메뉴 건너뛰기




Volumn 3, Issue 5, 2012, Pages

Herpes simplex virus γ34.5 interferes with autophagosome maturation and antigen presentation in dendritic cells

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84868381258     PISSN: 21612129     EISSN: 21507511     Source Type: Journal    
DOI: 10.1128/mBio.00267-12     Document Type: Article
Times cited : (73)

References (76)
  • 2
    • 0023136956 scopus 로고
    • Translational control mediated by eucary-otic initiation factor-2 is restricted to specific mRNAs in transfected cells
    • Kaufman RJ, Murtha P. 1987. Translational control mediated by eucary-otic initiation factor-2 is restricted to specific mRNAs in transfected cells. Mol. Cell. Biol. 7:1568-1571.
    • (1987) Mol. Cell. Biol , vol.7 , pp. 1568-1571
    • Kaufman, R.J.1    Murtha, P.2
  • 3
    • 0025320261 scopus 로고
    • Biosynthesis of reovirus-specified polypep-tides. 2-Aminopurine increases the efficiency of translation of reovirus s1 mRNA but not s4 mRNA in transfected cells
    • Samuel CE, Brody MS. 1990. Biosynthesis of reovirus-specified polypep-tides. 2-Aminopurine increases the efficiency of translation of reovirus s1 mRNA but not s4 mRNA in transfected cells. Virology 176:106-113.
    • (1990) Virology , vol.176 , pp. 106-113
    • Samuel, C.E.1    Brody, M.S.2
  • 4
    • 0026539149 scopus 로고
    • The gamma 1(34.5) gene of herpes simplex virus 1 precludes neuroblastoma cells from triggering total shutoff of protein synthesis characteristic of programed cell death in neuronal cells
    • Chou J, Roizman B. 1992. The gamma 1(34.5) gene of herpes simplex virus 1 precludes neuroblastoma cells from triggering total shutoff of protein synthesis characteristic of programed cell death in neuronal cells. Proc. Natl. Acad. Sci. U. S. A. 89:3266-3270.
    • (1992) Proc. Natl. Acad. Sci. U. S. A , vol.89 , pp. 3266-3270
    • Chou, J.1    Roizman, B.2
  • 5
    • 0028970730 scopus 로고
    • Association of a M(r) 90,000 phosphoprotein with protein kinase PKR in cells exhibiting enhanced phosphorylation of translation initiation factor eIF-2 alpha and premature shutoff of protein synthesis after infection with gamma 134.5-mutants of herpes simplex virus 1
    • Chou J, Chen JJ, Gross M, Roizman B. 1995. Association of a M(r) 90,000 phosphoprotein with protein kinase PKR in cells exhibiting enhanced phosphorylation of translation initiation factor eIF-2 alpha and premature shutoff of protein synthesis after infection with gamma 134.5-mutants of herpes simplex virus 1. Proc. Natl. Acad. Sci. U. S. A. 92: 10516-10520.
    • (1995) Proc. Natl. Acad. Sci. U. S. A , vol.92 , pp. 10516-10520
    • Chou, J.1    Chen, J.J.2    Gross, M.3    Roizman, B.4
  • 6
    • 0030793170 scopus 로고    scopus 로고
    • Suppression of the phenotype of gamma(1)34.5- herpes simplex virus 1:Failureof activated RNA-dependent protein kinasetoshut off protein synthesis is associated with a deletion in the domain of the alpha47 gene
    • He B, et al. 1997. Suppression of the phenotype of gamma(1)34.5- herpes simplex virus 1:failureof activated RNA-dependent protein kinasetoshut off protein synthesis is associated with a deletion in the domain of the alpha47 gene. J. Virol. 71:6049-6054.
    • (1997) J. Virol , vol.71 , pp. 6049-6054
    • He, B.1
  • 7
    • 38049044115 scopus 로고    scopus 로고
    • Aconserved domain of herpes simplex virus ICP34.5 regulates protein phosphatase complex in mammalian cells
    • Zhang C, et al. 2008. Aconserved domain of herpes simplex virus ICP34.5 regulates protein phosphatase complex in mammalian cells. FEBS Lett. 582:171-176.
    • (2008) FEBS Lett , vol.582 , pp. 171-176
    • Zhang, C.1
  • 8
    • 79960112123 scopus 로고    scopus 로고
    • ICP34.5 protein of herpes simplex virus facilitates the initiation of protein translation by bridging eukaryotic initiation factor 2alpha (eIF2alpha) and protein phosphatase 1
    • Li Y, et al. 2011. ICP34.5 protein of herpes simplex virus facilitates the initiation of protein translation by bridging eukaryotic initiation factor 2alpha (eIF2alpha) and protein phosphatase 1. J. Biol. Chem. 286: 24785-24792.
