ , vol.15 , pp. 274-282
    • Tufi, R.1    Panaretakis, T.2    Bianchi, K.3
  • 79
    • 37549048249 scopus 로고    scopus 로고
    • The BCL-2 protein family: Opposing activities that mediate cell death
    • Youle RJ, Strasser A. The BCL-2 protein family: opposing activities that mediate cell death. Nat Rev Mol Cell Biol 2008 9 : 47 59.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 47-59
    • Youle, R.J.1    Strasser, A.2
  • 83
    • 0031018914 scopus 로고    scopus 로고
    • FLICE induced apoptosis in a cell-free system. Cleavage of caspase zymogens
    • DOI 10.1074/jbc.272.5.2952
    • Muzio M, Salvesen GS, Dixit VM. FLICE induced apoptosis in a cell-free system. Cleavage of caspase zymogens. J Biol Chem 1997 272 : 2952 2956. (Pubitemid 27053346)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.5 , pp. 2952-2956
    • Muzio, M.1    Salvesen, G.S.2    Dixit, V.M.3
  • 84
    • 33750984207 scopus 로고    scopus 로고
    • Mutation of the myxoma virus SERP2 P1-site to prevent proteinase inhibition causes apoptosis in cultured RK-13 cells and attenuates disease in rabbits, but mutation to alter specificity causes apoptosis without reducing virulence
    • MacNeill AL, Turner PC, Moyer RW. Mutation of the myxoma virus SERP2 P1-site to prevent proteinase inhibition causes apoptosis in cultured RK-13 cells and attenuates disease in rabbits, but mutation to alter specificity causes apoptosis without reducing virulence. Virology 2006 356 : 12 22.
    • (2006) Virology , vol.356 , pp. 12-22
    • MacNeill, A.L.1    Turner, P.C.2    Moyer, R.W.3
  • 85
    • 0038475942 scopus 로고    scopus 로고
    • Mutational analyses of the p35-caspase interaction: A bowstring kinetic model of caspase inhibition by p35
    • DOI 10.1074/jbc.M211607200
    • Xu G, Rich RL, Steegborn C et al. Mutational analyses of the p35-caspase interaction. A bowstring kinetic model of caspase inhibition by p35. J Biol Chem 2003 278 : 5455 5461. (Pubitemid 36801062)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.7 , pp. 5455-5461
    • Xu, G.1    Rich, R.L.2    Steegborn, C.3    Min, T.4    Huang, Y.5    Myszka, D.G.6    Wu, H.7
  • 86
    • 0035932465 scopus 로고    scopus 로고
    • Covalent inhibition revealed by the crystal structure of the caspase-8/p35 complex
    • DOI 10.1038/35068604
    • Xu G, Cirilli M, Huang Y, Rich RL, Myszka DG, Wu H. Covalent inhibition revealed by the crystal structure of the caspase-8/p35 complex. Nature 2001 410 : 494 497. (Pubitemid 32240052)
    • (2001) Nature , vol.410 , Issue.6827 , pp. 494-497
    • Xu, G.1    Cirilli, M.2    Huang, Y.3    Rich, R.L.4    Myszka, D.G.5    Wu, H.6
  • 87
    • 85047278700 scopus 로고    scopus 로고
    • Baculovirus apoptotic suppressor P49 is a substrate inhibitor of initiator caspases resistant to P35 in vivo
    • Zoog SJ, Schiller JJ, Wetter JA, Chejanovsky N, Friesen PD. Baculovirus apoptotic suppressor P49 is a substrate inhibitor of initiator caspases resistant to P35 in vivo. EMBO J 2002 21 : 5130 5140.
    • (2002) EMBO J , vol.21 , pp. 5130-5140
    • Zoog, S.J.1    Schiller, J.J.2    Wetter, J.A.3    Chejanovsky, N.4    Friesen, P.D.5
  • 88
    • 0032575309 scopus 로고    scopus 로고
    • Interaction of the baculovirus anti-apoptotic protein p35 with caspases. Specificity, kinetics, and characterization of the caspase/p35 complex
    • DOI 10.1021/bi980893w
    • Zhou Q, Krebs JF, Snipas SJ et al. Interaction of the baculovirus anti-apoptotic protein p35 with caspases. Specificity, kinetics, and characterization of the caspase/p35 complex. Biochemistry 1998 37 : 10757 10765. (Pubitemid 28357877)
    • (1998) Biochemistry , vol.37 , Issue.30 , pp. 10757-10765
    • Zhou, Q.1    Krebs, J.F.2    Snipas, S.J.3    Price, A.4    Alnemri, E.S.5    Tomaselli, K.J.6    Salvesen, G.S.7
  • 89
    • 12244288291 scopus 로고    scopus 로고
    • The p35 relative, p49, inhibits mammalian and Drosophila caspases including DRONC and protects against apoptosis
    • Jabbour AM, Ekert PG, Coulson EJ, Knight MJ, Ashley DM, Hawkins CJ. The p35 relative, p49, inhibits mammalian and Drosophila caspases including DRONC and protects against apoptosis. Cell Death Differ 2002 9 : 1311 1320.
