메뉴 건너뛰기




Volumn 214, Issue 5, 2016, Pages 619-635

An siRNA screen for ATG protein depletion reveals the extent of the unconventional functions of the autophagy proteome in virus replication

(16)  Mauthe, Mario a,b   Langereis, Martijn c,k   Jung, Jennifer d   Zhou, Xingdong a,e   Jones, Alex a,b   Omta, Wienand b   Tooze, Sharon A f   Stork, Björn g   Paludan, Søren Riis h   Ahola, Tero i   Egan, Dave b   Behrends, Christian d   Mokry, Michal b,j   de Haan, Cornelis c   van Kuppeveld, Frank c   Reggiori, Fulvio a,b  


Author keywords

[No Author keywords available]

Indexed keywords

ATG13 PROTEIN; AUTOPHAGY RELATED PROTEIN; CELL PROTEIN; FIP200 PROTEIN; PROTEOME; SMALL INTERFERING RNA; ULK PROTEIN; UNCLASSIFIED DRUG; INTERFERON; PROTEIN TYROSINE KINASE; RB1CC1 PROTEIN, HUMAN;

EID: 84990821978     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201602046     Document Type: Article
Times cited : (52)

References (96)
  • 1
    • 84858390120 scopus 로고    scopus 로고
    • Pancreatic acinar cell-specific autophagy disruption reduces coxsackievirus replication and pathogenesis in vivo
    • Alirezaei, M., C.T. Flynn, M.R. Wood, and J.L. Whitton. 2012. Pancreatic acinar cell-specific autophagy disruption reduces coxsackievirus replication and pathogenesis in vivo. Cell Host Microbe. 11:298-305. http://dx.doi.org/10.1016/j.chom.2012.01.014
    • (2012) Cell Host Microbe , vol.11 , pp. 298-305
    • Alirezaei, M.1    Flynn, C.T.2    Wood, M.R.3    Whitton, J.L.4
  • 2
    • 84943782367 scopus 로고    scopus 로고
    • Coxsackievirus can exploit LC3 in both autophagy-dependent and-independent manners in vivo
    • Alirezaei, M., C.T. Flynn, M.R. Wood, S. Harkins, and J.L. Whitton. 2015. Coxsackievirus can exploit LC3 in both autophagy-dependent and-independent manners in vivo. Autophagy. 11:1389-1407. http://dx.doi.org/10.1080/15548627.2015.1063769
    • (2015) Autophagy , vol.11 , pp. 1389-1407
    • Alirezaei, M.1    Flynn, C.T.2    Wood, M.R.3    Harkins, S.4    Whitton, J.L.5
  • 3
    • 84928987900 scopus 로고    scopus 로고
    • HTSeq-a Python framework to work with high-throughput sequencing data
    • Anders, S., P.T. Pyl, and W. Huber. 2015. HTSeq-a Python framework to work with high-throughput sequencing data. Bioinformatics. 31:166-169. http://dx.doi.org/10.1093/bioinformatics/btu638
    • (2015) Bioinformatics , vol.31 , pp. 166-169
    • Anders, S.1    Pyl, P.T.2    Huber, W.3
  • 4
    • 50249084987 scopus 로고    scopus 로고
    • Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum
    • Axe, E.L., S.A. Walker, M. Manifava, P. Chandra, H.L. Roderick, A. Habermann, G. Griffiths, and N.T. Ktistakis. 2008. Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum. J. Cell Biol. 182:685-701. http://dx.doi.org/10.1083/jcb.200803137
    • (2008) J. Cell Biol , vol.182 , pp. 685-701
    • Axe, E.L.1    Walker, S.A.2    Manifava, M.3    Chandra, P.4    Roderick, H.L.5    Habermann, A.6    Griffiths, G.7    Ktistakis, N.T.8
  • 5
    • 84901931429 scopus 로고    scopus 로고
    • High-throughput functional screening using a homemade dual-glow luciferase assay
    • Baker, J.M., and F.M. Boyce. 2014. High-throughput functional screening using a homemade dual-glow luciferase assay. J. Vis. Exp. 88:50282. http://dx.doi.org/10.3791/50282
    • (2014) J. Vis. Exp , vol.88 , pp. 50282
    • Baker, J.M.1    Boyce, F.M.2
  • 6
    • 0020356798 scopus 로고
    • In vitro copying of viral positive strand RNA by poliovirus replicase. Characterization of the reaction and its products
