메뉴 건너뛰기




Volumn 28, Issue 5, 2009, Pages 376-393

Molecular mechanisms of viral immune evasion proteins to inhibit MHC class i antigen processing and presentation

Author keywords

CTL epitope; IFN ; IRF 1; JAK STAT signal transduction pathway; MHC class I antigen presentation; viral immune evasion protein

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOVIRUS E19 PROTEIN; AMINO ACID; DERLIN 1; DOUBLE STRANDED RNA; EPITOPE; FAS ANTIGEN; FAS LIGAND; GAMMA INTERFERON; ICP47 PROTEIN; INITIATION FACTOR 2; JANUS KINASE 1; JANUS KINASE 2; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; NONSTRUCTURAL PROTEIN 1; PROTEIN E7; PROTEIN KINASE R; PROTEIN P97; PROTEIN U21; STAT1 PROTEIN; TRANSPORTER ASSOCIATED ANTIGEN PROCESSING 1; TRANSPORTER ASSOCIATED ANTIGEN PROCESSING 2; UL49.5 PROTEIN; UNCLASSIFIED DRUG; UNIQUE SHORT TERM PROTEIN 11; UNIQUE SHORT TERM PROTEIN 2; UNIQUE SHORT TERM PROTEIN 6; VCP INTERACTING MEMBRANE PROTEIN; VIRAL IMMUNE EVASION PROTEIN; VIRUS ANTIGEN; VIRUS PROTEIN; HLA ANTIGEN CLASS 1;

EID: 73349128425     PISSN: 08830185     EISSN: 15635244     Source Type: Journal    
DOI: 10.1080/08830180903013034     Document Type: Review
Times cited : (13)

References (121)
  • 1
    • 26244439658 scopus 로고    scopus 로고
    • Viral modulation of antigen presentation: Manipulation of cellular targets in the ER and beyond
    • DOI 10.1111/j.0105-2896.2005.00318.x
    • B.N. Lilley and H.L. Ploeghm, Viral modulation of antigen presentation: Manipulation of cellular targets in the ER and beyond. Immunol Rev 207: 126-144, 2005. (Pubitemid 41415013)
    • (2005) Immunological Reviews , vol.207 , pp. 126-144
    • Lilley, B.N.1    Ploegh, H.L.2
  • 2
    • 0033280323 scopus 로고    scopus 로고
    • Mechanisms of viral interference with MHC class I antigen processing and presentation
    • DOI 10.1146/annurev.cellbio.15.1.579
    • J.W. Yewdell and J.R. Bennink, Mechanisms of viral interference with MHC class I antigen processing and presentation. Annu Rev Cell Dev Biol 15: 579-606, 1999. (Pubitemid 32250387)
    • (1999) Annual Review of Cell and Developmental Biology , vol.15 , pp. 579-606
    • Yewdell, J.W.1    Bennink, J.R.2
  • 3
    • 17644370329 scopus 로고    scopus 로고
    • Cell biology of antigen processing in vitro and in vivo
    • DOI 10.1146/annurev.immunol.22.012703.104538
    • E.S. Trombetta and I. Mellman, Cell biology of antigen processing in vitro and in vivo. Annu Rev Immunol 23: 975-1028, 2005. (Pubitemid 40563191)
    • (2005) Annual Review of Immunology , vol.23 , pp. 975-1028
    • Trombetta, E.S.1    Mellman, I.2
  • 4
    • 31944452502 scopus 로고    scopus 로고
    • Modulation of the antigen transport machinery TAP by friends and enemies
    • DOI 10.1016/j.febslet.2005.11.048, PII S0014579305014183, ABC Transporters
    • R. Abele and R. Tampe, Modulation of the antigen transport machinery TAP by friends and enemies. FEBS Lett 580: 1156-1163, 2006. (Pubitemid 43186039)
    • (2006) FEBS Letters , vol.580 , Issue.4 , pp. 1156-1163
    • Abele, R.1    Tampe, R.2
  • 5
    • 0029040720 scopus 로고
    • Antigenic and sequence variation in the C-terminal unique domain of the Epstein-Barr virus nuclear antigen EBNA-1
    • M.N. Wrightham, J.P. Stewart, N.J. Janjua, S.D. Pepper, C. Sample, C.M. Rooney, and J.R. Arrand, Antigenic and sequence variation in the C-terminal unique domain of the Epstein-Barr virus nuclear antigen EBNA-1. Virology 208: 521-530, 1995.
    • (1995) Virology , vol.208 , pp. 521-530
    • Wrightham, M.N.1    Stewart, J.P.2    Janjua, N.J.3    Pepper, S.D.4    Sample, C.5    Rooney, C.M.6    Arrand, J.R.7
  • 6
    • 0034748469 scopus 로고    scopus 로고
    • MHC class I ubiquitination by a viral PHD/LAP finger protein
    • DOI 10.1016/S1074-7613(01)00213-8
    • J.M. Boname and P.G. Stevenson, MHC class I ubiquitination by a viral PHD/LAP finger protein. Immunity 15: 627-636, 2001. (Pubitemid 33016447)
    • (2001) Immunity , vol.15 , Issue.4 , pp. 627-636
    • Boname, J.M.1    Stevenson, P.G.2
  • 7
    • 0029034237 scopus 로고
    • Herpes simplex virus turns off the TAP to evade host immunity
    • A. Hill, P. Jugovic, I. York, G. Russ, J. Bennink, J. Yewdell, et al., Herpes simplex virus turns off the TAP to evade host immunity. Nature 375: 411-415, 1995.
    • (1995) Nature , vol.375 , pp. 411-415
    • Hill, A.1    Jugovic, P.2    York, I.3    Russ, G.4    Bennink, J.5    Yewdell, J.6
  • 10
    • 0029069681 scopus 로고
    • A viral inhibitor of peptide transporters for antigen presentation
    • K. Fruh, K. Ahn, H. Djaballah, P. Sempe, P.M. van Endert, R. Tampe, et al., A viral inhibitor of peptide transporters for antigen presentation. Nature 375: 415-418, 1995.
    • (1995) Nature , vol.375 , pp. 415-418
    • Fruh, K.1    Ahn, K.2    Djaballah, H.3    Sempe, P.4    Van Endert, P.M.5    Tampe, R.6
  • 11
    • 0035930545 scopus 로고    scopus 로고
    • Molecular mechanism and structural aspects of transporter associated with antigen processing inhibition by the cytomegalovirus protein US6
    • C. Kyritsis, S. Gorbulev, S. Hutschenreiter, K. Pawlitschko, R. Abele, and R. Tampe, Molecular mechanism and structural aspects of transporter associated with antigen processing inhibition by the cytomegalovirus protein US6. J Biol Chem 276: 48031-48039, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 48031-48039
    • Kyritsis, C.1    Gorbulev, S.2    Hutschenreiter, S.3    Pawlitschko, K.4    Abele, R.5    Tampe, R.6
  • 15
    • 42449157557 scopus 로고    scopus 로고
    • Spatial and mechanistic separation of cross-presentation and endogenous antigen presentation
    • DOI 10.1038/ni.1601, PII NI.1601
    • S. Burgdorf, C. Scholz, A. Kautz,R. Tampe, and C. Kurts, Spatial and mechanistic separation of cross-presentation and endogenous antigen presentation. Nat Immunol 9: 558-566, 2008. (Pubitemid 351560525)
    • (2008) Nature Immunology , vol.9 , Issue.5 , pp. 558-566
    • Burgdorf, S.1    Scholz, C.2    Kautz, A.3    Tampe, R.4    Kurts, C.5
  • 16
    • 33744914586 scopus 로고    scopus 로고
    • Bovine herpesvirus 1 UL49.5 protein inhibits the transporter associated with antigen processing despite complex formation with glycoprotein M
    • DOI 10.1128/JVI.02707-05
    • A.D. Lipinska, D. Koppers-Lalic, M. Rychlowski, P. Admiraal, F.A. Rijsewijk, K. Bienkowska-Szewczyk, and E.J. Wiertz, Bovine herpesvirus 1 UL49.5 protein inhibits the transporter associated with antigen processing despite complex formation with glycoprotein M. J Virol 80: 5822-5832, 2006. (Pubitemid 43849160)
    • (2006) Journal of Virology , vol.80 , Issue.12 , pp. 5822-5832
    • Lipinska, A.D.1    Koppers-Lalic, D.2    Rychlowski, M.3    Admiraal, P.4    Rijsewijk, F.A.M.5    Bienkowska-Szewczyk, K.6    Wiertz, E.J.H.J.7
  • 17
    • 58149316657 scopus 로고    scopus 로고
    • The varicellovirus UL49.5 protein blocks the transporter associated with antigen processing (TAP) by inhibiting essential conformational transitions in the 6+6 transmembrane TAP core complex
    • M.C. Verweij, D. Koppers-Lalic, S. Loch, F. Klauschies, H. de la Salle, E. Quinten, P.J. Lehner, et al., The varicellovirus UL49.5 protein blocks the transporter associated with antigen processing (TAP) by inhibiting essential conformational transitions in the 6+6 transmembrane TAP core complex. J Immunol 181: 4894-4907, 2008.
