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Volumn 47, Issue 10, 2017, Pages 1819-1834

Herpes simplex virus 1 interferes with autophagy of murine dendritic cells and impairs their ability to stimulate CD8+ T lymphocytes

Author keywords

Antigen presentation processing; Autophagy; CD8+ T cells; Dendritic cells; Herpes simplex virus 1; MHC class 1

Indexed keywords

CELL PROTEIN; INFECTED CELL PROTEIN 34.5; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; UNCLASSIFIED DRUG; VIRAL PROTEIN; GAMMA 34.5 PROTEIN, HUMAN HERPESVIRUS 1; HLA ANTIGEN CLASS 1; VIRUS ANTIGEN;

EID: 85032151275     PISSN: 00142980     EISSN: 15214141     Source Type: Journal    
DOI: 10.1002/eji.201646908     Document Type: Article
Times cited : (25)

References (103)
  • 1
    • 0035849323 scopus 로고    scopus 로고
    • Herpes simplex virus infections
    • Whitley, R. J. and Roizman, B., Herpes simplex virus infections. Lancet 2001. 357: 1513–1518.
    • (2001) Lancet , vol.357 , pp. 1513-1518
    • Whitley, R.J.1    Roizman, B.2
  • 2
    • 84884524056 scopus 로고    scopus 로고
    • An inquiry into the molecular basis of HSV latency and reactivation
    • Roizman, B. and Whitley, R. J., An inquiry into the molecular basis of HSV latency and reactivation. Annu. Rev. Microbiol. 2013. 67: 355–374.
    • (2013) Annu. Rev. Microbiol. , vol.67 , pp. 355-374
    • Roizman, B.1    Whitley, R.J.2
  • 3
    • 84869501436 scopus 로고    scopus 로고
    • A cultured affair: HSV latency and reactivation in neurons
    • Wilson, A. C. and Mohr, I., A cultured affair: HSV latency and reactivation in neurons. Trends Microbiol. 2012. 20: 604–611.
    • (2012) Trends Microbiol. , vol.20 , pp. 604-611
    • Wilson, A.C.1    Mohr, I.2
  • 4
    • 0032129793 scopus 로고    scopus 로고
    • Herpes simplex virus latency and the immune response
    • Daheshia, M., Feldman, L. T. and Rouse, B. T., Herpes simplex virus latency and the immune response. Curr. Opin. Microbiol. 1998. 1: 430–435.
    • (1998) Curr. Opin. Microbiol. , vol.1 , pp. 430-435
    • Daheshia, M.1    Feldman, L.T.2    Rouse, B.T.3
  • 5
    • 33947144288 scopus 로고    scopus 로고
    • A triple entente: virus, neurons, and CD8+ T cells maintain HSV-1 latency
    • Divito, S., Cherpes, T. L. and Hendricks, R. L., A triple entente: virus, neurons, and CD8+ T cells maintain HSV-1 latency. Immunol. Res. 2006. 36: 119–126.
    • (2006) Immunol. Res. , vol.36 , pp. 119-126
    • Divito, S.1    Cherpes, T.L.2    Hendricks, R.L.3
  • 6
    • 33947424353 scopus 로고    scopus 로고
    • Virus-specific CD8+ T cells accumulate near sensory nerve endings in genital skin during subclinical HSV-2 reactivation
    • Zhu, J., Koelle, D. M., Cao, J., Vazquez, J., Huang, M. L., Hladik, F., Wald, A. et al., Virus-specific CD8+ T cells accumulate near sensory nerve endings in genital skin during subclinical HSV-2 reactivation. J. Exp. Med. 2007. 204: 595–603.
    • (2007) J. Exp. Med. , vol.204 , pp. 595-603
    • Zhu, J.1    Koelle, D.M.2    Cao, J.3    Vazquez, J.4    Huang, M.L.5    Hladik, F.6    Wald, A.7
  • 7
    • 37549019986 scopus 로고    scopus 로고
    • The dermis contains langerin+ dendritic cells that develop and function independently of epidermal Langerhans cells
    • Poulin, L. F., Henri, S., de Bovis, B., Devilard, E., Kissenpfennig, A. and Malissen, B., The dermis contains langerin+ dendritic cells that develop and function independently of epidermal Langerhans cells. J. Exp. Med. 2007. 204: 3119–3131.
    • (2007) J. Exp. Med. , vol.204 , pp. 3119-3131
    • Poulin, L.F.1    Henri, S.2    de Bovis, B.3    Devilard, E.4    Kissenpfennig, A.5    Malissen, B.6
  • 8
    • 37549030450 scopus 로고    scopus 로고
    • Blood-derived dermal langerin+ dendritic cells survey the skin in the steady state
    • Ginhoux, F., Collin, M. P., Bogunovic, M., Abel, M., Leboeuf, M., Helft, J., Ochando, J. et al., Blood-derived dermal langerin+ dendritic cells survey the skin in the steady state. J. Exp. Med. 2007. 204: 3133–3146.
    • (2007) J. Exp. Med. , vol.204 , pp. 3133-3146
    • Ginhoux, F.1    Collin, M.P.2    Bogunovic, M.3    Abel, M.4    Leboeuf, M.5    Helft, J.6    Ochando, J.7
  • 10
    • 33746027329 scopus 로고    scopus 로고
    • Migratory dendritic cells transfer antigen to a lymph node-resident dendritic cell population for efficient CTL priming
    • Allan, R. S., Waithman, J., Bedoui, S., Jones, C. M., Villadangos, J. A., Zhan, Y., Lew, A. M. et al., Migratory dendritic cells transfer antigen to a lymph node-resident dendritic cell population for efficient CTL priming. Immunity 2006. 25: 153–162.