    • (2002) Cell Death Differ , vol.9 , pp. 1311-1320
    • Jabbour, A.M.1    Ekert, P.G.2    Coulson, E.J.3    Knight, M.J.4    Ashley, D.M.5    Hawkins, C.J.6
  • 90
    • 34247165442 scopus 로고    scopus 로고
    • The large and small isoforms of human papillomavirus type 16 E6 bind to and differentially affect procaspase 8 stability and activity
    • Filippova M, Johnson MM, Bautista M et al. The large and small isoforms of human papillomavirus type 16 E6 bind to and differentially affect procaspase 8 stability and activity. J Virol 2007 81 : 4116 4129.
    • (2007) J Virol , vol.81 , pp. 4116-4129
    • Filippova, M.1    Johnson, M.M.2    Bautista, M.3
  • 92
    • 0037077205 scopus 로고    scopus 로고
    • The human papillomavirus 16 E6 protein binds to tumor necrosis factor (TNF) R1 and protects cells from TNF-induced apoptosis
    • Filippova M, Song H, Connolly JL, Dermody TS, Duerksen-Hughes PJ. The human papillomavirus 16 E6 protein binds to tumor necrosis factor (TNF) R1 and protects cells from TNF-induced apoptosis. J Biol Chem 2002 277 : 21730 21739.
    • (2002) J Biol Chem , vol.277 , pp. 21730-21739
    • Filippova, M.1    Song, H.2    Connolly, J.L.3    Dermody, T.S.4    Duerksen-Hughes, P.J.5
  • 94
    • 0030950228 scopus 로고    scopus 로고
    • A novel family of viral death effector domain-containing molecules that inhibit both CD-95- and tumor necrosis factor receptor-1-induced apoptosis
    • Hu S, Vincenz C, Buller M, Dixit VM. A novel family of viral death effector domain-containing molecules that inhibit both CD-95- and tumor necrosis factor receptor-1-induced apoptosis. J Biol Chem 1997 272 : 9621 9624.
    • (1997) J Biol Chem , vol.272 , pp. 9621-9624
    • Hu, S.1    Vincenz, C.2    Buller, M.3    Dixit, V.M.4
  • 96
    • 27144463628 scopus 로고    scopus 로고
    • Viral FLIP enhances Wnt signaling downstream of stabilized beta-catenin, leading to control of cell growth
    • Nakagiri S, Murakami A, Takada S, Akiyama T, Yonehara S. Viral FLIP enhances Wnt signaling downstream of stabilized beta-catenin, leading to control of cell growth. Mol Cell Biol 2005 25 : 9249 9258.
    • (2005) Mol Cell Biol , vol.25 , pp. 9249-9258
    • Nakagiri, S.1    Murakami, A.2    Takada, S.3    Akiyama, T.4    Yonehara, S.5
  • 98
    • 0345329602 scopus 로고    scopus 로고
    • Expression of K13/v-FLIP gene of human herpesvirus 8 and apoptosis in Kaposi's sarcoma spindle cells
    • Sturzl M, Hohenadl C, Zietz C et al. Expression of K13/v-FLIP gene of human herpesvirus 8 and apoptosis in Kaposi's sarcoma spindle cells. J Natl Cancer Inst 1999 91 : 1725 1733.
    • (1999) J Natl Cancer Inst , vol.91 , pp. 1725-1733
    • Sturzl, M.1    Hohenadl, C.2    Zietz, C.3
  • 100
    • 0035970321 scopus 로고    scopus 로고
    • Molluscum contagiosum virus inhibitors of apoptosis: The MC159 v-FLIP protein blocks Fas-induced activation of procaspases and degradation of the related MC160 protein
    • Shisler JL, Moss B. Molluscum contagiosum virus inhibitors of apoptosis: the MC159 v-FLIP protein blocks Fas-induced activation of procaspases and degradation of the related MC160 protein. Virology 2001 282 : 14 25.
    • (2001) Virology , vol.282 , pp. 14-25
    • Shisler, J.L.1    Moss, B.2
  • 101
    • 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
    • Saito K, Meyer K, Warner R, Basu A, Ray RB, Ray R. Hepatitis C virus core protein inhibits tumor necrosis factor alpha-mediated apoptosis by a protective effect involving cellular FLICE inhibitory protein. J Virol 2006 80 : 4372 4379.