    • (2008) J Immunol , vol.181 , pp. 4894-4907
    • Verweij, M.C.1    Koppers-Lalic, D.2    Loch, S.3    Klauschies, F.4    De La Salle, H.5    Quinten, E.6    Lehner, P.J.7
  • 18
    • 45149112794 scopus 로고    scopus 로고
    • Signaling of a varicelloviral factor across the endoplasmic reticulum membrane induces destruction of the peptide-loading complex and immune evasion
    • S. Loch, F. Klauschies, C. Scholz, M.C. Verweij, E.J.Wiertz, J. Koch, and R. Tampe, Signaling of a varicelloviral factor across the endoplasmic reticulum membrane induces destruction of the peptide-loading complex and immune evasion. J Biol Chem 283: 13428-13436, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 13428-13436
    • Loch, S.1    Klauschies, F.2    Scholz, C.3    Verweij, M.C.4    Wiertz, E.J.5    Koch, J.6    Tampe, R.7
  • 19
    • 0033136705 scopus 로고    scopus 로고
    • Cutting edge: Adenovirus E19 has two mechanisms for affecting class I MHC expression
    • E.M. Bennett, J.R. Bennink, J.W. Yewdell, F.M. and Brodsky, Cutting edge: Adenovirus E19 has two mechanisms for affecting class I MHC expression. J Immunol 162: 5049-5052, 1999. (Pubitemid 29307102)
    • (1999) Journal of Immunology , vol.162 , Issue.9 , pp. 5049-5052
    • Bennett, E.M.1    Bennink, J.R.2    Yewdell, J.W.3    Brodsky, F.M.4
  • 20
    • 0028195011 scopus 로고
    • Association of human class I MHC alleles with the adenovirus E3/19K protein
    • D.C. Beier, J.H. Cox, D.R. Vining, P. Cresswell, and V.H. Engelhard, Association of human class I MHC alleles with the adenovirus E3/19K protein. J Immunol 152: 3862-3872, 1994. (Pubitemid 24111058)
    • (1994) Journal of Immunology , vol.152 , Issue.8 , pp. 3862-3872
    • Beier, D.C.1    Cox, J.H.2    Vining, D.R.3    Cresswell, P.4    Engelhard, V.H.5
  • 21
    • 17444387098 scopus 로고    scopus 로고
    • Rhesus cytomegalovirus contains functional homologues of US2, US3, US6, and US11
    • DOI 10.1128/JVI.79.9.5786-5798.2005
    • N.T. Pande, C. Powers, K. Ahn, and K. Fruh, Rhesus cytomegalovirus contains functional homologues of US2, US3, US6, and US11. J Virol 79: 5786-5798, 2005. (Pubitemid 40548247)
    • (2005) Journal of Virology , vol.79 , Issue.9 , pp. 5786-5798
    • Pande, N.T.1    Powers, C.2    Ahn, K.3    Fruh, K.4
  • 22
  • 23
  • 24
    • 0037038689 scopus 로고    scopus 로고
    • The bovine papillomavirus oncoprotein E5 retains MHC class I molecules in the Golgi apparatus and prevents their transport to the cell surface
    • DOI 10.1038/sj.onc.1205885
    • B. Marchetti, G.H. Ashrafi, E. Tsirimonaki, P.M. O'Brien, and M.S. Campo, The bovine papillomavirus oncoprotein E5 retains MHC class I molecules in the Golgi apparatus and prevents their transport to the cell surface. Oncogene 21: 7808-7816, 2002. (Pubitemid 35398838)
    • (2002) Oncogene , vol.21 , Issue.51 , pp. 7808-7816
    • Marchetti, B.1    Ashrafi, G.H.2    Tsirimonaki, E.3    O'Brien, P.M.4    Campo, M.S.5
  • 25
    • 0031948857 scopus 로고    scopus 로고
    • Infection of cells with varicella-zoster virus down-regulates surface expression of class I major histocompatibility complex antigens
    • J.I. Cohen, Infection of cells with varicella-zoster virus down-regulates surface expression of class I major histocompatibility complex antigens. J Infect Dis 177: 1390-1393, 1998. (Pubitemid 28194285)
    • (1998) Journal of Infectious Diseases , vol.177 , Issue.5 , pp. 1390-1393
    • Cohen, J.I.1
  • 26
    • 0033026512 scopus 로고    scopus 로고
    • Varicella-zoster virus immune evasion
    • DOI 10.1111/j.1600-065X.1999.tb01289.x
    • A. Abendroth and A. Arvin, Varicella-zoster virus immune evasion. Immunol Rev 168: 143-156, 1999. (Pubitemid 29276679)
    • (1999) Immunological Reviews , vol.168 , pp. 143-156
    • Abendroth, A.1    Arvin, A.M.2
  • 27
    • 0348013275 scopus 로고    scopus 로고
    • The ER-lumenal domain of the HHV-7 immunoevasin U21 directs class I MHC molecules to lysosomes
    • DOI 10.1046/j.1398-9219.2003.0137.x
    • A.W. Hudson, D. Blom, P.M. Howley, and H.L. Ploegh, The ER-lumenal domain of the HHV-7 immunoevasin U21 directs class I MHC molecules to lysosomes. Traffic 4: 824-837, 2003. (Pubitemid 37540586)
    • (2003) Traffic , vol.4 , Issue.12 , pp. 824-837
    • Hudson, A.W.1    Blom, D.2    Howley, P.M.3    Ploegh, H.L.4
  • 28
    • 7444258608 scopus 로고    scopus 로고
    • Recent advances in the understanding of HIV-1 Vpu accessory protein functions
    • DOI 10.2174/1568008043339695
    • J. Binette and E.A. Cohen, Recent advances in the understanding of HIV-1 Vpu accessory protein functions. Curr Drug Targets Immune Endocr Metabol Disord 4: 297-307, 2004. (Pubitemid 39445427)
    • (2004) Current Drug Targets: Immune, Endocrine and Metabolic Disorders , vol.4 , Issue.4 , pp. 297-307
    • Binette, J.1    Cohen, E.A.2
  • 29
    • 0030876219 scopus 로고    scopus 로고
    • Molecular determinants of Nef function
    • DOI 10.1007/BF02255641
    • T. Luo, J.L. Foster, and J.V. Garcia, Molecular determinants of Nef function. J Biomed Sci 4: 132-138, 1997. (Pubitemid 27374998)
    • (1997) Journal of Biomedical Science , vol.4 , Issue.4 , pp. 132-138
    • Luo, T.1    Foster, J.L.2    Garcia, J.V.3
  • 30
    • 0036091854 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus K3 utilizes the ubiquitin-proteasome system in routing class I major histocompatibility complexes to late endocytic compartments
    • DOI 10.1128/JVI.76.11.5522-5531.2002
    • M.E. Lorenzo, J.U. Jung, and H.L. Ploegh, Kaposi's sarcoma-associated herpesvirus K3 utilizes the ubiquitin-proteasome system in routing class major histocompatibility complexes to late endocytic compartments. J Virol 76: 5522-5531, 2002. (Pubitemid 34517902)
    • (2002) Journal of Virology , vol.76 , Issue.11 , pp. 5522-5531
    • Lorenzo, M.E.1    Jung, J.U.2    Ploegh, H.L.3
  • 31
    • 0034068631 scopus 로고    scopus 로고
    • Downregulation of major histocompatibility complex class I molecules by Kaposi's sarcoma-associated herpesvirus K3 and K5 proteins
    • DOI 10.1128/JVI.74.11.5300-5309.2000
    • S. Ishido, C. Wang, B.S. Lee, G.B. Cohen, and J.U. Jung, Downregulation of major histocompatibility complex class I molecules by Kaposi's sarcoma-associated herpesvirus K3 and K5 proteins. J Virol 74: 5300-5309, 2000. (Pubitemid 30313872)
    • (2000) Journal of Virology , vol.74 , Issue.11 , pp. 5300-5309
    • Ishido, S.1    Wang, C.2    Lee, B.-S.3    Cohen, G.B.4    Jung, J.U.5
  • 32
    • 0346373729 scopus 로고    scopus 로고
    • Downregulation of Major Histocompatibility Complex Class I by Human Ubiquitin Ligases Related to Viral Immune Evasion Proteins
    • DOI 10.1128/JVI.78.3.1109-1120.2004
    • E. Bartee, M. Mansouri, B.T. Hovey Nerenberg, K. Gouveia, and K. Fruh, Downregulation of major histocompatibility complex class I by human ubiquitin ligases related to viral immune evasion proteins. J Virol 78: 1109-1120, 2004. (Pubitemid 38095821)
    • (2004) Journal of Virology , vol.78 , Issue.3 , pp. 1109-1120
    • Bartee, E.1    Mansouri, M.2    Nerenberg, B.T.H.3    Gouveia, K.4    Fruh, K.5
  • 33
    • 0033667743 scopus 로고    scopus 로고
    • Inhibition of natural killer cell-mediated cytotoxicity by Kaposi's sarcoma-associated herpesvirus K5 protein
    • S. Ishido, J.K. Choi, B.S. Lee, C. Wang, M. DeMaria, R.P. Johnson, et al., Inhibition of natural killer cell-mediated cytotoxicity by Kaposi's sarcoma-associated herpesvirus K5 protein. Immunity 13: 365-374, 2000.