    • (2011) J. Biol. Chem , vol.286 , pp. 24785-24792
    • Li, Y.1
  • 9
    • 59449109932 scopus 로고    scopus 로고
    • Control of TANK-binding kinase 1-mediated signaling by the gamma(1)34.5 protein of herpes simplex virus 1
    • Verpooten D, Ma Y, Hou S, Yan Z, He B. 2009. Control of TANK-binding kinase 1-mediated signaling by the gamma(1)34.5 protein of herpes simplex virus 1. J. Biol. Chem. 284:1097-1105.
    • (2009) J. Biol. Chem , vol.284 , pp. 1097-1105
    • Verpooten, D.1    Ma, Y.2    Hou, S.3    Yan, Z.4    He, B.5
  • 10
    • 84863127174 scopus 로고    scopus 로고
    • Inhibition of TANK binding kinase 1 by herpes simplex virus 1 facilitates productive infection
    • Ma Y, et al. 2012. Inhibition of TANK binding kinase 1 by herpes simplex virus 1 facilitates productive infection. J. Virol. 86:2188-2196.
    • (2012) J. Virol , vol.86 , pp. 2188-2196
    • Ma, Y.1
  • 11
    • 0037039442 scopus 로고    scopus 로고
    • Regulation of starvation- and virus-induced autophagy by the eIF2alpha kinase signaling pathway
    • Tallóczy Z, et al. 2002. Regulation of starvation- and virus-induced autophagy by the eIF2alpha kinase signaling pathway. Proc. Natl. Acad. Sci. U. S. A. 99:190-195.
    • (2002) Proc. Natl. Acad. Sci. U. S. A , vol.99 , pp. 190-195
    • Tallóczy, Z.1
  • 12
    • 0000730374 scopus 로고
    • Cytoplasmic components in hepatic cell lysosomes
    • Ashford TP, Porter KR. 1962. Cytoplasmic components in hepatic cell lysosomes. J. Cell Biol. 12:198-202.
    • (1962) J. Cell Biol , vol.12 , pp. 198-202
    • Ashford, T.P.1    Porter, K.R.2
  • 14
    • 0020040519 scopus 로고
    • Accumulation of autophagosomes after inhibition of hepatocytic protein degradation by vinblastine, leupep-tin or a lysosomotropic amine
    • Kovács AL, Reith A, Seglen PO. 1982. Accumulation of autophagosomes after inhibition of hepatocytic protein degradation by vinblastine, leupep-tin or a lysosomotropic amine. Exp. Cell Res. 137:191-201.
    • (1982) Exp. Cell Res , vol.137 , pp. 191-201
    • Kovács, A.L.1    Reith, A.2    Seglen, P.O.3
  • 15
    • 0024237661 scopus 로고
    • Amino acid control of intracellular protein degradation
    • Mortimore GE, Pösö AR. 1988. Amino acid control of intracellular protein degradation. Methods Enzymol. 166:461-476.
    • (1988) Methods Enzymol , vol.166 , pp. 461-476
    • Mortimore, G.E.1    Pösö, A.R.2
  • 16
    • 0035929650 scopus 로고    scopus 로고
    • The tumor suppressor PTEN positively regulates macroautophagy by inhibiting the phosphatidylinositol 3-kinase/protein kinase B pathway
    • Arico S, et al. 2001. The tumor suppressor PTEN positively regulates macroautophagy by inhibiting the phosphatidylinositol 3-kinase/protein kinase B pathway. J. Biol. Chem. 276:35243-35246.
    • (2001) J. Biol. Chem , vol.276 , pp. 35243-35246
    • Arico, S.1
  • 17
    • 19344368318 scopus 로고    scopus 로고
    • Autophagy regulates programmed cell death during the plant innate immune response
    • Liu Y, et al. 2005. Autophagy regulates programmed cell death during the plant innate immune response. Cell 121:567-577.
    • (2005) Cell , vol.121 , pp. 567-577
    • Liu, Y.1
  • 18
    • 38949119423 scopus 로고    scopus 로고
    • Hypoxia induces autophagic cell death in apoptosis-competent cells through a mechanism involving BNIP3
    • Azad MB, et al. 2008. Hypoxia induces autophagic cell death in apoptosis-competent cells through a mechanism involving BNIP3. Autophagy 4:195-204.
    • (2008) Autophagy , vol.4 , pp. 195-204
    • Azad, M.B.1
  • 19
    • 72549095406 scopus 로고    scopus 로고
    • Regulation mechanisms and signaling pathways of autophagy
    • He C, Klionsky DJ. 2009. Regulation mechanisms and signaling pathways of autophagy. Annu. Rev. Genet. 43:67-93.