    • (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
  • 103
    • 33646591256 scopus 로고    scopus 로고
    • HTLV-1 Tax protects against CD95-mediated apoptosis by induction of the cellular FLICE-inhibitory protein (c-FLIP)
    • Krueger A, Fas SC, Giaisi M et al. HTLV-1 Tax protects against CD95-mediated apoptosis by induction of the cellular FLICE-inhibitory protein (c-FLIP). Blood 2006 107 : 3933 3939.
    • (2006) Blood , vol.107 , pp. 3933-3939
    • Krueger, A.1    Fas, S.C.2    Giaisi, M.3
  • 104
    • 18244394529 scopus 로고    scopus 로고
    • HIV-1 Tat protein concomitantly down-regulates apical caspase-10 and up-regulates c-FLIP in lymphoid T cells: A potential molecular mechanism to escape TRAIL cytotoxicity
    • DOI 10.1002/jcp.20252
    • Gibellini D, Re MC, Ponti C et al. HIV-1 Tat protein concomitantly down-regulates apical caspase-10 and up-regulates c-FLIP in lymphoid T cells: a potential molecular mechanism to escape TRAIL cytotoxicity. J Cell Physiol 2005 203 : 547 556. (Pubitemid 40629017)
    • (2005) Journal of Cellular Physiology , vol.203 , Issue.3 , pp. 547-556
    • Gibellini, D.1    Re, M.C.2    Ponti, C.3    Vitone, F.4    Bon, I.5    Fabbri, G.6    Di Iasio, M.G.7    Zauli, G.8
  • 105
    • 53749089317 scopus 로고    scopus 로고
    • Bap31 is a novel target of the human papillomavirus E5 protein
    • Regan JA, Laimins LA. Bap31 is a novel target of the human papillomavirus E5 protein. J Virol 2008 82 : 10042 10051.
    • (2008) J Virol , vol.82 , pp. 10042-10051
    • Regan, J.A.1    Laimins, L.A.2
  • 106
    • 0029868112 scopus 로고    scopus 로고
    • The E1B 19K protein blocks apoptosis by interacting with and inhibiting the p53-inducible and death-promoting Bax protein
    • Han J, Sabbatini P, Perez D, Rao L, Modha D, White E. The E1B 19K protein blocks apoptosis by interacting with and inhibiting the p53-inducible and death-promoting Bax protein. Genes Dev 1996 10 : 461 477.
    • (1996) Genes Dev , vol.10 , pp. 461-477
    • Han, J.1    Sabbatini, P.2    Perez, D.3    Rao, L.4    Modha, D.5    White, E.6
  • 107
    • 27144523216 scopus 로고    scopus 로고
    • Mitochondrial localization of p53 during adenovirus infection and regulation of its activity by E1B-19K
    • DOI 10.1038/sj.onc.1208836, PII 1208836
    • Lomonosova E, Subramanian T, Chinnadurai G. Mitochondrial localization of p53 during adenovirus infection and regulation of its activity by E1B-19K. Oncogene 2005 24 : 6796 6808. (Pubitemid 41487038)
    • (2005) Oncogene , vol.24 , Issue.45 , pp. 6796-6808
    • Lomonosova, E.1    Subramanian, T.2    Chinnadurai, G.3
  • 109
    • 33745961009 scopus 로고    scopus 로고
    • Interaction of F1L with the BH3 domain of Bak is responsible for inhibiting vaccinia-induced apoptosis
    • DOI 10.1038/sj.cdd.4401853, PII 4401853
    • Postigo A, Cross JR, Downward J, Way M. Interaction of F1L with the BH3 domain of Bak is responsible for inhibiting vaccinia-induced apoptosis. Cell Death Differ 2006 13 : 1651 1662. (Pubitemid 44390853)
    • (2006) Cell Death and Differentiation , vol.13 , Issue.10 , pp. 1651-1662
    • Postigo, A.1    Cross, J.R.2    Downward, J.3    Way, M.4
  • 110
    • 27644535708 scopus 로고    scopus 로고
    • The vaccinia virus F1L protein interacts with the proapoptotic protein Bak and inhibits Bak activation
    • DOI 10.1128/JVI.79.22.14031-14043.2005
    • Wasilenko ST, Banadyga L, Bond D, Barry M. The vaccinia virus F1L protein interacts with the proapoptotic protein Bak and inhibits Bak activation. J Virol 2005 79 : 14031 14043. (Pubitemid 41552701)
    • (2005) Journal of Virology , vol.79 , Issue.22 , pp. 14031-14043
    • Wasilenko, S.T.1    Banadyga, L.2    Bond, D.3    Barry, M.4
  • 111
    • 33845972661 scopus 로고    scopus 로고
    • The vaccinia virus protein F1L interacts with Bim and inhibits activation of the pro-apoptotic protein Bax