    • (2000) Immunity , vol.13 , pp. 365-374
    • Ishido, S.1    Choi, J.K.2    Lee, B.S.3    Wang, C.4    Demaria, M.5    Johnson, R.P.6
  • 34
    • 0036711122 scopus 로고    scopus 로고
    • Immune evasion by a novel family of viral PHD/LAP-finger proteins of gamma-2 herpesviruses and poxviruses
    • DOI 10.1016/S0168-1702(02)00120-X, PII S016817020200120X
    • K. Fruh, E. Bartee, K. Gouveia, andM.Mansouri, Immune evasion by a novel family of viral PHD/LAP-finger proteins of gamma-2 herpesviruses and poxviruses. Virus Res 88: 55-69, 2002. (Pubitemid 35251899)
    • (2002) Virus Research , vol.88 , Issue.1-2 , pp. 55-69
    • Fruh, K.1    Bartee, E.2    Gouveia, K.3    Mansouri, M.4
  • 35
    • 0037228216 scopus 로고    scopus 로고
    • The PHD/LAP-domain protein M153R of myxomavirus is a ubiquitin ligase that induces the rapid internalization and lysosomal destruction of CD4
    • DOI 10.1128/JVI.77.2.1427-1440.2003
    • M. Mansouri, E. Bartee, K. Gouveia, B.T. Hovey Nerenberg, J. Barrett, L. Thomas, et al., The PHD/LAP-domain protein M153R of myxomavirus is a ubiquitin ligase that induces the rapid internalization and lysosomal destruction of CD4. J Virol 77: 1427-1440, 2003. (Pubitemid 36055564)
    • (2003) Journal of Virology , vol.77 , Issue.2 , pp. 1427-1440
    • Mansouri, M.1    Bartee, E.2    Gouveia, K.3    Hovey Nerenberg, B.T.4    Barrett, J.5    Thomas, L.6    Thomas, G.7    McFadden, G.8    Fruh, K.9
  • 36
    • 33750959438 scopus 로고    scopus 로고
    • Viral hijacking of cellular ubiquitination pathways as an anti-innate immunity strategy
    • DOI 10.1089/vim.2006.19.349
    • M. Chen and D. Gerlier, Viral hijacking of cellular ubiquitination pathways as an anti-innate immunity strategy. Viral Immunol 19: 349-362, 2006. (Pubitemid 44735049)
    • (2006) Viral Immunology , vol.19 , Issue.3 , pp. 349-362
    • Chen, M.1    Gerlier, D.2
  • 37
    • 49549117842 scopus 로고    scopus 로고
    • Ubiquitin chain editing revealed by polyubiquitin linkage-specific antibodies
    • K. Newton, M.L. Matsumoto, I.E. Wertz, D.S. Kirkpatrick, J.R. Lill, and J. Tan. Ubiquitin chain editing revealed by polyubiquitin linkage-specific antibodies. Cell 134: 668-678, 2008.
    • (2008) Cell , vol.134 , pp. 668-678
    • Newton, K.1    Matsumoto, M.L.2    Wertz, I.E.3    Kirkpatrick, D.S.4    Lill, J.R.5    Tan, J.6
  • 38
    • 0026746290 scopus 로고
    • Structure of a diubiquitin conjugate and a model for interaction with ubiquitin conjugating enzyme (E2)
    • W.J. Cook, L.C. Jeffrey, M. Carson, Z. Chen, and C.M. Pickart, Structure of a diubiquitin conjugate and a model for interaction with ubiquitin conjugating enzyme (E2). J Biol Chem267: 16467-16471, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 16467-16471
    • Cook, W.J.1    Jeffrey, L.C.2    Carson, M.3    Chen, Z.4    Pickart, C.M.5
  • 39
    • 1342304089 scopus 로고    scopus 로고
    • 63-linked Di-ubiquitin Chain Provides Clues to Functional Diversity of Polyubiquitin Signaling
    • DOI 10.1074/jbc.M309184200
    • R. Varadan, M. Assfalg, A. Haririnia, S. Raasi, C. Pickart, and D. Fushman, Solution conformation of Lys63-linked di-ubiquitin chain provides clues to functional diversity of polyubiquitin signaling. J Biol Chem 279: 7055-7063, 2004. (Pubitemid 38248851)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.8 , pp. 7055-7063
    • Varadan, R.1    Assfalg, M.2    Haririnia, A.3    Raasi, S.4    Pickart, C.5    Fushman, D.6
  • 40
    • 0024514688 scopus 로고
    • A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein
    • V. Chau, J.W. Tobias, A. Bachmair, D. Marriott, D.J. Ecker, D.K. Gonda, and A. Varshavsky, A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein. Science 243: 1576-1583, 1989. (Pubitemid 19090506)
    • (1989) Science , vol.243 , Issue.4898 , pp. 1576-1583
    • Chau, V.1    Tobias, J.W.2    Bachmair, A.3    Marriott, D.4    Ecker, D.J.5    Gonda, D.K.6    Varshavsky, A.7
  • 41
    • 34248570795 scopus 로고    scopus 로고
    • Ubiquitin-mediated activation of TAK1 and IKK
    • DOI 10.1038/sj.onc.1210413, PII 1210413
    • A. Adhikari, M. Xu, and Z.J. Chen, Ubiquitin-mediated activation of TAK1 and IKK. Oncogene 26: 3214-3226, 2007. (Pubitemid 46763016)
    • (2007) Oncogene , vol.26 , Issue.22 , pp. 3214-3226
    • Adhikari, A.1    Xu, M.2    Chen, Z.J.3
  • 42
    • 2342477917 scopus 로고    scopus 로고
    • The novel functions of ubiquitination in signaling
    • DOI 10.1016/j.ceb.2004.02.005, PII S0955067404000146
    • L. Sun and Z.J. Chen, The novel functions of ubiquitination in signaling. Curr Opin Cell Biol 16: 119-126, 2004. (Pubitemid 38757287)
    • (2004) Current Opinion in Cell Biology , vol.16 , Issue.2 , pp. 119-126
    • Sun, L.1    Chen, Z.J.2
  • 43
    • 1042290493 scopus 로고    scopus 로고
    • Recent developments in MHC-class-I-mediated antigen presentation
    • DOI 10.1016/j.coi.2003.11.012
    • P.J. Lehner and P. Cresswell, Recent developments in MHC-class-I-mediated antigen presentation. Curr Opin Immunol 16: 82-89, 2004. (Pubitemid 38198121)
    • (2004) Current Opinion in Immunology , vol.16 , Issue.1 , pp. 82-89
    • Lehner, P.J.1    Cresswell, P.2
  • 44
    • 12344285941 scopus 로고    scopus 로고
    • The murine gamma-herpesvirus-68 MK3 protein causes TAP degradation independent of MHC class I heavy chain degradation
    • DOI 10.1002/eji.200425459
    • J.M. Boname, J.S. May, and P.G. Stevenson, The murine gamma-herpesvirus-68 MK3 protein causes TAP degradation independent of MHC class I heavy chain degradation. Eur J Immunol 35: 171-179, 2005. (Pubitemid 40123863)
    • (2005) European Journal of Immunology , vol.35 , Issue.1 , pp. 171-179
    • Boname, J.M.1    May, J.S.2    Stevenson, P.G.3
  • 45
    • 3543104812 scopus 로고    scopus 로고
    • Model for the interaction of gammaherpesvirus 68 RING-CH finger protein mK3 with major histocompatibility complex class I and the peptide-loading complex
    • DOI 10.1128/JVI.78.16.8673-8686.2004
    • X. Wang, L. Lybarger, R. Connors, M.R. Harris, and T.H. Hansen, Model for the interaction of gammaherpesvirus 68 RING-CH finger protein mK3 with major histocompatibility complex class I and the peptide-loading complex. J Virol 78: 8673-8686, 2004. (Pubitemid 39025133)
    • (2004) Journal of Virology , vol.78 , Issue.16 , pp. 8673-8686
    • Wang, X.1    Lybarger, L.2    Connors, R.3    Harris, M.R.4    Hansen, T.H.5