    • (2009) Annu. Rev. Genet , vol.43 , pp. 67-93
    • He, C.1    Klionsky, D.J.2
  • 20
    • 34250864795 scopus 로고    scopus 로고
    • Protein turnover via autophagy: Implications for metabolism
    • Mizushima N, Klionsky DJ. 2007. Protein turnover via autophagy: implications for metabolism. Annu. Rev. Nutr. 27:19-40.
    • (2007) Annu. Rev. Nutr , vol.27 , pp. 19-40
    • Mizushima, N.1    Klionsky, D.J.2
  • 21
    • 67649607465 scopus 로고    scopus 로고
    • Autophagy, immunity, and microbial adaptations
    • Deretic V, Levine B. 2009. Autophagy, immunity, and microbial adaptations. Cell Host Microbe 5:527-549.
    • (2009) Cell Host Microbe , vol.5 , pp. 527-549
    • Deretic, V.1    Levine, B.2
  • 22
    • 0035911162 scopus 로고    scopus 로고
    • Dissection of autophagosome formation using Apg5-deficient mouse embryonic stem cells
    • Mizushima N, et al. 2001. Dissection of autophagosome formation using Apg5-deficient mouse embryonic stem cells. J. Cell Biol. 152:657-668.
    • (2001) J. Cell Biol , vol.152 , pp. 657-668
    • Mizushima, N.1
  • 24
    • 57549094368 scopus 로고    scopus 로고
    • The Atg8 conjugation system is indispensable for proper development of autophagic isolation membranes in mice
    • Sou YS, et al. 2008. The Atg8 conjugation system is indispensable for proper development of autophagic isolation membranes in mice. Mol. Biol. Cell 19:4762-4775.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 4762-4775
    • Sou, Y.S.1
  • 25
    • 79953153833 scopus 로고    scopus 로고
    • The late stage of autophagy: Cellular events and molecular regulation
    • Tong J, Yan X, Yu L. 2010. The late stage of autophagy: cellular events and molecular regulation. Protein Cell 1:907-915.
    • (2010) Protein Cell , vol.1 , pp. 907-915
    • Tong, J.1    Yan, X.2    Yu, L.3
  • 26
    • 0000906170 scopus 로고    scopus 로고
    • Induction of autophagy and inhibition of tumor-igenesis by beclin 1
    • Liang XH, et al. 1999. Induction of autophagy and inhibition of tumor-igenesis by beclin 1. Nature 402:672-676.
    • (1999) Nature , vol.402 , pp. 672-676
    • Liang, X.H.1
  • 27
    • 0035032723 scopus 로고    scopus 로고
    • Beclin-phosphatidylinositol 3-kinase complex functions at the trans-Golgi network
    • Kihara A, Kabeya Y, Ohsumi Y, Yoshimori T. 2001. Beclin-phosphatidylinositol 3-kinase complex functions at the trans-Golgi network. EMBO Rep. 2:330-335.
    • (2001) EMBO Rep , vol.2 , pp. 330-335
    • Kihara, A.1    Kabeya, Y.2    Ohsumi, Y.3    Yoshimori, T.4
  • 28
    • 33846224369 scopus 로고    scopus 로고
    • Antigen-loading compartments for major histocompatibility complex class II molecules continuously receive input from autophagosomes
    • Schmid D, Pypaert M, Münz C. 2007. Antigen-loading compartments for major histocompatibility complex class II molecules continuously receive input from autophagosomes. Immunity 26:79-92.
    • (2007) Immunity , vol.26 , pp. 79-92
    • Schmid, D.1    Pypaert, M.2    Münz, C.3
  • 29
    • 76949091325 scopus 로고    scopus 로고
    • In vivo requirement for Atg5 in antigen presentation by dendritic cells
    • Lee HK, et al. 2010. In vivo requirement for Atg5 in antigen presentation by dendritic cells. Immunity 32:227-239.
    • (2010) Immunity , vol.32 , pp. 227-239
    • Lee, H.K.1
  • 30
    • 67649585835 scopus 로고    scopus 로고
    • Autophagy pathway intersects with HIV-1 biosynthesis and regulates viral yields in macrophages
    • Kyei GB, et al. 2009. Autophagy pathway intersects with HIV-1 biosynthesis and regulates viral yields in macrophages. J. Cell Biol. 186:255-268.