    • Baron, M.H., and D. Baltimore. 1982. In vitro copying of viral positive strand RNA by poliovirus replicase. Characterization of the reaction and its products. J. Biol. Chem. 257:12359-12366.
    • (1982) J. Biol. Chem , vol.257 , pp. 12359-12366
    • Baron, M.H.1    Baltimore, D.2
  • 7
    • 77954237882 scopus 로고    scopus 로고
    • Network organization of the human autophagy system
    • Behrends, C., M.E. Sowa, S.P. Gygi, and J.W. Harper. 2010. Network organization of the human autophagy system. Nature. 466:68-76. http://dx.doi.org/10.1038/nature09204
    • (2010) Nature , vol.466 , pp. 68-76
    • Behrends, C.1    Sowa, M.E.2    Gygi, S.P.3    Harper, J.W.4
  • 8
    • 84883655855 scopus 로고    scopus 로고
    • Hidden behind autophagy: the unconventional roles of ATG proteins
    • Bestebroer, J., P. V'kovski, M. Mauthe, and F. Reggiori. 2013. Hidden behind autophagy: the unconventional roles of ATG proteins. Traffic. 14:1029-1041. http://dx.doi.org/10.1111/tra.12091
    • (2013) Traffic , vol.14 , pp. 1029-1041
    • Bestebroer, J.1    V'kovski, P.2    Mauthe, M.3    Reggiori, F.4
  • 9
    • 36349017113 scopus 로고    scopus 로고
    • Genetic evolution of enterovirus 71: epidemiological and pathological implications
    • Bible, J.M., P. Pantelidis, P.K. Chan, and C.Y. Tong. 2007. Genetic evolution of enterovirus 71: epidemiological and pathological implications. Rev. Med. Virol. 17:371-379. http://dx.doi.org/10.1002/rmv.538
    • (2007) Rev. Med. Virol , vol.17 , pp. 371-379
    • Bible, J.M.1    Pantelidis, P.2    Chan, P.K.3    Tong, C.Y.4
  • 10
    • 8044257699 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-kinase inhibitors wortmannin and LY294002 inhibit autophagy in isolated rat hepatocytes
    • Blommaart, E.F., U. Krause, J.P. Schellens, H. Vreeling-Sindelárová, and A.J. Meijer. 1997. The phosphatidylinositol 3-kinase inhibitors wortmannin and LY294002 inhibit autophagy in isolated rat hepatocytes. Eur. J. Biochem. 243:240-246. http://dx.doi.org/10.1111/j.1432-1033.1997.0240a.x
    • (1997) Eur. J. Biochem , vol.243 , pp. 240-246
    • Blommaart, E.F.1    Krause, U.2    Schellens, J.P.3    Vreeling-Sindelárová, H.4    Meijer, A.J.5
  • 11
    • 84920374896 scopus 로고    scopus 로고
    • Autophagic flux without a block differentiates varicellazoster virus infection from herpes simplex virus infection
    • Buckingham, E.M., J.E. Carpenter, W. Jackson, L. Zerboni, A.M. Arvin, and C. Grose. 2015. Autophagic flux without a block differentiates varicellazoster virus infection from herpes simplex virus infection. Proc. Natl. Acad. Sci. USA. 112:256-261. http://dx.doi.org/10.1073/pnas.1417878112
    • (2015) Proc. Natl. Acad. Sci. USA , vol.112 , pp. 256-261
    • Buckingham, E.M.1    Carpenter, J.E.2    Jackson, W.3    Zerboni, L.4    Arvin, A.M.5    Grose, C.6
  • 12
    • 84912120721 scopus 로고    scopus 로고
    • Coronavirus cell entry occurs through the endo-/lysosomal pathway in a proteolysis-dependent manner
    • (published erratum appears in PLoS Pathog. 2015. 11:e1004709)
    • Burkard, C., M.H. Verheije, O. Wicht, S.I. van Kasteren, F.J. van Kuppeveld, B.L. Haagmans, L. Pelkmans, P.J. Rottier, B.J. Bosch, and C.A. de Haan. 2014. Coronavirus cell entry occurs through the endo-/lysosomal pathway in a proteolysis-dependent manner. PLoS Pathog. 10:e1004502. (published erratum appears in PLoS Pathog. 2015. 11:e1004709) http://dx.doi.org/10.1371/journal.ppat.1004502
    • (2014) PLoS Pathog , vol.10