  • 46
    • 1642355724 scopus 로고    scopus 로고
    • Viral degradation of the MHC class I peptide loading complex
    • DOI 10.1016/S1074-7613(04)00047-0, PII S1074761304000470
    • J.M. Boname, B.D. de Lima, P.J. Lehner, and P.G. Stevenson, Viral degradation of the MHC class I peptide loading complex. Immunity 20: 305-317, 2004. (Pubitemid 38388232)
    • (2004) Immunity , vol.20 , Issue.3 , pp. 305-317
    • Boname, J.M.1    De Lima, B.D.2    Lehner, P.J.3    Stevenson, P.G.4
  • 47
    • 0037237794 scopus 로고    scopus 로고
    • Virus subversion of the MHC class I peptide-loading complex
    • DOI 10.1016/S1074-7613(02)00509-5
    • L. Lybarger, X. Wang, M.R. Harris, H.W.T. Virgin, and T.H. Hansen, Virus subversion of the MHC class I peptide-loading complex. Immunity 18: 121-130, 2003. (Pubitemid 36120693)
    • (2003) Immunity , vol.18 , Issue.1 , pp. 121-130
    • Lybarger, L.1    Wang, X.2    Harris, M.R.3    Virgin IV, H.W.4    Hansen, T.H.5
  • 48
    • 0035975641 scopus 로고    scopus 로고
    • KSHV-K5 inhibits phosphorylation of the major histocompatibility complex class I cytoplasmic tail
    • DOI 10.1006/viro.2001.1086
    • E. Paulson, C. Tran, K. Collins, and K. Fruh, KSHV-K5 inhibits phosphorylation of the major histocompatibility complex class I cytoplasmic tail. Virology 288: 369-378, 2001. (Pubitemid 32929916)
    • (2001) Virology , vol.288 , Issue.2 , pp. 369-378
    • Paulson, E.1    Tran, C.2    Collins, K.3    Fruh, K.4
  • 49
    • 0037007234 scopus 로고    scopus 로고
    • Multiple endocytic trafficking pathways of MHC class I molecules induced by a herpesvirus protein
    • DOI 10.1093/emboj/21.7.1638
    • R.E. Means, S. Ishido, X. Alvarez, and J.U. Jung, Multiple endocytic trafficking pathways of MHC class I molecules induced by a herpesvirus protein. Embo J 21: 1638-1649, 2002. (Pubitemid 34614620)
    • (2002) EMBO Journal , vol.21 , Issue.7 , pp. 1638-1649
    • Means, R.E.1    Ishido, S.2    Alvarez, X.3    Jung, J.U.4
  • 51
    • 33645466253 scopus 로고    scopus 로고
    • Structural basis for non-covalent interaction between ubiquitin and the ubiquitin conjugating enzyme variant human MMS2
    • M.J. Lewis, L.F. Saltibus, D.D. Hau, W. Xiao, and L. Spyracopoulos, Structural basis for non-covalent interaction between ubiquitin and the ubiquitin conjugating enzyme variant human MMS2. J Biomol NMR 34: 89-100, 2006.
    • (2006) J Biomol NMR , vol.34 , pp. 89-100
    • Lewis, M.J.1    Saltibus, L.F.2    Hau, D.D.3    Xiao, W.4    Spyracopoulos, L.5
  • 55
    • 33644872913 scopus 로고    scopus 로고
    • Exploring the ESCRTing machinery in eukaryotes
    • DOI 10.1016/j.tplants.2006.01.008, PII S1360138506000343
    • V. Winter and M.T. Hauser, Exploring the ESCRTing machinery in eukaryotes. Trends Plant Sci 11: 115-123, 2006. (Pubitemid 43376141)
    • (2006) Trends in Plant Science , vol.11 , Issue.3 , pp. 115-123
    • Winter, V.1    Hauser, M.-T.2
  • 56
    • 0041488656 scopus 로고    scopus 로고
    • Hrs regulates multivesicular body formation via ESCRT recruitment to endosomes
    • DOI 10.1083/jcb.200302131
    • K.G. Bache, A. Brech, A. Mehlum, and H. Stenmark, Hrs regulates multivesicular body formation via ESCRT recruitment to endosomes. J Cell Biol 162: 435-442, 2003. (Pubitemid 36988552)
    • (2003) Journal of Cell Biology , vol.162 , Issue.3 , pp. 435-442
    • Bache, K.G.1    Brech, A.2    Mehlum, A.3    Stenmark, H.4
  • 57
    • 0242643727 scopus 로고    scopus 로고
    • Hrs function: Viruses provide the clue
    • DOI 10.1016/j.tcb.2003.10.002
    • M.J. Clague and S. Urbe, Hrs function: Viruses provide the clue. Trends Cell Biol 13: 603-606, 2003. (Pubitemid 37415023)
    • (2003) Trends in Cell Biology , vol.13 , Issue.12 , pp. 603-606
    • Clague, M.J.1    Urbe, S.2
  • 58
    • 0036753657 scopus 로고    scopus 로고
    • A battle for survival: Immune control and immune evasion in murine γ-herpesvirus-68 infection
    • DOI 10.1016/S1286-4579(02)01643-X, PII S128645790201643X
    • P.G. Stevenson, J.M. Boname, B. de Lima, and S. Efstathiou, A battle for survival: Immune control and immune evasion in murine gamma-herpesvirus-68 infection. Microbes Infect 4: 1177-1182, 2002. (Pubitemid 35279525)
    • (2002) Microbes and Infection , vol.4 , Issue.11 , pp. 1177-1182
    • Stevenson, P.G.1    Boname, J.M.2    De Lima, B.3    Efstathiou, S.4
  • 61
    • 0036347729 scopus 로고    scopus 로고
    • K3-mediated evasion of CD8(+) T cells aids amplification of a latent gammaherpesvirus
    • P.G. Stevenson, J.S. May, X.G. Smith, S. Marques, H. Adler, U.H. Koszinowski, et al., K3-mediated evasion of CD8(+) T cells aids amplification of a latent gammaherpesvirus. Nat Immunol 3: 733-740, 2002.
    • (2002) Nat Immunol , vol.3 , pp. 733-740
    • Stevenson, P.G.1    May, J.S.2    Smith, X.G.3    Marques, S.4    Adler, H.5    Koszinowski, U.H.6
  • 62
    • 33646147146 scopus 로고    scopus 로고
    • Lysine-63-linked ubiquitination is required for endolysosomal degradation of class i molecules
    • L.M. Duncan, S. Piper, R.B.Dodd, M.K. Saville, C.M. Sanderson, J.P. Luzio, and P.J. Lehner, Lysine-63-linked ubiquitination is required for endolysosomal degradation of class I molecules. Embo J 25: 1635-1645, 2006.
    • (2006) Embo J , vol.25 , pp. 1635-1645
    • Duncan, L.M.1    Piper, S.2    Dodd, R.B.3    Saville, M.K.4    Sanderson, C.M.5    Luzio, J.P.6    Lehner, P.J.7
  • 63
    • 0032999976 scopus 로고    scopus 로고
    • The downregulation of CD4 and MHC-I by primate lentiviruses: A paradigm for the modulation of cell surface receptors
    • DOI 10.1111/j.1600-065X.1999.tb01282.x
    • V. Piguet, O. Schwartz, S. Le Gall, and D. Trono, The downregulation of CD4 and MHC-I by primate lentiviruses: A paradigm for the modulation of cell surface receptors. Immunol Rev 168: 51-63, 1999. (Pubitemid 29276672)
    • (1999) Immunological Reviews , vol.168 , pp. 51-63
    • Piguet, V.1    Schwartz, O.2    Le Gall, S.3    Trono, D.4
  • 64
    • 33745764302 scopus 로고    scopus 로고
    • Ultrastructure of long-range transport carriers moving from the trans Golgi network to peripheral endosomes
    • R.S. Polishchuk, E. San Pietro, A. Di Pentima, S. Tete, and J.S. Bonifacino, Ultrastructure of long-range transport carriers moving from the trans Golgi network to peripheral endosomes. Traffic 7: 1092-1103, 2006.