    • (2009) J. Cell Biol , vol.186 , pp. 255-268
    • Kyei, G.B.1
  • 31
    • 72649105081 scopus 로고    scopus 로고
    • Matrix protein 2 of influenza A virus blocks autophagosome fusion with lysosomes
    • Gannagé M, et al. 2009. Matrix protein 2 of influenza A virus blocks autophagosome fusion with lysosomes. Cell Host Microbe 6:367-380.
    • (2009) Cell Host Microbe , vol.6 , pp. 367-380
    • Gannagé, M.1
  • 32
    • 54449101892 scopus 로고    scopus 로고
    • Induction of incomplete autophagic response by hepatitis C virus via the unfolded protein response
    • Sir D, et al. 2008. Induction of incomplete autophagic response by hepatitis C virus via the unfolded protein response. Hepatology 48: 1054-1061.
    • (2008) Hepatology , vol.48 , pp. 1054-1061
    • Sir, D.1
  • 33
    • 77749292148 scopus 로고    scopus 로고
    • The early autophagic pathway is activated by hepatitis B virus and required for viral DNA replication
    • Sir D, et al. 2010. The early autophagic pathway is activated by hepatitis B virus and required for viral DNA replication. Proc. Natl. Acad. Sci. U. S. A 107:4383-4388.
    • (2010) Proc. Natl. Acad. Sci. U. S. A , vol.107 , pp. 4383-4388
    • Sir, D.1
  • 34
    • 50949133741 scopus 로고    scopus 로고
    • Autophagosome supports coxsackievirus B3 replication in host cells
    • Wong J, et al. 2008. Autophagosome supports coxsackievirus B3 replication in host cells. J. Virol. 82:9143-9153.
    • (2008) J. Virol , vol.82 , pp. 9143-9153
    • Wong, J.1
  • 35
    • 79960793780 scopus 로고    scopus 로고
    • Functional macroautophagy induction by influenza A virus without a contribution to major histocompatibility complex class II-restricted presentation
    • Comber JD, Robinson TM, Siciliano NA, Snook AE, Eisenlohr LC. 2011. Functional macroautophagy induction by influenza A virus without a contribution to major histocompatibility complex class II-restricted presentation. J. Virol. 85:6453-6463.
    • (2011) J. Virol , vol.85 , pp. 6453-6463
    • Comber, J.D.1    Robinson, T.M.2    Siciliano, N.A.3    Snook, A.E.4    Eisenlohr, L.C.5
  • 36
    • 84868383605 scopus 로고    scopus 로고
    • Autophagosomal protein dynamics and influenza virus infection
    • Dumit VI, Dengjel J. 2012. Autophagosomal protein dynamics and influenza virus infection. Front. Immunol. 3:43.
    • (2012) Front. Immunol , vol.3 , pp. 43
    • Dumit, V.I.1    Dengjel, J.2
  • 37
    • 33644609471 scopus 로고    scopus 로고
    • PKR-dependent autophagic degradation of herpes simplex virus type 1
    • Tallóczy Z, Virgin HW IV, Levine B. 2006. PKR-dependent autophagic degradation of herpes simplex virus type 1. Autophagy 2:24-29.
    • (2006) Autophagy , vol.2 , pp. 24-29
    • Tallóczy, Z.1    Virgin, H.W.I.V.2    Levine, B.3
  • 38
    • 33947715151 scopus 로고    scopus 로고
    • HSV-1 ICP34.5 confers neurovirulence by targeting the Beclin 1 autophagy protein
    • Orvedahl A, et al. 2007. HSV-1 ICP34.5 confers neurovirulence by targeting the Beclin 1 autophagy protein. Cell Host Microbe 1:23-35.
    • (2007) Cell Host Microbe , vol.1 , pp. 23-35
    • Orvedahl, A.1
  • 39
    • 70450159587 scopus 로고    scopus 로고
    • Interaction of ICP34.5 with Beclin 1 modulates herpes simplex virus type 1 pathogenesis through control of CD4+ T-cell responses
    • Leib DA, Alexander DE, Cox D, Yin J, Ferguson TA. 2009. Interaction of ICP34.5 with Beclin 1 modulates herpes simplex virus type 1 pathogenesis through control of CD4+ T-cell responses. J.Virol. 83:12164-12171.
    • (2009) J.Virol , vol.83 , pp. 12164-12171
    • Leib, D.A.1    Alexander, D.E.2    Cox, D.3    Yin, J.4    Ferguson, T.A.5
  • 40
    • 67349269904 scopus 로고    scopus 로고
    • Autophagy enhances the presentation of endogenous viral antigens on MHC class I molecules during HSV-1 infection
    • English L, et al. 2009. Autophagy enhances the presentation of endogenous viral antigens on MHC class I molecules during HSV-1 infection. Nat. Immunol. 10:480-487.