    • DOI 10.1074/jbc.M607465200
    • Taylor JM, Quilty D, Banadyga L, Barry M. The vaccinia virus protein F1L interacts with Bim and inhibits activation of the pro-apoptotic protein Bax. J Biol Chem 2006 281 : 39728 39739. (Pubitemid 46041932)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.51 , pp. 39728-39739
    • Taylor, J.M.1    Quilty, D.2    Banadyga, L.3    Barry, M.4
  • 112
    • 35148886675 scopus 로고    scopus 로고
    • Fowlpox virus encodes a Bcl-2 homologue that protects cells from apoptotic death through interaction with the proapoptotic protein bak
    • DOI 10.1128/JVI.00734-07
    • Banadyga L, Gerig J, Stewart T, Barry M. Fowlpox virus encodes a Bcl-2 homologue that protects cells from apoptotic death through interaction with the proapoptotic protein Bak. J Virol 2007 81 : 11032 11045. (Pubitemid 47536076)
    • (2007) Journal of Virology , vol.81 , Issue.20 , pp. 11032-11045
    • Banadyga, L.1    Gerig, J.2    Stewart, T.3    Barry, M.4
  • 113
    • 67650453767 scopus 로고    scopus 로고
    • The fowlpox virus BCL-2 homologue, FPV039, interacts with activated Bax and a discrete subset of BH3-only proteins to inhibit apoptosis
    • Banadyga L, Veugelers K, Campbell S, Barry M. The fowlpox virus BCL-2 homologue, FPV039, interacts with activated Bax and a discrete subset of BH3-only proteins to inhibit apoptosis. J Virol 2009 83 : 7085 7098.
    • (2009) J Virol , vol.83 , pp. 7085-7098
    • Banadyga, L.1    Veugelers, K.2    Campbell, S.3    Barry, M.4
  • 114
    • 0037013894 scopus 로고    scopus 로고
    • Characterization of an anti-apoptotic glycoprotein encoded by Kaposi's sarcoma-associated herpesvirus which resembles a spliced variant of human survivin
    • DOI 10.1093/emboj/21.11.2602
    • Wang HW, Sharp TV, Koumi A, Koentges G, Boshoff C. Characterization of an anti-apoptotic glycoprotein encoded by Kaposi's sarcoma-associated herpesvirus which resembles a spliced variant of human survivin. EMBO J 2002 21 : 2602 2615. (Pubitemid 34619376)
    • (2002) EMBO Journal , vol.21 , Issue.11 , pp. 2602-2615
    • Wang, H.-W.1    Sharp, T.V.2    Koumi, A.3    Koentges, G.4    Boshoff, C.5
  • 115
    • 33645531325 scopus 로고    scopus 로고
    • Inhibition of lymphotoxin-beta receptor-mediated cell death by survivin-DeltaEx3
    • You RI, Chen MC, Wang HW, Chou YC, Lin CH, Hsieh SL. Inhibition of lymphotoxin-beta receptor-mediated cell death by survivin-DeltaEx3. Cancer Res 2006 66 : 3051 3061.
    • (2006) Cancer Res , vol.66 , pp. 3051-3061
    • You, R.I.1    Chen, M.C.2    Wang, H.W.3    Chou, Y.C.4    Lin, C.H.5    Hsieh, S.L.6
  • 117
    • 0032861298 scopus 로고    scopus 로고
    • The murine gammaherpesvirus-68 M11 protein inhibits Fas- and TNF-induced apoptosis
    • Wang GH, Garvey TL, Cohen JI. The murine gammaherpesvirus-68 M11 protein inhibits Fas- and TNF-induced apoptosis. J Gen Virol 1999 10 : 2737 2740.
    • (1999) J Gen Virol , vol.10 , pp. 2737-2740
    • Wang, G.H.1    Garvey, T.L.2    Cohen, J.I.3
  • 118
    • 0037213306 scopus 로고    scopus 로고
    • Disruption of mitochondrial networks by the human cytomegalovirus UL37 gene product viral mitochondrion-localized inhibitor of apoptosis
    • DOI 10.1128/JVI.77.1.631-641.2003
    • McCormick AL, Smith VL, Chow D, Mocarski ES. Disruption of mitochondrial networks by the human cytomegalovirus UL37 gene product viral mitochondrion-localized inhibitor of apoptosis. J Virol 2003 77 : 631 641. (Pubitemid 36005000)
    • (2003) Journal of Virology , vol.77 , Issue.1 , pp. 631-641
    • McCormick, A.L.1    Smith, V.L.2    Chow, D.3    Mocarski, E.S.4
  • 121
    • 0029948542 scopus 로고    scopus 로고
    • An African swine fever virus Bc1-2 homolog, 5-HL, suppresses apoptotic cell death
    • Afonso CL, Neilan JG, Kutish GF, Rock DL. An African swine fever virus Bc1-2 homolog, 5-HL, suppresses apoptotic cell death. J Virol 1996 70 : 4858 4863.