    • (2006) Traffic , vol.7 , pp. 1092-1103
    • Polishchuk, R.S.1    San Pietro, E.2    Di Pentima, A.3    Tete, S.4    Bonifacino, J.S.5
  • 66
    • 0040142226 scopus 로고    scopus 로고
    • Sorting of furin at the trans-Golgi network. Interaction of the cytoplasmic tail sorting signals with AP-1 Golgi-specific assembly proteins
    • M. Teuchert, W. Schafer, S. Berghofer, B. Hoflack, H.D. Klenk, and W. Garten, Sorting of furin at the trans-Golgi network. Interaction of the cytoplasmic tail sorting signals with AP-1 Golgi-specific assembly proteins.J Biol Chem 274: 8199-8207, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 8199-8207
    • Teuchert, M.1    Schafer, W.2    Berghofer, S.3    Hoflack, B.4    Klenk, H.D.5    Garten, W.6
  • 67
    • 10344258588 scopus 로고    scopus 로고
    • HIV-1 Nef disrupts MHC-I trafficking by recruiting AP-1 to the MHC-I cytoplasmic tail
    • DOI 10.1083/jcb.200407031
    • J.F. Roeth, M. Williams, M.R. Kasper, T.M. Filzen, and K.L. Collins, HIV-1 Nef disrupts MHC-I trafficking by recruiting AP-1 to the MHC-I cytoplasmic tail. J Cell Biol 167: 903-913, 2004. (Pubitemid 39628112)
    • (2004) Journal of Cell Biology , vol.167 , Issue.5 , pp. 903-913
    • Roeth, J.F.1    Kasper, M.R.2    Filzen, T.M.3    Collins, K.L.4
  • 68
    • 0026782870 scopus 로고
    • Cytomegalovirus prevents antigen presentation by blocking the transport of peptide-loaded major histocompatibility complex class i molecules into the medial-Golgi compartment
    • M. del Val, H. Hengel, H. Hacker, U. Hartlaub, T. Ruppert, P. Lucin, and U.H. Koszinowski, Cytomegalovirus prevents antigen presentation by blocking the transport of peptide-loaded major histocompatibility complex class I molecules into the medial-Golgi compartment. J Exp Med 176: 729-738, 1992.
    • (1992) J Exp Med , vol.176 , pp. 729-738
    • Del Val, M.1    Hengel, H.2    Hacker, H.3    Hartlaub, U.4    Ruppert, T.5    Lucin, P.6    Koszinowski, U.H.7
  • 69
    • 0028147393 scopus 로고
    • Restoration of cytomegalovirus antigen presentation by gamma interferon combats viral escape
    • H. Hengel, P. Lucin, S. Jonjic, T. Ruppert, and U.H. Koszinowski, Restoration of cytomegalovirus antigen presentation by gamma interferon combats viral escape. J Virol 68: 289-297, 1994.
    • (1994) J Virol , vol.68 , pp. 289-297
    • Hengel, H.1    Lucin, P.2    Jonjic, S.3    Ruppert, T.4    Koszinowski, U.H.5
  • 70
    • 0036100579 scopus 로고    scopus 로고
    • Processing and presentation of murine cytomegalovirus pORFm164-derived peptide in fibroblasts in the face of all viral immunosubversive early gene functions
    • DOI 10.1128/JVI.76.12.6044-6053.2002
    • R. Holtappels, N.K. Grzimek, C.O. Simon, D. Thomas, D. Dreis, and M.J. Reddehase, Processing and presentation of murine cytomegalovirus pORFm164-derived peptide in fibroblasts in the face of all viral immunosubversive early gene functions. J Virol 76: 6044-6053, 2002. (Pubitemid 34556299)
    • (2002) Journal of Virology , vol.76 , Issue.12 , pp. 6044-6053
    • Holtappels, R.1    Grzimek, N.K.A.2    Simon, C.O.3    Thomas, D.4    Dreis, D.5    Reddehase, M.J.6
  • 72
    • 0037120003 scopus 로고    scopus 로고
    • Major histocompatibility complex class i allele-specific cooperative and competitive interactions between immune evasion proteins of cytomegalovirus
    • M. Wagner, A. Gutermann, J. Podlech, M.J. Reddehase, and U.H. Koszinowski, Major histocompatibility complex class I allele-specific cooperative and competitive interactions between immune evasion proteins of cytomegalovirus.J Exp Med 196: 805-816, 2002.
    • (2002) J Exp Med , vol.196 , pp. 805-816
    • Wagner, M.1    Gutermann, A.2    Podlech, J.3    Reddehase, M.J.4    Koszinowski, U.H.5
  • 73
    • 0033900029 scopus 로고    scopus 로고
    • Macrophages escape inhibition of major histocompatibility complex class I-dependent antigen presentation by cytomegalovirus
    • DOI 10.1128/JVI.74.17.7861-7868.2000
    • H. Hengel, U. Reusch, G. Geginat, R. Holtappels, T. Ruppert, E. Hellebrand, and U.H.Koszinowski, Macrophages escape inhibition of major histocompatibility complex class I-dependent antigen presentation by cytomegalovirus. J Virol 74: 7861-7868, 2000. (Pubitemid 30641629)
    • (2000) Journal of Virology , vol.74 , Issue.17 , pp. 7861-7868
    • Hengel, H.1    Reusch, U.2    Geginat, G.3    Holtappels, R.4    Ruppert, T.5    Hellebrand, E.6    Koszinowski, U.H.7
  • 74
    • 30344474901 scopus 로고    scopus 로고
    • Human cytomegalovirus-encoded US2 and US11 target unassembled MHC class I heavy chains for degradation
    • DOI 10.1016/j.molimm.2005.07.005, PII S0161589005002786
    • M.T. Barel, G.C. Hassink, S. van Voorden, and E.J. Wiertz, Human cytomegalovirus-encoded US2 and US11 target unassembled MHC class I heavy chains for degradation. Mol Immunol 43: 1258-1266, 2006. (Pubitemid 43063178)
    • (2006) Molecular Immunology , vol.43 , Issue.8 , pp. 1258-1266
    • Barel, M.T.1    Hassink, G.C.2    Voorden, S.V.3    Wiertz, E.J.H.J.4
  • 75
    • 0033523771 scopus 로고    scopus 로고
    • The pathway of US11-dependent degradation of MHC class i heavy chains involves a ubiquitinconjugated intermediate
    • C.E. Shamu, C.M. Story, T.A. Rapoport, and H.L. Ploegh, The pathway of US11-dependent degradation of MHC class I heavy chains involves a ubiquitinconjugated intermediate. J Cell Biol 147: 45-58, 1999.