    • (2009) Nat. Immunol , vol.10 , pp. 480-487
    • English, L.1
  • 41
    • 81455135819 scopus 로고    scopus 로고
    • Activation of autophagy by a-herpesviruses in myeloid cells is mediated by cytoplasmic viral DNA through a mechanism dependent on stimulator of IFN genes
    • Rasmussen SB, et al. 2011. Activation of autophagy by a-herpesviruses in myeloid cells is mediated by cytoplasmic viral DNA through a mechanism dependent on stimulator of IFN genes. J. Immunol. 187:5268-5276.
    • (2011) J. Immunol , vol.187 , pp. 5268-5276
    • Rasmussen, S.B.1
  • 42
    • 65349167768 scopus 로고    scopus 로고
    • The gamma 1 34.5 protein of herpes simplex virus 1 is required to interfere with dendritic cell maturation during productive infection
    • Jin H, et al. 2009. The gamma 1 34.5 protein of herpes simplex virus 1 is required to interfere with dendritic cell maturation during productive infection. J. Virol. 83:4984-4994.
    • (2009) J. Virol , vol.83 , pp. 4984-4994
    • Jin, H.1
  • 43
    • 79952583971 scopus 로고    scopus 로고
    • A herpesvirus virulence factor inhibits dendritic cell maturation through protein phosphatase 1 and Ikappa B kinase
    • Jin H, Yan Z, Ma Y, Cao Y, He B. 2011. A herpesvirus virulence factor inhibits dendritic cell maturation through protein phosphatase 1 and Ikappa B kinase. J. Virol. 85:3397-3407.
    • (2011) J. Virol , vol.85 , pp. 3397-3407
    • Jin, H.1    Yan, Z.2    Ma, Y.3    Cao, Y.4    He, B.5
  • 44
    • 64749117051 scopus 로고    scopus 로고
    • Differential migration of epidermal and dermal dendritic cells during skin infection
    • Eidsmo L, et al. 2009. Differential migration of epidermal and dermal dendritic cells during skin infection. J. Immunol. 182:3165-3172.
    • (2009) J. Immunol , vol.182 , pp. 3165-3172
    • Eidsmo, L.1
  • 45
    • 35848967804 scopus 로고    scopus 로고
    • How to interpret LC3 immunoblot-ting
    • Mizushima N, Yoshimori T. 2007. How to interpret LC3 immunoblot-ting. Autophagy 3:542-545.
    • (2007) Autophagy , vol.3 , pp. 542-545
    • Mizushima, N.1    Yoshimori, T.2
  • 46
    • 0025925091 scopus 로고
    • Bafilomycin A1, a specific inhibitor of vacuolar-type H(+)-ATPase, inhibits acidification and protein degradation in lysosomes of cultured cells
    • Yoshimori T, Yamamoto A, Moriyama Y, Futai M, Tashiro Y. 1991. Bafilomycin A1, a specific inhibitor of vacuolar-type H(+)-ATPase, inhibits acidification and protein degradation in lysosomes of cultured cells. J. Biol. Chem. 266:17707-17712.
    • (1991) J. Biol. Chem , vol.266 , pp. 17707-17712
    • Yoshimori, T.1    Yamamoto, A.2    Moriyama, Y.3    Futai, M.4    Tashiro, Y.5
  • 47
    • 0031593675 scopus 로고    scopus 로고
    • Bafilomycin A1 prevents maturation of autophagic vacuoles by inhibiting fusion between autophagosomes and lysosomes in rat hepatoma cell line, H-4-II-E cells
    • Yamamoto A, et al. 1998. Bafilomycin A1 prevents maturation of autophagic vacuoles by inhibiting fusion between autophagosomes and lysosomes in rat hepatoma cell line, H-4-II-E cells. Cell Struct. Funct. 23: 33-42.
    • (1998) Cell Struct. Funct , vol.23 , pp. 33-42
    • Yamamoto, A.1
  • 48
    • 27944504351 scopus 로고    scopus 로고
    • p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
    • Bjørkøy G, et al. 2005. p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. J. Cell Biol. 171:603-614.
    • (2005) J. Cell Biol , vol.171 , pp. 603-614
    • Bjørkøy, G.1
  • 49
    • 59249105964 scopus 로고    scopus 로고
    • Monitoring autophagic degradation of p62/ SQSTM1
    • Bjørkøy G, et al. 2009. Monitoring autophagic degradation of p62/ SQSTM1. Methods Enzymol. 452:181-197.