    • (1996) J Virol , vol.70 , pp. 4858-4863
    • Afonso, C.L.1    Neilan, J.G.2    Kutish, G.F.3    Rock, D.L.4
  • 122
    • 0027264124 scopus 로고
    • An African swine fever virus gene with similarity to the proto-oncogene bcl-2 and the Esptein-Barr virus gene BHRF1
    • Neilan JG, Lu Z, Afonso CL, Kutish GF, Sussman MD, Rock DL. An African swine fever virus gene with similarity to the proto-oncogene bcl-2 and the Epstein-Barr virus gene BHRF1. J Virol 1993 67 : 4391 4394. (Pubitemid 23180769)
    • (1993) Journal of Virology , vol.67 , Issue.7 , pp. 4391-4394
    • Neilan, J.G.1    Lu, Z.2    Afonso, C.L.3    Kutish, G.F.4    Sussman, M.D.5    Rock, D.L.6
  • 125
    • 33947727119 scopus 로고    scopus 로고
    • Structure of M11L: A myxoma virus structural homolog of the apoptosis inhibitor, Bcl-2
    • Douglas AE, Corbett KD, Berger JM, McFadden G, Handel TM. Structure of M11L: a myxoma virus structural homolog of the apoptosis inhibitor, Bcl-2. Protein Sci 2007 16 : 695 703.
    • (2007) Protein Sci , vol.16 , pp. 695-703
    • Douglas, A.E.1    Corbett, K.D.2    Berger, J.M.3    McFadden, G.4    Handel, T.M.5
  • 127
    • 31144454896 scopus 로고    scopus 로고
    • Myxoma virus M11L blocks apoptosis through inhibition of conformational activation of Bax at the mitochondria
    • DOI 10.1128/JVI.80.3.1140-1151.2006
    • Su J, Wang G, Barrett JW, Irvine TS, Gao X, McFadden G. Myxoma virus M11L blocks apoptosis through inhibition of conformational activation of Bax at the mitochondria. J Virol 2006 80 : 1140 1151. (Pubitemid 43134071)
    • (2006) Journal of Virology , vol.80 , Issue.3 , pp. 1140-1151
    • Su, J.1    Wang, G.2    Barrett, J.W.3    Irvine, T.S.4    Gao, X.5    McFadden, G.6
  • 132
    • 29144463656 scopus 로고    scopus 로고
    • Epstein-barr virus provides a new paradigm: A requirement for the immediate inhibition of apoptosis
    • DOI 10.1371/journal.pbio.0030404, e404
    • Altmann M, Hammerschmidt W. Epstein-Barr virus provides a new paradigm: a requirement for the immediate inhibition of apoptosis. PLoS Biol 2005 3 : e404. (Pubitemid 41796330)
    • (2005) PLoS Biology , vol.3 , Issue.12 , pp. 1-10
    • Altmann, M.1    Hammerschmidt, W.2
  • 133
    • 15244354017 scopus 로고    scopus 로고
    • Herpesvirus pan encodes a functional homologue of BHRF1, the Epstein-Barr virus v-Bcl-2
    • Howell M, Williams T, Hazlewood SA. Herpesvirus pan encodes a functional homologue of BHRF1, the Epstein-Barr virus v-Bcl-2. BMC Microbiol 2005 5 : 6.
    • (2005) BMC Microbiol , vol.5 , pp. 6
    • Howell, M.1    Williams, T.2    Hazlewood, S.A.3
  • 134
    • 0033916528 scopus 로고    scopus 로고
    • Herpesvirus papio encodes a functional homologue of the Epstein-Barr virus apoptosis suppressor, BHRF1
    • Meseda CA, Arrand JR, Mackett M. Herpesvirus papio encodes a functional homologue of the Epstein-Barr virus apoptosis suppressor, BHRF1. J Gen Virol 2000 81 : 1801 1805.
    • (2000) J Gen Virol , vol.81 , pp. 1801-1805
    • Meseda, C.A.1    Arrand, J.R.2    MacKett, M.3
  • 135
    • 0031746909 scopus 로고    scopus 로고
    • Antiapoptotic activity of the herpesvirus saimiri-encoded Bcl-2 homolog: Stabilization of mitochondria and inhibition of caspase-3-like activity
    • Derfuss T, Fickenscher H, Kraft MS et al. Antiapoptotic activity of the herpesvirus saimiri-encoded Bcl-2 homolog: stabilization of mitochondria and inhibition of caspase-3-like activity. J Virol 1998 72 : 5897 5904.