    • (2006) Immunity , vol.25 , pp. 153-162
    • Allan, R.S.1    Waithman, J.2    Bedoui, S.3    Jones, C.M.4    Villadangos, J.A.5    Zhan, Y.6    Lew, A.M.7
  • 11
    • 2942541735 scopus 로고    scopus 로고
    • Cross-presentation, dendritic cell subsets, and the generation of immunity to cellular antigens
    • Heath, W. R., Belz, G. T., Behrens, G. M., Smith, C. M., Forehan, S. P., Parish, I. A., Davey, G. M. et al., Cross-presentation, dendritic cell subsets, and the generation of immunity to cellular antigens. Immunol. Rev. 2004. 199: 9–26.
    • (2004) Immunol. Rev. , vol.199 , pp. 9-26
    • Heath, W.R.1    Belz, G.T.2    Behrens, G.M.3    Smith, C.M.4    Forehan, S.P.5    Parish, I.A.6    Davey, G.M.7
  • 13
    • 0031017382 scopus 로고    scopus 로고
    • 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
    • He, B., Gross, M. and 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. U. S. A. 1997. 94: 843–848.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 843-848
    • He, B.1    Gross, M.2    Roizman, B.3
  • 15
    • 33644609471 scopus 로고    scopus 로고
    • PKR-dependent autophagic degradation of herpes simplex virus type 1
    • Talloczy, Z., Virgin, H. W. T. and Levine, B., PKR-dependent autophagic degradation of herpes simplex virus type 1. Autophagy 2006. 2: 24–29.
    • (2006) Autophagy , vol.2 , pp. 24-29
    • Talloczy, Z.1    Virgin, H.W.T.2    Levine, B.3
  • 16
    • 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. and He, B., Control of TANK-binding kinase 1-mediated signaling by the gamma(1)34.5 protein of herpes simplex virus 1. J. Biol. Chem. 2009. 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
  • 17
    • 84863127174 scopus 로고    scopus 로고
    • Inhibition of TANK binding kinase 1 by herpes simplex virus 1 facilitates productive infection
    • Ma, Y., Jin, H., Valyi-Nagy, T., Cao, Y., Yan, Z. and He, B., Inhibition of TANK binding kinase 1 by herpes simplex virus 1 facilitates productive infection. J. Virol. 2012. 86: 2188–2196.
    • (2012) J. Virol. , vol.86 , pp. 2188-2196
    • Ma, Y.1    Jin, H.2    Valyi-Nagy, T.3    Cao, Y.4    Yan, Z.5    He, B.6
  • 19
    • 84868381258 scopus 로고    scopus 로고
    • Herpes simplex virus gamma34.5 interferes with autophagosome maturation and antigen presentation in dendritic cells
    • Gobeil, P. A. and Leib, D. A., Herpes simplex virus gamma34.5 interferes with autophagosome maturation and antigen presentation in dendritic cells. MBio 2012. 3: e00267–e00212.
    • (2012) MBio , vol.3 , pp. 212-267
    • Gobeil, P.A.1    Leib, D.A.2
  • 20
    • 79958182653 scopus 로고    scopus 로고
    • Autophagy in herpesvirus immune control and immune escape
    • Taylor, G. S., Mautner, J. and Munz, C., Autophagy in herpesvirus immune control and immune escape. Herpesviridae 2011. 2: 2.
    • (2011) Herpesviridae , vol.2 , pp. 2
    • Taylor, G.S.1    Mautner, J.2    Munz, C.3
  • 21
    • 36048964024 scopus 로고    scopus 로고
    • Analysis of the role of autophagy in replication of herpes simplex virus in cell culture
    • Alexander, D. E., Ward, S. L., Mizushima, N., Levine, B. and Leib, D. A., Analysis of the role of autophagy in replication of herpes simplex virus in cell culture. J. Virol. 2007. 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
  • 22
    • 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, D. A., Alexander, D. E., Cox, D., Yin, J. and Ferguson, T. A., Interaction of ICP34.5 with Beclin 1 modulates herpes simplex virus type 1 pathogenesis through control of CD4+ T-cell responses. J. Virol. 2009. 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
  • 24
    • 36249025723 scopus 로고    scopus 로고
    • Autophagy: process and function
    • Mizushima, N., Autophagy: process and function. Genes Dev. 2007. 21: 2861–2873.
    • (2007) Genes Dev. , vol.21 , pp. 2861-2873
    • Mizushima, N.1
  • 25
    • 77956404377 scopus 로고    scopus 로고
    • Eaten alive: a history of macroautophagy
    • Yang, Z. and Klionsky, D. J., Eaten alive: a history of macroautophagy. Nat. Cell Biol. 2010. 12: 814–822.
    • (2010) Nat. Cell Biol. , vol.12 , pp. 814-822
    • Yang, Z.1    Klionsky, D.J.2
  • 26
    • 0020510501 scopus 로고
    • Quantitative correlation between proteolysis and macro- and microautophagy in mouse hepatocytes during starvation and refeeding
    • Mortimore, G. E., Hutson, N. J. and Surmacz, C. A., Quantitative correlation between proteolysis and macro- and microautophagy in mouse hepatocytes during starvation and refeeding. Proc. Natl. Acad. Sci. U. S. A. 1983. 80: 2179–2183.
    • (1983) Proc. Natl. Acad. Sci. U. S. A. , vol.80 , pp. 2179-2183
    • Mortimore, G.E.1    Hutson, N.J.2    Surmacz, C.A.3
  • 27
    • 0024975155 scopus 로고
    • A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins
    • Chiang, H. L., Terlecky, S. R., Plant, C. P. and Dice, J. F., A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins. Science 1989. 246: 382–385.
    • (1989) Science , vol.246 , pp. 382-385
    • Chiang, H.L.1    Terlecky, S.R.2    Plant, C.P.3    Dice, J.F.4
  • 28
    • 0031041902 scopus 로고    scopus 로고
    • A population of rat liver lysosomes responsible for the selective uptake and degradation of cytosolic proteins
    • Cuervo, A. M., Dice, J. F. and Knecht, E., A population of rat liver lysosomes responsible for the selective uptake and degradation of cytosolic proteins. J. Biol. Chem. 1997. 272: 5606–5615.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5606-5615
    • Cuervo, A.M.1    Dice, J.F.2    Knecht, E.3
  • 29
    • 34848886914 scopus 로고    scopus 로고
    • Autophagosome formation: core machinery and adaptations
    • Xie, Z. and Klionsky, D. J., Autophagosome formation: core machinery and adaptations. Nat. Cell Biol. 2007. 9: 1102–1109.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 1102-1109
    • Xie, Z.1    Klionsky, D.J.2
  • 30
    • 34548700796 scopus 로고    scopus 로고
    • Unveiling the roles of autophagy in innate and adaptive immunity
    • Levine, B. and Deretic, V., Unveiling the roles of autophagy in innate and adaptive immunity. Nat. Rev. Immunol. 2007. 7: 767–777.