    • (2009) Methods Enzymol , vol.452 , pp. 181-197
    • Bjørkøy, G.1
  • 50
    • 0031569109 scopus 로고    scopus 로고
    • Cloned dendritic cells can present exogenous antigens on both MHC class I and class II molecules
    • Shen Z, Reznikoff G, Dranoff G, Rock KL. 1997. Cloned dendritic cells can present exogenous antigens on both MHC class I and class II molecules. J. Immunol. 158:2723-2730.
    • (1997) J. Immunol , vol.158 , pp. 2723-2730
    • Shen, Z.1    Reznikoff, G.2    Dranoff, G.3    Rock, K.L.4
  • 51
    • 83955164193 scopus 로고    scopus 로고
    • Suppression of the maturation and activation of the dendritic cell line DC2.4 by melanoma-derived factors
    • Hargadon KM, Forrest OA, Reddy PR. 2012. Suppression of the maturation and activation of the dendritic cell line DC2.4 by melanoma-derived factors. Cell. Immunol. 272:275-282.
    • (2012) Cell Immunol , vol.272 , pp. 275-282
    • Hargadon, K.M.1    Forrest, O.A.2    Reddy, P.R.3
  • 52
    • 0027424777 scopus 로고
    • Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae
    • Tsukada M, Ohsumi Y. 1993. Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae. FEBS Lett. 333: 169-174.
    • (1993) FEBS Lett , vol.333 , pp. 169-174
    • Tsukada, M.1    Ohsumi, Y.2
  • 53
    • 24744441497 scopus 로고    scopus 로고
    • Autophagy is required for maintenance of amino acid levels and protein synthesis under nitrogen starvation
    • Onodera J, Ohsumi Y. 2005. Autophagy is required for maintenance of amino acid levels and protein synthesis under nitrogen starvation. J. Biol. Chem. 280:31582-31586.
    • (2005) J. Biol. Chem , vol.280 , pp. 31582-31586
    • Onodera, J.1    Ohsumi, Y.2
  • 54
    • 19944434059 scopus 로고    scopus 로고
    • Inhibition of macroautophagy triggers apoptosis
    • Boya P, et al. 2005. Inhibition of macroautophagy triggers apoptosis. Mol. Cell. Biol. 25:1025-1040.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 1025-1040
    • Boya, P.1
  • 55
    • 0021724835 scopus 로고
    • Segregation of mutant ovalbumins and ovalbumin-globin fusion proteins in Xenopus oocytes. Identification of an ovalbumin signal sequence
    • Tabe L, et al. 1984. Segregation of mutant ovalbumins and ovalbumin-globin fusion proteins in Xenopus oocytes. Identification of an ovalbumin signal sequence. J. Mol. Biol. 180:645-666.
    • (1984) J. Mol. Biol , vol.180 , pp. 645-666
    • Tabe, L.1
  • 56
    • 0031468120 scopus 로고    scopus 로고
    • Influence of cellular location of expressed antigen on the efficacy of DNA vaccination: Cytotoxic T lymphocyte and antibody responses are suboptimal when antigen is cytoplasmic after intramuscular DNA immunization
    • Boyle JS, Koniaras C, Lew AM. 1997. Influence of cellular location of expressed antigen on the efficacy of DNA vaccination: cytotoxic T lymphocyte and antibody responses are suboptimal when antigen is cytoplasmic after intramuscular DNA immunization. Int. Immunol. 9:1897-1906.
    • (1997) Int. Immunol , vol.9 , pp. 1897-1906
    • Boyle, J.S.1    Koniaras, C.2    Lew, A.M.3
  • 57
    • 0031897801 scopus 로고    scopus 로고
    • Defective TCR expression in transgenic mice constructed using cDNA-based alpha- and beta-chain genes under the control of heterologous regulatory elements
    • Barnden MJ, Allison J, Heath WR, Carbone FR. 1998. Defective TCR expression in transgenic mice constructed using cDNA-based alpha- and beta-chain genes under the control of heterologous regulatory elements. Immunol. Cell Biol. 76:34-40.
    • (1998) Immunol. Cell Biol , vol.76 , pp. 34-40
    • Barnden, M.J.1    Allison, J.2    Heath, W.R.3    Carbone, F.R.4
  • 58
    • 0034193990 scopus 로고    scopus 로고
    • DO11.10 and OT-II T cells recognize a C-terminal ovalbumin 323-339 epitope
    • Robertson JM, Jensen PE, Evavold BD. 2000. DO11.10 and OT-II T cells recognize a C-terminal ovalbumin 323-339 epitope. J. Immunol. 164: 4706-4712.