    • (1998) J Virol , vol.72 , pp. 5897-5904
    • Derfuss, T.1    Fickenscher, H.2    Kraft, M.S.3
  • 138
    • 0033616139 scopus 로고    scopus 로고
    • Role of actin in regulated exocytosis and compensatory membrane retrieval: Insights from an old acquaintance
    • DOI 10.1006/bbrc.1999.1883
    • Valentijn K, Valentijn JA, Jamieson JD. Role of actin in regulated exocytosis and compensatory membrane retrieval: insights from an old acquaintance. Biochem Biophys Res Commun 1999 266 : 652 661. (Pubitemid 30042490)
    • (1999) Biochemical and Biophysical Research Communications , vol.266 , Issue.3 , pp. 652-661
    • Valentijn, K.1    Valentijn, J.A.2    Jamieson, J.D.3
  • 139
    • 48749083469 scopus 로고    scopus 로고
    • Inhibition of SNAP25 expression by HIV-1 Tat involves the activity of mir-128a
    • Eletto D, Russo G, Passiatore G et al. Inhibition of SNAP25 expression by HIV-1 Tat involves the activity of mir-128a. J Cell Physiol 2008 216 : 764 770.
    • (2008) J Cell Physiol , vol.216 , pp. 764-770
    • Eletto, D.1    Russo, G.2    Passiatore, G.3
  • 140
    • 9644268172 scopus 로고    scopus 로고
    • Budding events in herpesvirus morphogenesis
    • Mettenleiter TC. Budding events in herpesvirus morphogenesis. Virus Res 2004 106 : 167 180.
    • (2004) Virus Res , vol.106 , pp. 167-180
    • Mettenleiter, T.C.1
  • 141
    • 23344448723 scopus 로고    scopus 로고
    • The use of calnexin and calreticulin by cellular and viral glycoproteins
    • DOI 10.1074/jbc.M501020200
    • Pieren M, Galli C, Denzel A, Molinari M. The use of calnexin and calreticulin by cellular and viral glycoproteins. J Biol Chem 2005 280 : 28265 28271. (Pubitemid 41105722)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.31 , pp. 28265-28271
    • Pieren, M.1    Galli, C.2    Denzel, A.3    Molinari, M.4
  • 142
    • 0028360278 scopus 로고
    • Viral induction of the human autoantigen calreticulin
    • Zhu J, Newkirk MM. Viral induction of the human autoantigen calreticulin. Clin Invest Med 1994 17 : 196 205. (Pubitemid 24204865)
    • (1994) Clinical and Investigative Medicine , vol.17 , Issue.3 , pp. 196-205
    • Zhu, J.1    Newkirk, M.M.2
  • 143
    • 0035213883 scopus 로고    scopus 로고
    • The measles virus (MV) glycoproteins interact with cellular chaperones in the endoplasmic reticulum and MV infection upregulates chaperone expression
    • DOI 10.1007/s007050170020
    • Bolt G. The measles virus (MV) glycoproteins interact with cellular chaperones in the endoplasmic reticulum and MV infection upregulates chaperone expression. Arch Virol 2001 146 : 2055 2068. (Pubitemid 33145582)
    • (2001) Archives of Virology , vol.146 , Issue.11 , pp. 2055-2068
    • Bolt, G.1
  • 144
    • 0034231849 scopus 로고    scopus 로고
    • Folding of viral envelope glycoproteins in the endoplasmic reticulum
    • Braakman I, van Anken E. Folding of viral envelope glycoproteins in the endoplasmic reticulum. Traffic 2000 1 : 533 539.
    • (2000) Traffic , vol.1 , pp. 533-539
    • Braakman, I.1    Van Anken, E.2
  • 145
    • 33744526790 scopus 로고    scopus 로고
    • Cleavage of endoplasmic reticulum Proteins in hepatocellular carcinoma: Detection of generated fragments in patient sera
    • DOI 10.1053/j.gastro.2006.02.058, PII S0016508506007372
    • Chignard N, Shang S, Wang H et al. Cleavage of endoplasmic reticulum proteins in hepatocellular carcinoma: detection of generated fragments in patient sera. Gastroenterology 2006 130 : 2010 2022. (Pubitemid 43816962)
    • (2006) Gastroenterology , vol.130 , Issue.7 , pp. 2010-2022
    • Chignard, N.1    Shang, S.2    Wang, H.3    Marrero, J.4    Brechot, C.5    Hanash, S.6    Beretta, L.7
  • 146
    • 67650751080 scopus 로고    scopus 로고
    • Guidelines for the use and interpretation of assays for monitoring cell death in higher eukaryotes
    • Galluzzi L, Aaronson SA, Abrams J et al. Guidelines for the use and interpretation of assays for monitoring cell death in higher eukaryotes. Cell Death Differ 2009 16 : 1093 1107.