    • (1999) J Cell Biol , vol.147 , pp. 45-58
    • Shamu, C.E.1    Story, C.M.2    Rapoport, T.A.3    Ploegh, H.L.4
  • 76
    • 22544438727 scopus 로고    scopus 로고
    • Determination of interactions between tegument proteins of herpes simplex virus type 1
    • DOI 10.1128/JVI.79.15.9566-9571.2005
    • V. Vittone, E. Diefenbach, D. Triffett, M.W. Douglas, A.L. Cunningham, and R.J. Diefenbach, Determination of interactions between tegument proteins of herpes simplex virus type 1. J Virol 79: 9566-9571, 2005. (Pubitemid 41022299)
    • (2005) Journal of Virology , vol.79 , Issue.15 , pp. 9566-9571
    • Vittone, V.1    Diefenbach, E.2    Triffett, D.3    Douglas, M.W.4    Cunningham, A.L.5    Diefenbach, R.J.6
  • 77
    • 3042677637 scopus 로고    scopus 로고
    • A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol
    • DOI 10.1038/nature02656
    • Y. Ye, Y. Shibata, C. Yun, D. Ron, and T.A. Rapoport, A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol. Nature 429: 841-847, 2004. (Pubitemid 38843292)
    • (2004) Nature , vol.429 , Issue.6994 , pp. 841-847
    • Ye, Y.1    Shibata, Y.2    Yun, C.3    Ron, D.4    Rapoport, T.A.5
  • 78
    • 0348147560 scopus 로고    scopus 로고
    • Effective Suppression of Class I Major Histocompatibility Complex Expression by the US11 or ICP47 Genes Can Be Limited by Cell Type or Interferon-γ Exposure
    • T.J. Radosevich, T. Seregina, and C.J. Link, Effective suppression of class I major histocompatibility complex expression by the US11 or ICP47 genes can be limited by cell type or interferon-gamma exposure. Hum Gene Ther 14: 1765-1775, 2003. (Pubitemid 38010666)
    • (2003) Human Gene Therapy , vol.14 , Issue.18 , pp. 1765-1775
    • Radosevich, T.J.1    Seregina, T.2    Link, C.J.3
  • 79
    • 0036499973 scopus 로고    scopus 로고
    • Visualization of the ER-to-cytosol dislocation reaction of a type I membrane protein
    • DOI 10.1093/emboj/21.5.1041
    • E. Fiebiger, C. Story, H.L. Ploegh, and D. Tortorella, Visualization of the ER-tocytosol dislocation reaction of a type I membrane protein. Embo J 21: 1041-1053, 2002. (Pubitemid 34206177)
    • (2002) EMBO Journal , vol.21 , Issue.5 , pp. 1041-1053
    • Fiebiger, E.1    Story, C.2    Ploegh, H.L.3    Tortorella, D.4
  • 80
    • 0029791030 scopus 로고    scopus 로고
    • Human cytomegalovirus inhibits peptide translocation into the endoplasmic reticulum for MHC class I assembly
    • H. Hengel, T. Flohr, G.J. Hammerling, U.H. Koszinowski, and F.Momburg, Human cytomegalovirus inhibits peptide translocation into the endoplasmic reticulum for MHC class I assembly. J Gen Virol 77: 2287-2296, 1996. (Pubitemid 26316100)
    • (1996) Journal of General Virology , vol.77 , Issue.9 , pp. 2287-2296
    • Hengel, H.1    Flohr, T.2    Hammerling, G.J.3    Koszinowski, U.H.4    Momburg, F.5
  • 81
    • 3042616595 scopus 로고    scopus 로고
    • A membrane protein required for dislocation of misfolded proteins from the ER
    • DOI 10.1038/nature02592
    • B.N. Lilley and H.L. Ploegh, A membrane protein required for dislocation of misfolded proteins from the ER.Nature 429: 834-840, 2004. (Pubitemid 38843291)
    • (2004) Nature , vol.429 , Issue.6994 , pp. 834-840
    • Lilley, B.N.1    Ploegh, H.L.2
  • 82
    • 28344454052 scopus 로고    scopus 로고
    • Viral evasion of the MHC class I antigen-processing machinery
    • DOI 10.1007/s00424-005-1420-8
    • S. Loch and R. Tampe, Viral evasion of the MHC class I antigen-processing machinery. Pflugers Arch 451: 409-417, 2005. (Pubitemid 41719572)
    • (2005) Pflugers Archiv European Journal of Physiology , vol.451 , Issue.3 , pp. 409-417
    • Loch, S.1    Tampe, R.2
  • 84
    • 0035652377 scopus 로고    scopus 로고
    • Inhibition of IFN-γ signaling by an Epstein-Barr virus immediate-early protein
    • DOI 10.1016/S1074-7613(01)00226-6
    • T.E. Morrison, A. Mauser, A. Wong, J.P. Ting, and S.C. Kenney, Inhibition of IFNgamma signaling by an Epstein-Barr virus immediate-early protein. Immunity 15: 787-799, 2001. (Pubitemid 34008506)
    • (2001) Immunity , vol.15 , Issue.5 , pp. 787-799
    • Morrison, T.E.1    Mauser, A.2    Wong, A.3    Ting, J.P.-Y.4    Kenney, S.C.5
  • 86
    • 33644787000 scopus 로고    scopus 로고
    • Inhibition of interferon signaling by the Kaposi's sarcoma-associated herpesvirus full-length viral interferon regulatory factor 2 protein
    • DOI 10.1128/JVI.80.6.3092-3097.2006
    • S. Fuld, C. Cunningham, K. Klucher, A.J. Davison, and D.J. Blackbourn, Inhibition of interferon signaling by the Kaposi's sarcoma-associated herpesvirus full-length viral interferon regulatory factor 2 protein. J Virol 80: 3092-3097, 2006. (Pubitemid 43346406)
    • (2006) Journal of Virology , vol.80 , Issue.6 , pp. 3092-3097
    • Fuld, S.1    Cunningham, C.2    Klucher, K.3    Davison, A.J.4    Blackbourn, D.J.5
  • 87
    • 0033520422 scopus 로고    scopus 로고
    • Stat protein transactivation domains recruit p300/CBP through widely divergent sequences
    • M. Paulson, S. Pisharody, L. Pan, S. Guadagno, A.L. Mui, and D.E. Levy, Stat protein transactivation domains recruit p300/CBP through widely divergent sequences. J Biol Chem 274: 25343-25349, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 25343-25349
    • Paulson, M.1    Pisharody, S.2    Pan, L.3    Guadagno, S.4    Mui, A.L.5    Levy, D.E.6
  • 88
    • 0242384027 scopus 로고    scopus 로고
    • The C-terminal half-fragment of the Sendai virus C protein prevents the gamma-activated factor from binding to a gamma-activated sequence site
    • DOI 10.1016/S0042-6822(03)00590-7
    • B. Gotoh, T. Komatsu, K. Takeuchi, and J. Yokoo, The C-terminal half-fragment of the Sendai virus C protein prevents the gamma-activated factor from binding to a gamma-activated sequence site. Virology 316: 29-40, 2003. (Pubitemid 37346306)
    • (2003) Virology , vol.316 , Issue.1 , pp. 29-40
    • Gotoh, B.1    Komatsu, T.2    Takeuchi, K.3    Yokoo, J.4
  • 89
    • 0025346309 scopus 로고
    • A 21S enzyme complex from HeLa cells that functions in simian virus 40 DNA replication in vitro
    • DOI 10.1021/bi00479a004
    • L.H. Malkas, R.J. Hickey, C. Li, N. Pedersen, and E.F. Baril, A 21S enzyme complex from HeLa cells that functions in simian virus 40 DNA replication in vitro. Biochemistry 29: 6362-6374, 1990. (Pubitemid 20210785)
    • (1990) Biochemistry , vol.29 , Issue.27 , pp. 6362-6374
    • Malkas, L.H.1    Hickey, R.J.2    Li, C.3    Pedersen, N.4    Baril, E.F.5
  • 90
    • 0024270343 scopus 로고
    • Complete enzymatic synthesis of DNA containing the SV40 origin of replication
    • Y. Ishimi, A. Claude, P. Bullock, and J. Hurwitz, Complete enzymatic synthesis of DNA containing the SV40 origin of replication. J Biol Chem 263: 19723-19733, 1988. (Pubitemid 19016456)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.36 , pp. 19723-19733
    • Ishimi, Y.1    Claude, A.2    Bullock, P.3    Hurwitz, J.4
  • 91
    • 0026057917 scopus 로고
    • Interferon action: Binding of viral RNA to the 40-kilodalton 2′-5′-oligoadenylate synthetase in interferon-treated HeLa cells infected with encephalomyocarditis virus
    • G. Gribaudo, D. Lembo, G. Cavallo, S. Landolfo, and P. Lengyel, Interferon action: binding of viral RNA to the 40-kilodalton 2′-5′-oligoadenylate synthetase in interferon-treated HeLa cells infected with encephalomyocarditis virus. J Virol 65: 1748-1757, 1991.
    • (1991) J Virol , vol.65 , pp. 1748-1757
    • Gribaudo, G.1    Lembo, D.2    Cavallo, G.3    Landolfo, S.4    Lengyel, P.5
  • 92
    • 12244278334 scopus 로고    scopus 로고
    • Structural basis for ubiquitin-like ISG 15 protein binding to the NS1 protein of influenza B virus: A protein-protein interaction function that is not shared by the corresponding N-terminal domain of the NS1 protein of influenza A virus
    • DOI 10.1006/viro.2002.1663
    • W. Yuan, J.M. Aramini, G.T. Montelione, and R.M. Krug, Structural basis for ubiquitin-like ISG 15 protein binding to the NS1 protein of influenza B virus: A protein-protein interaction function that is not shared by the corresponding N-terminal domain of the NS1 protein of influenza A virus. Virology 304: 291-301, 2002. (Pubitemid 36069170)
    • (2002) Virology , vol.304 , Issue.2 , pp. 291-301
    • Yuan, W.1    Aramini, J.M.2    Montelione, G.T.3    Krug, R.M.4
  • 93
    • 0035253852 scopus 로고    scopus 로고
    • Influenza B virus NS1 protein inhibits conjugation of the interferon (IFN)-induced ubiquitin-like ISG15 protein
    • DOI 10.1093/emboj/20.3.362
    • W. Yuan and R.M. Krug, Influenza B virus NS1 protein inhibits conjugation of the interferon (IFN)-induced ubiquitin-like ISG15 protein. Embo J 20: 362-371, 2001. (Pubitemid 32126972)
    • (2001) EMBO Journal , vol.20 , Issue.3 , pp. 362-371
    • Yuan, W.1    Krug, R.M.2
  • 94
    • 33846211908 scopus 로고    scopus 로고
    • Antigens and autophagy: The path less travelled?