    • (2000) J. Immunol , vol.164 , pp. 4706-4712
    • Robertson, J.M.1    Jensen, P.E.2    Evavold, B.D.3
  • 59
    • 84863006955 scopus 로고    scopus 로고
    • Herpes simplex virus type I induces an incomplete autophagic response in human neuroblastoma cells
    • Santana S, Bullido MJ, Recuero M, Valdivieso F, Aldudo J. 2012. Herpes simplex virus type I induces an incomplete autophagic response in human neuroblastoma cells. J. Alzheimers Dis. 30:815-831.
    • (2012) J. Alzheimers Dis , vol.30 , pp. 815-831
    • Santana, S.1    Bullido, M.J.2    Recuero, M.3    Valdivieso, F.4    Aldudo, J.5
  • 60
    • 84857195479 scopus 로고    scopus 로고
    • Activation of autophagy by inflammatory signals limits IL-1/3 production by targeting ubiquitinated inflammasomes for destruction
    • Shi CS, et al. 2012. Activation of autophagy by inflammatory signals limits IL-1/3 production by targeting ubiquitinated inflammasomes for destruction. Nat. Immunol. 13:255-263.
    • (2012) Nat. Immunol , vol.13 , pp. 255-263
    • Shi, C.S.1
  • 61
    • 79955577268 scopus 로고    scopus 로고
    • Crucial role for autophagy in degranulation of mast cells
    • e6. PubMed
    • Ushio H, et al. 2011. Crucial role for autophagy in degranulation of mast cells. J. Allergy Clin. Immunol. 127:1267-1276.e6. PubMed.
    • (2011) J. Allergy Clin. Immunol , vol.127 , pp. 1267-1276
    • Ushio, H.1
  • 62
    • 80455122654 scopus 로고    scopus 로고
    • Autophagy machinery mediates macroendocytic processing and entotic cell death by targeting single membranes
    • Florey O, Kim SE, Sandoval CP, Haynes CM, Overholtzer M. 2011. Autophagy machinery mediates macroendocytic processing and entotic cell death by targeting single membranes. Nat. Cell Biol. 13:1335-1343.
    • (2011) Nat. Cell Biol , vol.13 , pp. 1335-1343
    • Florey, O.1    Kim, S.E.2    Sandoval, C.P.3    Haynes, C.M.4    Overholtzer, M.5
  • 63
    • 80054825045 scopus 로고    scopus 로고
    • Microtubule-associated protein 1 light chain 3 alpha (LC3)-associated phagocytosis is required for the efficient clearance of dead cells
    • Martinez J, et al. 2011. Microtubule-associated protein 1 light chain 3 alpha (LC3)-associated phagocytosis is required for the efficient clearance of dead cells. Proc. Natl. Acad. Sci. U. S. A. 108:17396-17401.
    • (2011) Proc. Natl. Acad. Sci. U. S. A , vol.108 , pp. 17396-17401
    • Martinez, J.1
  • 64
    • 0036634212 scopus 로고    scopus 로고
    • Cell surface major histocompatibility complex class II proteins are regulated by the products of the gamma(1)34.5 and U(L)41 genes of herpes simplex virus 1
    • Trgovcich J, Johnson D, Roizman B. 2002. Cell surface major histocompatibility complex class II proteins are regulated by the products of the gamma(1)34.5 and U(L)41 genes of herpes simplex virus 1. J. Virol. 76: 6974-6986.
    • (2002) J. Virol , vol.76 , pp. 6974-6986
    • Trgovcich, J.1    Johnson, D.2    Roizman, B.3
  • 65
    • 0032871905 scopus 로고    scopus 로고
    • Inhibition of dendritic cell maturation by herpes simplex virus
    • Salio M, Cella M, Suter M, Lanzavecchia A. 1999. Inhibition of dendritic cell maturation by herpes simplex virus. Eur. J. Immunol. 29: 3245-3253.
    • (1999) Eur. J. Immunol , vol.29 , pp. 3245-3253
    • Salio, M.1    Cella, M.2    Suter, M.3    Lanzavecchia, A.4
  • 66
    • 0742272509 scopus 로고    scopus 로고
    • Toll-like receptors and dendritic cells: For whom the bug tolls
    • Reis e Sousa C. 2004. Toll-like receptors and dendritic cells: for whom the bug tolls. Semin. Immunol. 16:27-34.
    • (2004) Semin. Immunol , vol.16 , pp. 27-34
    • Reis e Sousa, C.1
  • 67
    • 76349090912 scopus 로고    scopus 로고
    • The IKK complex contributes to the induction of autophagy
    • Criollo A, et al. 2010. The IKK complex contributes to the induction of autophagy. EMBO J. 29:619-631.