    • (2009) Cell Death Differ , vol.16 , pp. 1093-1107
    • Galluzzi, L.1    Aaronson, S.A.2    Abrams, J.3
  • 149
    • 65249149086 scopus 로고    scopus 로고
    • The Epstein-Barr virus Bcl-2 homolog, BHRF1, blocks apoptosis by binding to a limited amount of Bim
    • Desbien AL, Kappler JW, Marrack P. The Epstein-Barr virus Bcl-2 homolog, BHRF1, blocks apoptosis by binding to a limited amount of Bim. Proc Natl Acad Sci USA 2009 106 : 5663 5668.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 5663-5668
    • Desbien, A.L.1    Kappler, J.W.2    Marrack, P.3
  • 151
    • 58149529737 scopus 로고    scopus 로고
    • Interaction of dengue virus envelope protein with endoplasmic reticulum-resident chaperones facilitates dengue virus production
    • Limjindaporn T, Wongwiwat W, Noisakran S et al. Interaction of dengue virus envelope protein with endoplasmic reticulum-resident chaperones facilitates dengue virus production. Biochem Biophys Res Commun 2009 379 : 196 200.
    • (2009) Biochem Biophys Res Commun , vol.379 , pp. 196-200
    • Limjindaporn, T.1    Wongwiwat, W.2    Noisakran, S.3
  • 152
    • 0031957011 scopus 로고    scopus 로고
    • Involvement of endoplasmic reticulum chaperones in the folding of hepatitis C virus glycoproteins
    • Choukhi A, Ung S, Wychowski C, Dubuisson J. Involvement of endoplasmic reticulum chaperones in the folding of hepatitis C virus glycoproteins. J Virol 1998 72 : 3851 3858. (Pubitemid 28188685)
    • (1998) Journal of Virology , vol.72 , Issue.5 , pp. 3851-3858
    • Choukhi, A.1    Ung, S.2    Wychowski, C.3    Dubuisson, J.4
  • 155
    • 0033059215 scopus 로고    scopus 로고
    • Transient association of calnexin and calreticulin with newly synthesized
    • Veijola J, Pettersson RF. Transient association of calnexin and calreticulin with newly synthesized G1 and G2 glycoproteins of uukuniemi virus (family Bunyaviridae). J Virol 1999 73 : 6123 6127. (Pubitemid 29274905)
    • (1999) Journal of Virology , vol.73 , Issue.7 , pp. 6123-6127
    • Veijola, J.1    Pettersson, R.F.2
  • 156
    • 0031924469 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 glycoprotein B requires a cysteine residue at position 633 for folding, processing, and incorporation into mature infectious virus particles
    • Laquerre S, Anderson DB, Argnani R, Glorioso JC. Herpes simplex virus type 1 glycoprotein B requires a cysteine residue at position 633 for folding, processing, and incorporation into mature infectious virus particles. J Virol 1998 72 : 4940 4949. (Pubitemid 28215673)
    • (1998) Journal of Virology , vol.72 , Issue.6 , pp. 4940-4949
    • Laquerre, S.1    Anderson, D.B.2    Argnani, R.3    Glorioso, J.C.4
  • 157
    • 0028606112 scopus 로고
    • Identification of calreticulin as a rubella virus RNA binding protein
    • Singh NK, Atreya CD, Nakhasi HL. Identification of calreticulin as a rubella virus RNA binding protein. Proc Natl Acad Sci USA 1994 91 : 12770 12774.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12770-12774
    • Singh, N.K.1    Atreya, C.D.2    Nakhasi, H.L.3
  • 158
    • 0029066118 scopus 로고
    • The rubella virus RNA binding activity of human calreticulin is localized to the N-terminal domain
    • Atreya CD, Singh NK, Nakhasi HL. The rubella virus RNA binding activity of human calreticulin is localized to the N-terminal domain. J Virol 1995 69 : 3848 3851.