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 767-777
    • Levine, B.1    Deretic, V.2
  • 31
    • 34447629523 scopus 로고    scopus 로고
    • Innate and adaptive immunity through autophagy
    • Schmid, D. and Munz, C., Innate and adaptive immunity through autophagy. Immunity 2007. 27: 11–21.
    • (2007) Immunity , vol.27 , pp. 11-21
    • Schmid, D.1    Munz, C.2
  • 32
    • 84886797274 scopus 로고    scopus 로고
    • Autophagy in infection, inflammation and immunity
    • Deretic, V., Saitoh, T. and Akira, S., Autophagy in infection, inflammation and immunity. Nat. Rev. Immunol. 2013. 13: 722–737.
    • (2013) Nat. Rev. Immunol. , vol.13 , pp. 722-737
    • Deretic, V.1    Saitoh, T.2    Akira, S.3
  • 33
    • 33748331335 scopus 로고    scopus 로고
    • CD40 induces macrophage anti-Toxoplasma gondii activity by triggering autophagy-dependent fusion of pathogen-containing vacuoles and lysosomes
    • Andrade, R. M., Wessendarp, M., Gubbels, M. J., Striepen, B. and Subauste, C. S., CD40 induces macrophage anti-Toxoplasma gondii activity by triggering autophagy-dependent fusion of pathogen-containing vacuoles and lysosomes. J. Clin. Invest. 2006. 116: 2366–2377.
    • (2006) J. Clin. Invest. , vol.116 , pp. 2366-2377
    • Andrade, R.M.1    Wessendarp, M.2    Gubbels, M.J.3    Striepen, B.4    Subauste, C.S.5
  • 34
    • 10944253145 scopus 로고    scopus 로고
    • Autophagy is a defense mechanism inhibiting BCG and Mycobacterium tuberculosis survival in infected macrophages
    • Gutierrez, M. G., Master, S. S., Singh, S. B., Taylor, G. A., Colombo, M. I. and Deretic, V., Autophagy is a defense mechanism inhibiting BCG and Mycobacterium tuberculosis survival in infected macrophages. Cell 2004. 119: 753–766.
    • (2004) Cell , vol.119 , pp. 753-766
    • Gutierrez, M.G.1    Master, S.S.2    Singh, S.B.3    Taylor, G.A.4    Colombo, M.I.5    Deretic, V.6
  • 35
    • 33748444233 scopus 로고    scopus 로고
    • Vacuolar and plasma membrane stripping and autophagic elimination of Toxoplasma gondii in primed effector macrophages
    • Ling, Y. M., Shaw, M. H., Ayala, C., Coppens, I., Taylor, G. A., Ferguson, D. J. and Yap, G. S., Vacuolar and plasma membrane stripping and autophagic elimination of Toxoplasma gondii in primed effector macrophages. J. Exp. Med. 2006. 203: 2063–2071.
    • (2006) J. Exp. Med. , vol.203 , pp. 2063-2071
    • Ling, Y.M.1    Shaw, M.H.2    Ayala, C.3    Coppens, I.4    Taylor, G.A.5    Ferguson, D.J.6    Yap, G.S.7
  • 38
    • 77249112669 scopus 로고    scopus 로고
    • Antigen processing via autophagy–not only for MHC class II presentation anymore?
    • Munz, C., Antigen processing via autophagy–not only for MHC class II presentation anymore? Curr. Opin. Immunol. 2010. 22: 89–93.
    • (2010) Curr. Opin. Immunol. , vol.22 , pp. 89-93
    • Munz, C.1
  • 39
    • 67349269904 scopus 로고    scopus 로고
    • Autophagy enhances the presentation of endogenous viral antigens on MHC class I molecules during HSV-1 infection
    • English, L., Chemali, M., Duron, J., Rondeau, C., Laplante, A., Gingras, D., Alexander, D. et al., Autophagy enhances the presentation of endogenous viral antigens on MHC class I molecules during HSV-1 infection. Nat. Immunol. 2009. 10: 480–487.
    • (2009) Nat. Immunol. , vol.10 , pp. 480-487
    • English, L.1    Chemali, M.2    Duron, J.3    Rondeau, C.4    Laplante, A.5    Gingras, D.6    Alexander, D.7
  • 40
    • 84963959622 scopus 로고    scopus 로고
    • Macroautophagy proteins control MHC class I levels on dendritic cells and shape anti-viral CD8(+) T cell responses
    • Loi, M., Muller, A., Steinbach, K., Niven, J., Barreira da Silva, R., Paul, P., Ligeon, L. A. et al., Macroautophagy proteins control MHC class I levels on dendritic cells and shape anti-viral CD8(+) T cell responses. Cell Rep. 2016. 15: 1076–1087.
    • (2016) Cell Rep. , vol.15 , pp. 1076-1087
    • Loi, M.1    Muller, A.2    Steinbach, K.3    Niven, J.4    Barreira da Silva, R.5    Paul, P.6    Ligeon, L.A.7
  • 41
    • 84981507079 scopus 로고    scopus 로고
    • ATGs help MHC class II, but inhibit MHC class I antigen presentation
    • Loi, M., Gannage, M. and Munz, C., ATGs help MHC class II, but inhibit MHC class I antigen presentation. Autophagy 2016. 12: 1681–1682.