    • G.S. Taylor, and A.B. Rickinson, Antigens and Autophagy: The Path Less Travelled By? Autophagy 3: 60-62, 2007. (Pubitemid 46100717)
    • (2007) Autophagy , vol.3 , Issue.1 , pp. 60-62
    • Taylor, G.S.1    Rickinson, A.B.2
  • 95
    • 0037169360 scopus 로고    scopus 로고
    • Human interferon-γ mRNA autoregulates its translation through a pseudoknot that activates the interferon-inducible protein kinase PKR
    • DOI 10.1016/S0092-8674(02)00616-5
    • Y. Ben-Asouli, Y. Banai, Y. Pel-Or, A. Shir, and R. Kaempfer. Human interferongamma mRNA autoregulates its translation through a pseudoknot that activates the interferon-inducible protein kinase PKR. Cell 108: 221-232, 2002. (Pubitemid 34161142)
    • (2002) Cell , vol.108 , Issue.2 , pp. 221-232
    • Ben-Asouli, Y.1    Banai, Y.2    Pel-Or, Y.3    Shir, A.4    Kaempfer, R.5
  • 96
    • 0035958080 scopus 로고    scopus 로고
    • Enhanced antiviral and antiproliferative properties of a STAT1 mutant unable to interact with the protein kinase PKR
    • A.H.Wong, J.E. Durbin, S. Li, T.E. Dever, T. Decker, and A.E. Koromilas, Enhanced antiviral and antiproliferative properties of a STAT1 mutant unable to interact with the protein kinase PKR. J Biol Chem 276: 13727-13737, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 13727-13737
    • Wong, A.H.1    Durbin, J.E.2    Li, S.3    Dever, T.E.4    Decker, T.5    Koromilas, A.E.6
  • 97
    • 0035869495 scopus 로고    scopus 로고
    • Role of double-stranded RNA-dependent protein kinase in mediating hypersensitivity of fanconi anemia complementation group C cells to interferon γ, tumor necrosis factor-α, and double-stranded RNA
    • DOI 10.1182/blood.V97.6.1644
    • Q. Pang,W. Keeble, J. Diaz, T.A. Christianson, S. Fagerlie, K. Rathbun, et al., Role of double-stranded RNA-dependent protein kinase in mediating hypersensitivity of Fanconi anemia complementation group C cells to interferon gamma, tumor necrosis factor-alpha, and double-stranded RNA. Blood 97: 1644-1652, 2001. (Pubitemid 32217229)
    • (2001) Blood , vol.97 , Issue.6 , pp. 1644-1652
    • Pang, Q.1    Keeble, W.2    Diaz, J.3    Christianson, T.A.4    Fagerlie, S.5    Rathbun, K.6    Faulkner, G.R.7    O'Dwyer, M.8    Bagby Jr., G.C.9
  • 98
    • 0028820772 scopus 로고
    • The interferon-inducible protein kinase PKR modulates the transcriptional activation of immunoglobulin kappa gene
    • A.E. Koromilas, C. Cantin, A.W. Craig, R. Jagus, J. Hiscott, and N. Sonenberg, The interferon-inducible protein kinase PKR modulates the transcriptional activation of immunoglobulin kappa gene. J Biol Chem 270: 25426-25434, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 25426-25434
    • Koromilas, A.E.1    Cantin, C.2    Craig, A.W.3    Jagus, R.4    Hiscott, J.5    Sonenberg, N.6
  • 99
    • 0034721082 scopus 로고    scopus 로고
    • The interferon-induced protein kinase (PKR), triggers apoptosis through FADD-mediated activation of caspase 8 in a manner independent of Fas and TNF-α receptors
    • J. Gil andM. Esteban, The interferon-induced protein kinase (PKR), triggers apoptosis through FADD-mediated activation of caspase 8 in a manner independent of Fas and TNF-alpha receptors. Oncogene 19: 3665-3674, 2000. (Pubitemid 30608488)
    • (2000) Oncogene , vol.19 , Issue.32 , pp. 3665-3674
    • Gil, J.1    Esteban, M.2
  • 100
    • 0034898890 scopus 로고    scopus 로고
    • Inhibition of p53 tumor suppressor by viral interferon regulatory factor
    • DOI 10.1128/JVI.75.16.7572-7582.2001
    • H. Nakamura,M. Li, J. Zarycki, and J.U. Jung, Inhibition of p53 tumor suppressor by viral interferon regulatory factor. J Virol 75: 7572-7582, 2001. (Pubitemid 32738015)
    • (2001) Journal of Virology , vol.75 , Issue.16 , pp. 7572-7582
    • Nakamura, H.1    Li, M.2    Zarycki, J.3    Jung, J.U.4
  • 102
    • 0035094982 scopus 로고    scopus 로고
    • Host defense, viruses and apoptosis
    • DOI 10.1038/sj.cdd.4400823
    • G.N. Barber, Host defense, viruses and apoptosis. Cell Death Differ 8: 113-126, 2001. (Pubitemid 32201359)
    • (2001) Cell Death and Differentiation , vol.8 , Issue.2 , pp. 113-126
    • Barber, G.N.1
  • 104
    • 27844589460 scopus 로고    scopus 로고
    • Activation of the RNA-dependent protein kinase (PKR) of lymphocytes by regulatory RNAs: Implications for immunomodulation in HIV infection
    • DOI 10.2174/157016205774370447
    • M.A. Watanabe, L.R. de Souza, J.M. Murad, and F.L. De Lucca, Activation of the RNA-dependent protein kinase (PKR) of lymphocytes by regulatory RNAs: Implications for immunomodulation in HIV infection. Curr HIV Res 3: 329-337, 2005. (Pubitemid 41644874)
    • (2005) Current HIV Research , vol.3 , Issue.4 , pp. 329-337
    • Watanabe, M.A.E.1    De Souza, L.R.2    Murad, J.M.3    De Lucca, F.L.4
  • 105
  • 106
    • 0027949937 scopus 로고
    • The 58,000-dalton cellular inhibitor of the interferon-induced double-stranded RNA-activated protein kinase (PKR) is a member of the tetratricopeptide repeat family of proteins
    • T.G. Lee, N. Tang, S. Thompson, J. Miller, and M.G. Katze, The 58,000-dalton cellular inhibitor of the interferon-induced double-stranded RNA-activated protein kinase (PKR) is a member of the tetratricopeptide repeat family of proteins. Mol Cell Biol 14: 2331-2342, 1994.
    • (1994) Mol Cell Biol , vol.14 , pp. 2331-2342
    • Lee, T.G.1    Tang, N.2    Thompson, S.3    Miller, J.4    Katze, M.G.5
  • 107
    • 0033230617 scopus 로고    scopus 로고
    • PKR: A sentinel kinase for cellular stress
    • B.R.Williams, PKR: A sentinel kinase for cellular stress. Oncogene 18: 6112-6120, 1999.
    • (1999) Oncogene , vol.18 , pp. 6112-6120
    • Williams, B.R.1
  • 108
    • 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
    • M. Mulvey, J. Poppers, D. Sternberg, and I. Mohr, Regulation of eIF2alpha phosphorylation by different functions that act during discrete phases in the herpes simplex virus type 1 life cycle. J Virol 77: 10917-10928, 2003. (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
  • 109
    • 1642553357 scopus 로고    scopus 로고
    • Neutralizing innate host defenses to control viral translation in HSV-1 infected cells
    • I. Mohr, Neutralizing innate host defenses to control viral translation in HSV-1 infected cells. Int Rev Immunol 23: 199-220, 2004. (Pubitemid 38121753)
    • (2004) International Reviews of Immunology , vol.23 , Issue.1-2 , pp. 199-220
    • Mohr, I.1
  • 110
    • 0031716920 scopus 로고    scopus 로고
    • RNA binding and modulation of PKR activity
    • S. Gunnery and M.B. Mathews, RNA binding and modulation of PKR activity. Methods 15: 189-198, 1998.