    • (1995) J Virol , vol.69 , pp. 3848-3851
    • Atreya, C.D.1    Singh, N.K.2    Nakhasi, H.L.3
  • 159
    • 0037372070 scopus 로고    scopus 로고
    • Cellular proteins from human monocytes bind to dengue 4 virus minus-strand 3′ untranslated region RNA
    • DOI 10.1128/JVI.77.5.3067-3076.2003
    • Yocupicio-Monroy RM, Medina F, Reyes-del Valle J, del Angel RM. Cellular proteins from human monocytes bind to dengue 4 virus minus-strand 3′ untranslated region RNA. J Virol 2003 77 : 3067 3076. (Pubitemid 36228092)
    • (2003) Journal of Virology , vol.77 , Issue.5 , pp. 3067-3076
    • Yocupicio-Monroy, R.M.E.1    Medina, F.2    Reyes-del Valle, J.3    Del Angel, R.M.4
  • 160
    • 0030053103 scopus 로고    scopus 로고
    • Calreticulin interacts with newly synthesized human immunodeficiency virus type 1 envelope glycoprotein, suggesting a chaperone function similar to that of calnexin
    • DOI 10.1074/jbc.271.1.97
    • Otteken A, Moss B. Calreticulin interacts with newly synthesized human immunodeficiency virus type 1 envelope glycoprotein, suggesting a chaperone function similar to that of calnexin. J Biol Chem 1996 271 : 97 103. (Pubitemid 26026563)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.1 , pp. 97-103
    • Otteken, A.1    Moss, B.2
  • 161
    • 0034845609 scopus 로고    scopus 로고
    • Folding of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum
    • DOI 10.1016/S0300-9084(01)01314-1
    • Land A, Braakman I. Folding of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum. Biochimie 2001 83 : 783 790. (Pubitemid 32821244)
    • (2001) Biochimie , vol.83 , Issue.8 , pp. 783-790
    • Land, A.1    Braakman, I.2
  • 162
    • 0029934119 scopus 로고    scopus 로고
    • Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes
    • Hebert DN, Foellmer B, Helenius A. Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes. EMBO J 1996 15 : 2961 2968. (Pubitemid 26187744)
    • (1996) EMBO Journal , vol.15 , Issue.12 , pp. 2961-2968
    • Hebert, D.N.1    Foellmer, B.2    Helenius, A.3
  • 163
    • 0037245727 scopus 로고    scopus 로고
    • N-linked glycans direct the cotranslational folding pathway of Influenza hemagglutinin
    • DOI 10.1016/S1097-2765(02)00821-3
    • Daniels R, Kurowski B, Johnson AE, Hebert DN. N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin. Mol Cell 2003 11 : 79 90. (Pubitemid 36126592)
    • (2003) Molecular Cell , vol.11 , Issue.1 , pp. 79-90
    • Daniels, R.1    Kurowski, B.2    Johnson, A.E.3    Hebert, D.N.4
  • 164
    • 0033385217 scopus 로고    scopus 로고
    • Kinetics of interactions of Sendai virus envelope glycoproteins, F and HN, with endoplasmic reticulum-resident molecular chaperones, BiP, calnexin, and calreticulin
    • Tomita Y, Yamashita T, Sato H, Taira H. Kinetics of interactions of sendai virus envelope glycoproteins, F and HN, with endoplasmic reticulum-resident molecular chaperones, BiP, calnexin, and calreticulin. J Biochem 1999 126 : 1090 1100. (Pubitemid 30014456)
    • (1999) Journal of Biochemistry , vol.126 , Issue.6 , pp. 1090-1100
    • Tomita, Y.1    Yamashita, T.2    Sato, H.3    Taira, H.4
  • 165
    • 57749100292 scopus 로고    scopus 로고
    • The cotranslational maturation program for the type II membrane glycoprotein influenza neuraminidase
    • Wang N, Glidden EJ, Murphy SR, Pearse BR, Hebert DN. The cotranslational maturation program for the type II membrane glycoprotein influenza neuraminidase. J Biol Chem 2008 283 : 33826 33837.
    • (2008) J Biol Chem , vol.283 , pp. 33826-33837
    • Wang, N.1    Glidden, E.J.2    Murphy, S.R.3    Pearse, B.R.4    Hebert, D.N.5
  • 167
    • 34248226475 scopus 로고    scopus 로고
    • Interaction of HTLV-1 Tax protein with calreticulin: Implications for Tax nuclear export and secretion
    • DOI 10.1016/j.biopha.2007.02.005, PII S0753332207000200
    • Alefantis T, Flaig KE, Wigdahl B, Jain P. Interaction of HTLV-1 Tax protein with calreticulin: implications for Tax nuclear export and secretion. Biomed Pharmacother 2007 61 : 194 200. (Pubitemid 46705478)
    • (2007) Biomedicine and Pharmacotherapy , vol.61 , Issue.4 , pp. 194-200
    • Alefantis, T.1    Flaig, K.E.2    Wigdahl, B.3    Jain, P.4


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