    • (2016) Autophagy , vol.12 , pp. 1681-1682
    • Loi, M.1    Gannage, M.2    Munz, C.3
  • 42
    • 84992740234 scopus 로고    scopus 로고
    • Autophagy Beyond intracellular MHC class II antigen presentation
    • Munz, C., Autophagy Beyond intracellular MHC class II antigen presentation. Trends Immunol. 2016. 37: 755–763.
    • (2016) Trends Immunol. , vol.37 , pp. 755-763
    • Munz, C.1
  • 43
    • 33846212766 scopus 로고    scopus 로고
    • Autophagy in MHC class II presentation: sampling from within
    • Menendez-Benito, V. and Neefjes, J., Autophagy in MHC class II presentation: sampling from within. Immunity 2007. 26: 1–3.
    • (2007) Immunity , vol.26 , pp. 1-3
    • Menendez-Benito, V.1    Neefjes, J.2
  • 44
    • 41449101843 scopus 로고    scopus 로고
    • Viral evasion of autophagy
    • Orvedahl, A. and Levine, B., Viral evasion of autophagy. Autophagy 2008. 4: 280–285.
    • (2008) Autophagy , vol.4 , pp. 280-285
    • Orvedahl, A.1    Levine, B.2
  • 46
    • 67649585835 scopus 로고    scopus 로고
    • Autophagy pathway intersects with HIV-1 biosynthesis and regulates viral yields in macrophages
    • Kyei, G. B., Dinkins, C., Davis, A. S., Roberts, E., Singh, S. B., Dong, C., Wu, L. et al., Autophagy pathway intersects with HIV-1 biosynthesis and regulates viral yields in macrophages. J. Cell Biol. 2009. 186: 255–268.
    • (2009) J. Cell Biol. , vol.186 , pp. 255-268
    • Kyei, G.B.1    Dinkins, C.2    Davis, A.S.3    Roberts, E.4    Singh, S.B.5    Dong, C.6    Wu, L.7
  • 48
    • 54449101892 scopus 로고    scopus 로고
    • Induction of incomplete autophagic response by hepatitis C virus via the unfolded protein response
    • Sir, D., Chen, W. L., Choi, J., Wakita, T., Yen, T. S. and Ou, J. H., Induction of incomplete autophagic response by hepatitis C virus via the unfolded protein response. Hepatology 2008. 48: 1054–1061.
    • (2008) Hepatology , vol.48 , pp. 1054-1061
    • Sir, D.1    Chen, W.L.2    Choi, J.3    Wakita, T.4    Yen, T.S.5    Ou, J.H.6
  • 49
    • 77749292148 scopus 로고    scopus 로고
    • The early autophagic pathway is activated by hepatitis B virus and required for viral DNA replication
    • Sir, D., Tian, Y., Chen, W. L., Ann, D. K., Yen, T. S. and Ou, J. H., The early autophagic pathway is activated by hepatitis B virus and required for viral DNA replication. Proc. Natl. Acad. Sci. U. S. A. 2010. 107: 4383–4388.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 4383-4388
    • Sir, D.1    Tian, Y.2    Chen, W.L.3    Ann, D.K.4    Yen, T.S.5    Ou, J.H.6
  • 50
    • 50949133741 scopus 로고    scopus 로고
    • Autophagosome supports coxsackievirus B3 replication in host cells
    • Wong, J., Zhang, J., Si, X., Gao, G., Mao, I., McManus, B. M. and Luo, H., Autophagosome supports coxsackievirus B3 replication in host cells. J. Virol. 2008. 82: 9143–9153.
    • (2008) J. Virol. , vol.82 , pp. 9143-9153
    • Wong, J.1    Zhang, J.2    Si, X.3    Gao, G.4    Mao, I.5    McManus, B.M.6    Luo, H.7
  • 51
    • 79960793780 scopus 로고    scopus 로고
    • Functional macroautophagy induction by influenza A virus without a contribution to major histocompatibility complex class II-restricted presentation
    • Comber, J. D., Robinson, T. M., Siciliano, N. A., Snook, A. E. and Eisenlohr, L. C., Functional macroautophagy induction by influenza A virus without a contribution to major histocompatibility complex class II-restricted presentation. J. Virol. 2011. 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
  • 52
    • 84868383605 scopus 로고    scopus 로고
    • Autophagosomal protein dynamics and influenza virus infection
    • Dumit, V. I. and Dengjel, J., Autophagosomal protein dynamics and influenza virus infection. Front. Immunol. 2012. 3: 43.
    • (2012) Front. Immunol. , vol.3 , pp. 43
    • Dumit, V.I.1    Dengjel, J.2
  • 53
    • 84880919517 scopus 로고    scopus 로고
    • Autophagy and viruses: adversaries or allies?
    • Dong, X. and Levine, B., Autophagy and viruses: adversaries or allies? J. Innate Immun. 2013. 5: 480–493.
    • (2013) J. Innate Immun. , vol.5 , pp. 480-493
    • Dong, X.1    Levine, B.2
  • 54
    • 0036086102 scopus 로고    scopus 로고
    • Dendritic cells: immune regulators in health and disease
    • Lipscomb, M. F. and Masten, B. J., Dendritic cells: immune regulators in health and disease. Physiol. Rev. 2002. 82: 97–130.
    • (2002) Physiol. Rev. , vol.82 , pp. 97-130
    • Lipscomb, M.F.1    Masten, B.J.2
  • 55
    • 48749092592 scopus 로고    scopus 로고
    • The known unknowns of antigen processing and presentation
    • Vyas, J. M., Van der Veen, A. G. and Ploegh, H. L., The known unknowns of antigen processing and presentation. Nat. Rev. Immunol. 2008. 8: 607–618.
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 607-618
    • Vyas, J.M.1    Van der Veen, A.G.2    Ploegh, H.L.3
  • 56
    • 0017126775 scopus 로고
    • Cross-priming for a secondary cytotoxic response to minor H antigens with H-2 congenic cells which do not cross-react in the cytotoxic assay
    • Bevan, M. J., Cross-priming for a secondary cytotoxic response to minor H antigens with H-2 congenic cells which do not cross-react in the cytotoxic assay. J. Exp. Med. 1976. 143: 1283–1288.