    • (2010) EMBO J , vol.29 , pp. 619-631
    • Criollo, A.1
  • 68
    • 80052045217 scopus 로고    scopus 로고
    • Subversion of cellular autophagy machinery by hepatitis B virus for viral envelopment
    • Li J, et al. 2011. Subversion of cellular autophagy machinery by hepatitis B virus for viral envelopment. J. Virol. 85:6319-6333.
    • (2011) J. Virol , vol.85 , pp. 6319-6333
    • Li, J.1
  • 69
    • 84865357562 scopus 로고    scopus 로고
    • TBK-1 Promotes autophagy-mediated antimicrobial defense by controlling autophagosome maturation
    • Pilli M, et al. 2012. TBK-1 Promotes autophagy-mediated antimicrobial defense by controlling autophagosome maturation. Immunity 37: 223-234.
    • (2012) Immunity , vol.37 , pp. 223-234
    • Pilli, M.1
  • 70
    • 77956861450 scopus 로고    scopus 로고
    • Interferon regulatory factor 3-dependent pathways are critical for control of herpes simplex virus type 1 central nervous system infection
    • Menachery VD, Pasieka TJ, Leib DA. 2010. Interferon regulatory factor 3-dependent pathways are critical for control of herpes simplex virus type 1 central nervous system infection. J. Virol. 84:9685-9694.
    • (2010) J. Virol , vol.84 , pp. 9685-9694
    • Menachery, V.D.1    Pasieka, T.J.2    Leib, D.A.3
  • 71
    • 70450170073 scopus 로고    scopus 로고
    • Control of herpes simplex virus replication is mediated through an interferon regulatory factor 3-dependent pathway
    • Menachery VD, Leib DA. 2009. Control of herpes simplex virus replication is mediated through an interferon regulatory factor 3-dependent pathway. J. Virol. 83:12399-12406.
    • (2009) J. Virol , vol.83 , pp. 12399-12406
    • Menachery, V.D.1    Leib, D.A.2
  • 72
    • 36048964024 scopus 로고    scopus 로고
    • Analysis of the role of autophagy in replication of herpes simplex virus in cell culture
    • Alexander DE, Ward SL, Mizushima N, Levine B, Leib DA. 2007. Analysis of the role of autophagy in replication of herpes simplex virus in cell culture. J. Virol. 81:12128-12134.
    • (2007) J. Virol , vol.81 , pp. 12128-12134
    • Alexander, D.E.1    Ward, S.L.2    Mizushima, N.3    Levine, B.4    Leib, D.A.5
  • 73
    • 34248206736 scopus 로고    scopus 로고
    • NK cells negatively regulate antigen presentation and tumor-specific CTLs in a syngeneic lymphoma model
    • Barber MA, Zhang T, Gagne BA, Sentman CL. 2007. NK cells negatively regulate antigen presentation and tumor-specific CTLs in a syngeneic lymphoma model. J. Immunol. 178:6140-6147.
    • (2007) J. Immunol , vol.178 , pp. 6140-6147
    • Barber, M.A.1    Zhang, T.2    Gagne, B.A.3    Sentman, C.L.4
  • 74
    • 0036147535 scopus 로고    scopus 로고
    • The cyclin-dependent kinase inhibitor roscovitine inhibits the transactivating activity and alters the posttranslational modification of herpes simplex virus type 1 ICP0
    • Davido DJ, Leib DA, Schaffer PA. 2002. The cyclin-dependent kinase inhibitor roscovitine inhibits the transactivating activity and alters the posttranslational modification of herpes simplex virus type 1 ICP0. J. Virol. 76:1077-1088.
    • (2002) J. Virol , vol.76 , pp. 1077-1088
    • Davido, D.J.1    Leib, D.A.2    Schaffer, P.A.3
  • 75
    • 0024465766 scopus 로고
    • Herpes simplex virus type 1 ICP0 plays a critical role in the de novo synthesis of infectious virus following transfection of viral DNA
    • Cai WZ, Schaffer PA. 1989. Herpes simplex virus type 1 ICP0 plays a critical role in the de novo synthesis of infectious virus following transfection of viral DNA. J. Virol. 63:4579-4589.
    • (1989) J. Virol , vol.63 , pp. 4579-4589
    • Cai, W.Z.1    Schaffer, P.A.2
  • 76
    • 38949108670 scopus 로고    scopus 로고
    • Guidelines for the use and interpretation of assays for monitoring autophagy in higher eukaryotes
    • Klionsky DJ, et al. 2008. Guidelines for the use and interpretation of assays for monitoring autophagy in higher eukaryotes. Autophagy 4:151-175.
    • (2008) Autophagy , vol.4 , pp. 151-175
    • Klionsky, D.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.