    • (1998) Methods , vol.15 , pp. 189-198
    • Gunnery, S.1    Mathews, M.B.2
  • 111
    • 0033013721 scopus 로고    scopus 로고
    • A herpesvirus ribosome-associated, RNA-binding protein confers a growth advantage upon mutants deficient in a GADD34-related function
    • M. Mulvey, J. Poppers, A. Ladd, and I. Mohr, A herpesvirus ribosome-associated, RNA-binding protein confers a growth advantage upon mutants deficient in a GADD34-related function. J Virol 73: 3375-3385, 1999. (Pubitemid 29135731)
    • (1999) Journal of Virology , vol.73 , Issue.4 , pp. 3375-3385
    • Mulvey, M.1    Poppers, J.2    Ladd, A.3    Mohr, I.4
  • 112
    • 0033554631 scopus 로고    scopus 로고
    • The human papilloma virus (HPV)-18 E6 oncoprotein physically associates with Tyk2 and impairs Jak-STAT activation by interferon-α
    • DOI 10.1038/sj.onc.1202960
    • S. Li, S. Labrecque, M.C. Gauzzi, A.R. Cuddihy, A.H.Wong, S. Pellegrini, et al., The human papilloma virus (HPV)-18 E6 oncoprotein physically associates with Tyk2 and impairs Jak-STAT activation by interferon-alpha. Oncogene 18: 5727-5737, 1999. (Pubitemid 29507426)
    • (1999) Oncogene , vol.18 , Issue.42 , pp. 5727-5737
    • Li, S.1    Labrecque, S.2    Gauzzi, M.C.3    Cuddihy, A.R.4    Wong, A.H.5    Pellegrini, S.6    Matlashewski, G.J.7    Koromilas, A.E.8
  • 113
    • 18844406437 scopus 로고    scopus 로고
    • Kinetic analysis of the interactions of human papillomavirus E6 oncoproteins with the ubiquitin ligase E6AP using surface plasmon resonance
    • DOI 10.1016/j.jmb.2005.03.071, PII S0022283605003621
    • K. Zanier, S. Charbonnier, M. Baltzinger, Y. Nomine, D. Altschuh, and G. Trave, Kinetic analysis of the interactions of human papillomavirus E6 oncoproteins with the ubiquitin ligase E6AP using surface plasmon resonance. J Mol Biol 349: 401-412, 2005. (Pubitemid 40693758)
    • (2005) Journal of Molecular Biology , vol.349 , Issue.2 , pp. 401-412
    • Zanier, K.1    Charbonnier, S.2    Baltzinger, M.3    Nomine, Y.4    Altschuh, D.5    Trave, G.6    Yaniv, M.7
  • 114
    • 0037188431 scopus 로고    scopus 로고
    • Abrogation of IRF-1 response by high-risk HPV E7 protein in vivo
    • S.J. Um, J.W. Rhyu, E.J. Kim, K.C. Jeon, E.S. Hwang, and J.S. Park, Abrogation of IRF-1 response by high-risk HPV E7 protein in vivo. Cancer Lett 179: 205-212, 2002.
    • (2002) Cancer Lett , vol.179 , pp. 205-212
    • Um, S.J.1    Rhyu, J.W.2    Kim, E.J.3    Jeon, K.C.4    Hwang, E.S.5    Park, J.S.6
  • 115
    • 0034629279 scopus 로고    scopus 로고
    • Inactivation of interferon regulatory factor-1 tumor suppressor protein by HPV E7 oncoprotein. Implication for the E7-mediated immune evasion mechanism in cervical carcinogenesis
    • J.S. Park, E.J. Kim, H.J. Kwon, E.S. Hwang, S.E. Namkoong, and S.J. Um, Inactivation of interferon regulatory factor-1 tumor suppressor protein by HPV E7 oncoprotein. Implication for the E7-mediated immune evasion mechanism in cervical carcinogenesis. J Biol Chem 275: 6764-6769, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 6764-6769
    • Park, J.S.1    Kim, E.J.2    Kwon, H.J.3    Hwang, E.S.4    Namkoong, S.E.5    Um, S.J.6
  • 116
    • 0344304443 scopus 로고    scopus 로고
    • Interferon-stimulated transcription and innate antiviral immunity require deacetylase activity and histone deacetylase 1
    • DOI 10.1073/pnas.2433987100
    • I. Nusinzon and C.M. Horvath, Interferon-stimulated transcription and innate antiviral immunity require deacetylase activity and histone deacetylase 1. Proc Natl Acad Sci U S A 100: 14742-14747, 2003. (Pubitemid 37517961)
    • (2003) Proceedings of the National Academy of Sciences of the United States of America , vol.100 , Issue.25 , pp. 14742-14747
    • Nusinzon, I.1    Horvath, C.M.2
  • 117
    • 0036138855 scopus 로고    scopus 로고
    • Human papillomavirus type 16 E7 maintains elevated levels of the cdc25A tyrosine phosphatase during deregulation of cell cycle arrest
    • DOI 10.1128/JVI.76.2.619-632.2002
    • D.X. Nguyen, T.F.Westbrook, andD.J. McCance,Human papillomavirus type 16E7 maintains elevated levels of the cdc25A tyrosine phosphatase during deregulation of cell cycle arrest. J Virol 76: 619-632, 2002. (Pubitemid 34033361)
    • (2002) Journal of Virology , vol.76 , Issue.2 , pp. 619-632
    • Nguyen, D.X.1    Westbrook, T.F.2    McCance, D.J.3
  • 118
    • 0034609767 scopus 로고    scopus 로고
    • Transcriptional regulation of the major histocompatibility complex (MHC) class i heavy chain, TAP1 and LMP2 genes by the human papillomavirus (HPV) type 6b, 16 and 18 E7 oncoproteins
    • N.T. Georgopoulos, J.L. Proffitt, and G.E. Blair, Transcriptional regulation of the major histocompatibility complex (MHC) class I heavy chain, TAP1 and LMP2 genes by the human papillomavirus (HPV) type 6b, 16 and 18 E7 oncoproteins. Oncogene 19: 4930-4935, 2000.
    • (2000) Oncogene , vol.19 , pp. 4930-4935
    • Georgopoulos, N.T.1    Proffitt, J.L.2    Blair, G.E.3
  • 119
    • 0033919402 scopus 로고    scopus 로고
    • Human papillomavirus type 16 E6 induces self-ubiquitination of the E6AP ubiquitin-protein ligase
    • DOI 10.1128/JVI.74.14.6408-6417.2000
    • W.H. Kao, S.L. Beaudenon, A.L. Talis, J.M. Huibregtse, and P.M. Howley, Human papillomavirus type 16 E6 induces self-ubiquitination of the E6AP ubiquitinprotein ligase. J Virol 74: 6408-6417, 2000. (Pubitemid 30429807)
    • (2000) Journal of Virology , vol.74 , Issue.14 , pp. 6408-6417
    • Kao, W.H.1    Beaudenon, S.L.2    Talis, A.L.3    Huibregtse, J.M.4    Howley, P.M.5
  • 120
    • 0034595056 scopus 로고    scopus 로고
    • Viral interferon regulatory factor 1 of Kaposi's sarcoma-associated herpesvirus (human herpesvirus 8) binds to, and inhibits transactivation of, CREB-binding protein
    • DOI 10.1006/bbrc.2000.2393
    • T. Seo, D. Lee, B. Lee, J.H. Chung, and J. Choe, Viral interferon regulatory factor 1 of Kaposi's sarcoma-associated herpesvirus (human herpesvirus 8) binds to, and inhibits transactivation of, CREB-binding protein. Biochem Biophys Res Commun 270: 23-27, 2000. (Pubitemid 30440387)
    • (2000) Biochemical and Biophysical Research Communications , vol.270 , Issue.1 , pp. 23-27
    • Seo, T.1    Lee, D.2    Lee, B.3    Chung, J.H.4    Choe, J.5
  • 121
    • 1542289919 scopus 로고    scopus 로고
    • Kaposi's Sarcoma-assoclated Herpesvirus-encoded vIRF-3 Stimulates the Transcriptional Activity of Cellullar IRF-3 and IRF-7
    • DOI 10.1074/jbc.M309485200
    • B. Lubyova, M.J. Kellum, A.J. Frisancho, and P.M. Pitha, Kaposi's sarcomaassociated herpesvirus-encoded vIRF-3 stimulates the transcriptional activity of cellular IRF-3 and IRF-7. J Biol Chem 279: 7643-7654, 2004. (Pubitemid 38294645)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.9 , pp. 7643-7654
    • Lubyova, B.1    Kellum, M.J.2    Frisancho, A.J.3    Pitha, P.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.