    • (1976) J. Exp. Med. , vol.143 , pp. 1283-1288
    • Bevan, M.J.1
  • 58
    • 34250864795 scopus 로고    scopus 로고
    • Protein turnover via autophagy: implications for metabolism
    • Mizushima, N. and Klionsky, D. J., Protein turnover via autophagy: implications for metabolism. Annu. Rev. Nutr. 2007. 27: 19–40.
    • (2007) Annu. Rev. Nutr. , vol.27 , pp. 19-40
    • Mizushima, N.1    Klionsky, D.J.2
  • 59
    • 84899131967 scopus 로고    scopus 로고
    • Autophagy in antimicrobial immunity
    • Gomes, L. C. and Dikic, I., Autophagy in antimicrobial immunity. Mol. Cell 2014. 54: 224–233.
    • (2014) Mol. Cell , vol.54 , pp. 224-233
    • Gomes, L.C.1    Dikic, I.2
  • 60
    • 84879591892 scopus 로고    scopus 로고
    • Similar antigen cross-presentation capacity and phagocytic functions in all freshly isolated human lymphoid organ-resident dendritic cells
    • Segura, E., Durand, M. and Amigorena, S., Similar antigen cross-presentation capacity and phagocytic functions in all freshly isolated human lymphoid organ-resident dendritic cells. J. Exp. Med. 2013. 210: 1035–1047.
    • (2013) J. Exp. Med. , vol.210 , pp. 1035-1047
    • Segura, E.1    Durand, M.2    Amigorena, S.3
  • 61
    • 0033942450 scopus 로고    scopus 로고
    • Mature dendritic cells infected with herpes simplex virus type 1 exhibit inhibited T-cell stimulatory capacity
    • Kruse, M., Rosorius, O., Kratzer, F., Stelz, G., Kuhnt, C., Schuler, G., Hauber, J. et al., Mature dendritic cells infected with herpes simplex virus type 1 exhibit inhibited T-cell stimulatory capacity. J. Virol. 2000. 74: 7127–7136.
    • (2000) J. Virol. , vol.74 , pp. 7127-7136
    • Kruse, M.1    Rosorius, O.2    Kratzer, F.3    Stelz, G.4    Kuhnt, C.5    Schuler, G.6    Hauber, J.7
  • 62
    • 0034978155 scopus 로고    scopus 로고
    • Immature monocyte-derived dendritic cells are productively infected with herpes simplex virus type 1
    • Mikloska, Z., Bosnjak, L. and Cunningham, A. L., Immature monocyte-derived dendritic cells are productively infected with herpes simplex virus type 1. J. Virol. 2001. 75: 5958–5964.
    • (2001) J. Virol. , vol.75 , pp. 5958-5964
    • Mikloska, Z.1    Bosnjak, L.2    Cunningham, A.L.3
  • 64
    • 0037333481 scopus 로고    scopus 로고
    • Deletion of the virion host shutoff protein (vhs) from herpes simplex virus (HSV) relieves the viral block to dendritic cell activation: potential of vhs- HSV vectors for dendritic cell-mediated immunotherapy
    • Samady, L., Costigliola, E., MacCormac, L., McGrath, Y., Cleverley, S., Lilley, C. E., Smith, J. et al., Deletion of the virion host shutoff protein (vhs) from herpes simplex virus (HSV) relieves the viral block to dendritic cell activation: potential of vhs- HSV vectors for dendritic cell-mediated immunotherapy. J. Virol. 2003. 77: 3768–3776.
    • (2003) J. Virol. , vol.77 , pp. 3768-3776
    • Samady, L.1    Costigliola, E.2    MacCormac, L.3    McGrath, Y.4    Cleverley, S.5    Lilley, C.E.6    Smith, J.7
  • 65
    • 0030016036 scopus 로고    scopus 로고
    • Molecular mechanism and species specificity of TAP inhibition by herpes simplex virus ICP47
    • Ahn, K., Meyer, T. H., Uebel, S., Sempe, P., Djaballah, H., Yang, Y., Peterson, P. A. et al., Molecular mechanism and species specificity of TAP inhibition by herpes simplex virus ICP47. EMBO J. 1996. 15: 3247–3255.
    • (1996) EMBO J. , vol.15 , pp. 3247-3255
    • Ahn, K.1    Meyer, T.H.2    Uebel, S.3    Sempe, P.4    Djaballah, H.5    Yang, Y.6    Peterson, P.A.7
  • 66
    • 0032472875 scopus 로고    scopus 로고
    • Infected cell protein (ICP)47 enhances herpes simplex virus neurovirulence by blocking the CD8+ T cell response
    • Goldsmith, K., Chen, W., Johnson, D. C. and Hendricks, R. L., Infected cell protein (ICP)47 enhances herpes simplex virus neurovirulence by blocking the CD8+ T cell response. J. Exp. Med. 1998. 187: 341–348.
    • (1998) J. Exp. Med. , vol.187 , pp. 341-348
    • Goldsmith, K.1    Chen, W.2    Johnson, D.C.3    Hendricks, R.L.4
  • 67
  • 68
    • 0034194169 scopus 로고    scopus 로고
    • Inhibition of CD83 cell surface expression during dendritic cell maturation by interference with nuclear export of CD83 mRNA
    • Kruse, M., Rosorius, O., Kratzer, F., Bevec, D., Kuhnt, C., Steinkasserer, A., Schuler, G. et al., Inhibition of CD83 cell surface expression during dendritic cell maturation by interference with nuclear export of CD83 mRNA. J. Exp. Med. 2000. 191: 1581–1590.
    • (2000) J. Exp. Med. , vol.191 , pp. 1581-1590
    • Kruse, M.1    Rosorius, O.2    Kratzer, F.3    Bevec, D.4    Kuhnt, C.5    Steinkasserer, A.6    Schuler, G.7
  • 69
    • 73949102414 scopus 로고    scopus 로고
    • The herpes simplex virus-1 encoded glycoprotein B diverts HLA-DR into the exosome pathway
    • Temme, S., Eis-Hubinger, A. M., McLellan, A. D. and Koch, N., The herpes simplex virus-1 encoded glycoprotein B diverts HLA-DR into the exosome pathway. J. Immunol. 2010. 184: 236–243.
    • (2010) J. Immunol. , vol.184 , pp. 236-243
    • Temme, S.1    Eis-Hubinger, A.M.2    McLellan, A.D.3    Koch, N.4
  • 70
    • 79960110441 scopus 로고    scopus 로고
    • Infection of dendritic cells with herpes simplex virus type 1 induces rapid degradation of CYTIP, thereby modulating adhesion and migration
    • Theodoridis, A. A., Eich, C., Figdor, C. G. and Steinkasserer, A., Infection of dendritic cells with herpes simplex virus type 1 induces rapid degradation of CYTIP, thereby modulating adhesion and migration. Blood 2011. 118: 107–115.
    • (2011) Blood , vol.118 , pp. 107-115
    • Theodoridis, A.A.1    Eich, C.2    Figdor, C.G.3    Steinkasserer, A.4
  • 71
    • 81455135819 scopus 로고    scopus 로고
    • Activation of autophagy by alpha-herpesviruses in myeloid cells is mediated by cytoplasmic viral DNA through a mechanism dependent on stimulator of IFN genes
    • Rasmussen, S. B., Horan, K. A., Holm, C. K., Stranks, A. J., Mettenleiter, T. C., Simon, A. K., Jensen, S. B. et al., Activation of autophagy by alpha-herpesviruses in myeloid cells is mediated by cytoplasmic viral DNA through a mechanism dependent on stimulator of IFN genes. J. Immunol. 2011. 187: 5268–5276.
    • (2011) J. Immunol. , vol.187 , pp. 5268-5276
    • Rasmussen, S.B.1    Horan, K.A.2    Holm, C.K.3    Stranks, A.J.4    Mettenleiter, T.C.5    Simon, A.K.6    Jensen, S.B.7
  • 72
    • 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., Ma, Y., Prabhakar, B. S., Feng, Z., Valyi-Nagy, T., Yan, Z., Verpooten, D. et al., The gamma 1 34.5 protein of herpes simplex virus 1 is required to interfere with dendritic cell maturation during productive infection. J. Virol. 2009. 83: 4984–4994.
    • (2009) J. Virol. , vol.83 , pp. 4984-4994
    • Jin, H.1    Ma, Y.2    Prabhakar, B.S.3    Feng, Z.4    Valyi-Nagy, T.5    Yan, Z.6    Verpooten, D.7
  • 73
    • 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. and He, B., A herpesvirus virulence factor inhibits dendritic cell maturation through protein phosphatase 1 and Ikappa B kinase. J. Virol. 2011. 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
  • 74
    • 64749117051 scopus 로고    scopus 로고
    • Differential migration of epidermal and dermal dendritic cells during skin infection
    • Eidsmo, L., Allan, R., Caminschi, I., van Rooijen, N., Heath, W. R. and Carbone, F. R., Differential migration of epidermal and dermal dendritic cells during skin infection. J. Immunol. 2009. 182: 3165–3172.
    • (2009) J. Immunol. , vol.182 , pp. 3165-3172
    • Eidsmo, L.1    Allan, R.2    Caminschi, I.3    van Rooijen, N.4    Heath, W.R.5    Carbone, F.R.6
  • 75
    • 0036219008 scopus 로고    scopus 로고
    • Characterization of two TCR transgenic mouse lines specific for herpes simplex virus
    • Mueller, S. N., Heath, W., McLain, J. D., Carbone, F. R. and Jones, C. M., Characterization of two TCR transgenic mouse lines specific for herpes simplex virus. Immunol. Cell Biol. 2002. 80: 156–163.
    • (2002) Immunol. Cell Biol. , vol.80 , pp. 156-163
    • Mueller, S.N.1    Heath, W.2    McLain, J.D.3    Carbone, F.R.4    Jones, C.M.5
  • 76
    • 75749122303 scopus 로고    scopus 로고
    • Methods in mammalian autophagy research
    • Mizushima, N., Yoshimori, T. and Levine, B., Methods in mammalian autophagy research. Cell 2010. 140: 313–326.
    • (2010) Cell , vol.140 , pp. 313-326
    • Mizushima, N.1    Yoshimori, T.2    Levine, B.3
  • 78
    • 84866560614 scopus 로고    scopus 로고
    • A novel image-based cytometry method for autophagy detection in living cells
    • Chan, L. L., Shen, D., Wilkinson, A. R., Patton, W., Lai, N., Chan, E., Kuksin, D. et al., A novel image-based cytometry method for autophagy detection in living cells. Autophagy 2012. 8: 1371–1382.
    • (2012) Autophagy , vol.8 , pp. 1371-1382
    • Chan, L.L.1    Shen, D.2    Wilkinson, A.R.3    Patton, W.4    Lai, N.5    Chan, E.6    Kuksin, D.7
  • 80
    • 0028236443 scopus 로고
    • Glycoprotein C-independent binding of herpes simplex virus to cells requires cell surface heparan sulphate and glycoprotein B
    • Herold, B. C., Visalli, R. J., Susmarski, N., Brandt, C. R. and Spear, P. G., Glycoprotein C-independent binding of herpes simplex virus to cells requires cell surface heparan sulphate and glycoprotein B. J. Gen. Virol. 1994. 75 (Pt 6): 1211–1222.
    • (1994) J. Gen. Virol. , vol.75 , pp. 1211-1222
    • Herold, B.C.1    Visalli, R.J.2    Susmarski, N.3    Brandt, C.R.4    Spear, P.G.5
  • 81
    • 0030793170 scopus 로고    scopus 로고
    • Suppression of the phenotype of gamma(1)34.5- herpes simplex virus 1: failure of activated RNA-dependent protein kinase to shut off protein synthesis is associated with a deletion in the domain of the alpha47 gene
    • He, B., Chou, J., Brandimarti, R., Mohr, I., Gluzman, Y. and Roizman, B., Suppression of the phenotype of gamma(1)34.5- herpes simplex virus 1: failure of activated RNA-dependent protein kinase to shut off protein synthesis is associated with a deletion in the domain of the alpha47 gene. J. Virol. 1997. 71: 6049–6054.
    • (1997) J. Virol. , vol.71 , pp. 6049-6054
    • He, B.1    Chou, J.2    Brandimarti, R.3    Mohr, I.4    Gluzman, Y.5    Roizman, B.6
  • 82
    • 84863006955 scopus 로고    scopus 로고
    • Herpes simplex virus type I induces an incomplete autophagic response in human neuroblastoma cells
    • Santana, S., Bullido, M. J., Recuero, M., Valdivieso, F. and Aldudo, J., Herpes simplex virus type I induces an incomplete autophagic response in human neuroblastoma cells. J. Alzheimers Dis. 2012. 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
  • 83
    • 84929494305 scopus 로고    scopus 로고
    • Viral inhibition of the transporter associated with antigen processing (TAP): a striking example of functional convergent evolution
    • Verweij, M. C., Horst, D., Griffin, B. D., Luteijn, R. D., Davison, A. J., Ressing, M. E. and Wiertz, E. J., Viral inhibition of the transporter associated with antigen processing (TAP): a striking example of functional convergent evolution. PLoS Pathog. 2015. 11: e1004743.
    • (2015) PLoS Pathog. , vol.11
    • Verweij, M.C.1    Horst, D.2    Griffin, B.D.3    Luteijn, R.D.4    Davison, A.J.5    Ressing, M.E.6    Wiertz, E.J.7
  • 84
    • 84864535321 scopus 로고    scopus 로고
    • Autophagy mediates transporter associated with antigen processing-independent presentation of viral epitopes through MHC class I pathway
    • Tey, S. K. and Khanna, R., Autophagy mediates transporter associated with antigen processing-independent presentation of viral epitopes through MHC class I pathway. Blood 2012. 120: 994–1004.
    • (2012) Blood , vol.120 , pp. 994-1004
    • Tey, S.K.1    Khanna, R.2
  • 85
    • 84975490489 scopus 로고    scopus 로고
    • Autophagy proteins in antigen processing for presentation on MHC molecules
    • Munz, C., Autophagy proteins in antigen processing for presentation on MHC molecules. Immunol. Rev. 2016. 272: 17–27.
    • (2016) Immunol. Rev. , vol.272 , pp. 17-27
    • Munz, C.1
  • 86
    • 0032871905 scopus 로고    scopus 로고
    • Inhibition of dendritic cell maturation by herpes simplex virus
    • Salio, M., Cella, M., Suter, M. and Lanzavecchia, A., Inhibition of dendritic cell maturation by herpes simplex virus. Eur. J. Immunol. 1999. 29: 3245–3253.
    • (1999) Eur. J. Immunol. , vol.29 , pp. 3245-3253
    • Salio, M.1    Cella, M.2    Suter, M.3    Lanzavecchia, A.4
  • 87
    • 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. and Roizman, B., 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. 2002. 76: 6974–6986.
    • (2002) J. Virol. , vol.76 , pp. 6974-6986
    • Trgovcich, J.1    Johnson, D.2    Roizman, B.3
  • 88
    • 84857195479 scopus 로고    scopus 로고
    • Activation of autophagy by inflammatory signals limits IL-1beta production by targeting ubiquitinated inflammasomes for destruction
    • Shi, C. S., Shenderov, K., Huang, N. N., Kabat, J., Abu-Asab, M., Fitzgerald, K. A., Sher, A. et al., Activation of autophagy by inflammatory signals limits IL-1beta production by targeting ubiquitinated inflammasomes for destruction. Nat. Immunol. 2012. 13: 255–263.
    • (2012) Nat. Immunol. , vol.13 , pp. 255-263
    • Shi, C.S.1    Shenderov, K.2    Huang, N.N.3    Kabat, J.4    Abu-Asab, M.5    Fitzgerald, K.A.6    Sher, A.7
  • 89
    • 0030792648 scopus 로고    scopus 로고
    • Evidence for cooperation between TCR V region and junctional sequences in determining a dominant cytotoxic T lymphocyte response to herpes simplex virus glycoprotein B
    • Jones, C. M., Cose, S. C. and Carbone, F. R., Evidence for cooperation between TCR V region and junctional sequences in determining a dominant cytotoxic T lymphocyte response to herpes simplex virus glycoprotein B. Int. Immunol. 1997. 9: 1319–1328.
    • (1997) Int. Immunol. , vol.9 , pp. 1319-1328
    • Jones, C.M.1    Cose, S.C.2    Carbone, F.R.3
  • 90
    • 0026691899 scopus 로고
    • The surface phenotype of dendritic cells purified from mouse thymus and spleen: investigation of the CD8 expression by a subpopulation of dendritic cells
    • Vremec, D., Zorbas, M., Scollay, R., Saunders, D. J., Ardavin, C. F., Wu, L. and Shortman, K., The surface phenotype of dendritic cells purified from mouse thymus and spleen: investigation of the CD8 expression by a subpopulation of dendritic cells. J. Exp. Med. 1992. 176: 47–58.
    • (1992) J. Exp. Med. , vol.176 , pp. 47-58
    • Vremec, D.1    Zorbas, M.2    Scollay, R.3    Saunders, D.J.4    Ardavin, C.F.5    Wu, L.6    Shortman, K.7
  • 91
    • 84877904363 scopus 로고    scopus 로고
    • A herpes simplex virus-derived replicative vector expressing LIF limits experimental demyelinating disease and modulates autoimmunity
    • Nygardas, M., Paavilainen, H., Muther, N., Nagel, C. H., Roytta, M., Sodeik, B. and Hukkanen, V., A herpes simplex virus-derived replicative vector expressing LIF limits experimental demyelinating disease and modulates autoimmunity. PLoS One 2013. 8: e64200.
    • (2013) PLoS One , vol.8
    • Nygardas, M.1    Paavilainen, H.2    Muther, N.3    Nagel, C.H.4    Roytta, M.5    Sodeik, B.6    Hukkanen, V.7
  • 92
    • 84872620818 scopus 로고    scopus 로고
    • Cytosolic herpes simplex virus capsids not only require binding inner tegument protein pUL36 but also pUL37 for active transport prior to secondary envelopment
    • Sandbaumhuter, M., Dohner, K., Schipke, J., Binz, A., Pohlmann, A., Sodeik, B. and Bauerfeind, R., Cytosolic herpes simplex virus capsids not only require binding inner tegument protein pUL36 but also pUL37 for active transport prior to secondary envelopment. Cell Microbiol. 2013. 15: 248–269.
    • (2013) Cell Microbiol. , vol.15 , pp. 248-269
    • Sandbaumhuter, M.1    Dohner, K.2    Schipke, J.3    Binz, A.4    Pohlmann, A.5    Sodeik, B.6    Bauerfeind, R.7
  • 94
    • 33645053126 scopus 로고    scopus 로고
    • Two-step red-mediated recombination for versatile high-efficiency markerless DNA manipulation in Escherichia coli
    • Tischer, B. K., von Einem, J., Kaufer, B. and Osterrieder, N., Two-step red-mediated recombination for versatile high-efficiency markerless DNA manipulation in Escherichia coli. Biotechniques 2006. 40: 191–197.
    • (2006) Biotechniques , vol.40 , pp. 191-197
    • Tischer, B.K.1    von Einem, J.2    Kaufer, B.3    Osterrieder, N.4
  • 95
    • 84921300270 scopus 로고    scopus 로고
    • Construction and characterization of bacterial artificial chromosomes (BACs) containing herpes simplex virus full-length genomes
    • Nagel, C. H., Pohlmann, A. and Sodeik, B., Construction and characterization of bacterial artificial chromosomes (BACs) containing herpes simplex virus full-length genomes. Methods Mol. Biol. 2014. 1144: 43–62.
    • (2014) Methods Mol. Biol. , vol.1144 , pp. 43-62
    • Nagel, C.H.1    Pohlmann, A.2    Sodeik, B.3
  • 96
    • 0030896925 scopus 로고    scopus 로고
    • Microtubule-mediated transport of incoming herpes simplex virus 1 capsids to the nucleus
    • Sodeik, B., Ebersold, M. W. and Helenius, A., Microtubule-mediated transport of incoming herpes simplex virus 1 capsids to the nucleus. J. Cell Biol. 1997. 136: 1007–1021.
    • (1997) J. Cell Biol. , vol.136 , pp. 1007-1021
    • Sodeik, B.1    Ebersold, M.W.2    Helenius, A.3
  • 97
    • 33746853425 scopus 로고    scopus 로고
    • Eclipse phase of herpes simplex virus type 1 infection: efficient dynein-mediated capsid transport without the small capsid protein VP26
    • Dohner, K., Radtke, K., Schmidt, S. and Sodeik, B., Eclipse phase of herpes simplex virus type 1 infection: efficient dynein-mediated capsid transport without the small capsid protein VP26. J. Virol. 2006. 80: 8211–8224.
    • (2006) J. Virol. , vol.80 , pp. 8211-8224
    • Dohner, K.1    Radtke, K.2    Schmidt, S.3    Sodeik, B.4
  • 98
    • 24644432375 scopus 로고    scopus 로고
    • Herpes simplex virus glycoprotein B binds to cell surfaces independently of heparan sulfate and blocks virus entry
    • Bender, F. C., Whitbeck, J. C., Lou, H., Cohen, G. H. and Eisenberg, R. J., Herpes simplex virus glycoprotein B binds to cell surfaces independently of heparan sulfate and blocks virus entry. J. Virol. 2005. 79: 11588–11597.
    • (2005) J. Virol. , vol.79 , pp. 11588-11597
    • Bender, F.C.1    Whitbeck, J.C.2    Lou, H.3    Cohen, G.H.4    Eisenberg, R.J.5
  • 100
    • 0020364438 scopus 로고
    • Monoclonal antibodies to three non-glycosylated antigens of herpes simplex virus type 2
    • McLean, C., Buckmaster, A., Hancock, D., Buchan, A., Fuller, A. and Minson, A., Monoclonal antibodies to three non-glycosylated antigens of herpes simplex virus type 2. J. Gen. Virol. 1982. 63: 297–305.
    • (1982) J. Gen. Virol. , vol.63 , pp. 297-305
    • McLean, C.1    Buckmaster, A.2    Hancock, D.3    Buchan, A.4    Fuller, A.5    Minson, A.6
  • 101
    • 0036720419 scopus 로고    scopus 로고
    • Signals that dictate nuclear, nucleolar, and cytoplasmic shuttling of the gamma(1)34.5 protein of herpes simplex virus type 1
    • Cheng, G., Brett, M. E. and He, B., Signals that dictate nuclear, nucleolar, and cytoplasmic shuttling of the gamma(1)34.5 protein of herpes simplex virus type 1. J. Virol. 2002. 76: 9434–9445.
    • (2002) J. Virol. , vol.76 , pp. 9434-9445
    • Cheng, G.1    Brett, M.E.2    He, B.3
  • 103
    • 84867746835 scopus 로고    scopus 로고
    • Autophagy inhibition due to thymidine analogues as novel mechanism leading to hepatocyte dysfunction and lipid accumulation
    • Stankov, M. V., Panayotova-Dimitrova, D., Leverkus, M., Vondran, F. W., Bauerfeind, R., Binz, A. and Behrens, G. M., Autophagy inhibition due to thymidine analogues as novel mechanism leading to hepatocyte dysfunction and lipid accumulation. AIDS 2012. 26: 1995–2006.
    • (2012) AIDS , vol.26 , pp. 1995-2006
    • Stankov, M.V.1    Panayotova-Dimitrova, D.2    Leverkus, M.3    Vondran, F.W.4    Bauerfeind, R.5    Binz, A.6    Behrens, G.M.7


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