    • Burkard, C.1    Verheije, M.H.2    Wicht, O.3    van Kasteren, S.I.4    van Kuppeveld, F.J.5    Haagmans, B.L.6    Pelkmans, L.7    Rottier, P.J.8    Bosch, B.J.9    de Haan, C.A.10
  • 13
    • 84869057548 scopus 로고    scopus 로고
    • RNase L triggers autophagy in response to viral infections
    • Chakrabarti, A., P.K. Ghosh, S. Banerjee, C. Gaughan, and R.H. Silverman. 2012. RNase L triggers autophagy in response to viral infections. J. Virol. 86:11311-11321. http://dx.doi.org/10.1128/JVI.00270-12
    • (2012) J. Virol , vol.86 , pp. 11311-11321
    • Chakrabarti, A.1    Ghosh, P.K.2    Banerjee, S.3    Gaughan, C.4    Silverman, R.H.5
  • 14
    • 34548482499 scopus 로고    scopus 로고
    • siRNA screening of the kinome identifies ULK1 as a multidomain modulator of autophagy
    • Chan, E.Y., S. Kir, and S.A. Tooze. 2007. siRNA screening of the kinome identifies ULK1 as a multidomain modulator of autophagy. J. Biol. Chem. 282:25464-25474. http://dx.doi.org/10.1074/jbc.M703663200
    • (2007) J. Biol. Chem , vol.282 , pp. 25464-25474
    • Chan, E.Y.1    Kir, S.2    Tooze, S.A.3
  • 15
    • 84962476246 scopus 로고    scopus 로고
    • Distinct roles of autophagy-dependent and-independent functions of FIP200 revealed by generation and analysis of a mutant knock-in mouse model
    • Chen, S., C. Wang, S. Yeo, C.C. Liang, T. Okamoto, S. Sun, J. Wen, and J.L. Guan. 2016. Distinct roles of autophagy-dependent and-independent functions of FIP200 revealed by generation and analysis of a mutant knock-in mouse model. Genes Dev. 30:856-869. http://dx.doi.org/10.1101/gad.276428.115
    • (2016) Genes Dev , vol.30 , pp. 856-869
    • Chen, S.1    Wang, C.2    Yeo, S.3    Liang, C.C.4    Okamoto, T.5    Sun, S.6    Wen, J.7    Guan, J.L.8
  • 16
    • 0142124183 scopus 로고    scopus 로고
    • Coronaviruses as vectors: position dependence of foreign gene expression
    • de Haan, C.A., L. van Genne, J.N. Stoop, H. Volders, and P.J. Rottier. 2003. Coronaviruses as vectors: position dependence of foreign gene expression. J. Virol. 77:11312-11323. http://dx.doi.org/10.1128/JVI.77.21.11312-11323.2003
    • (2003) J. Virol , vol.77 , pp. 11312-11323
    • de Haan, C.A.1    van Genne, L.2    Stoop, J.N.3    Volders, H.4    Rottier, P.J.5
  • 17
    • 84920901634 scopus 로고    scopus 로고
    • BPI FB3 regulates autophagy and coxsackievirus B replication through a noncanonical pathway independent of the core initiation machinery
    • Delorme-Axford, E., S. Morosky, J. Bomberger, D.B. Stolz, W.T. Jackson, and C.B. Coyne. 2014. BPI FB3 regulates autophagy and coxsackievirus B replication through a noncanonical pathway independent of the core initiation machinery. MBio. 5:e02147. http://dx.doi.org/10.1128/mBio.02147-14
    • (2014) MBio , vol.5
    • Delorme-Axford, E.1    Morosky, S.2    Bomberger, J.3    Stolz, D.B.4    Jackson, W.T.5    Coyne, C.B.6
  • 18
    • 53649106470 scopus 로고    scopus 로고
    • Selective inhibitors of picornavirus replication
    • De Palma, A.M., I. Vliegen, E. De Clercq, and J. Neyts. 2008. Selective inhibitors of picornavirus replication. Med. Res. Rev. 28:823-884. http://dx.doi.org/10.1002/med.20125
    • (2008) Med. Res. Rev , vol.28 , pp. 823-884
    • De Palma, A.M.1    Vliegen, I.2    De Clercq, E.3    Neyts, J.4
  • 20
    • 84943576637 scopus 로고    scopus 로고
    • Modulation of the host lipid landscape to promote RNA virus replication: the picornavirus encephalomyocarditis virus converges on the pathway used by hepatitis C virus
    • Dorobantu, C.M., L. Albulescu, C. Harak, Q. Feng, M. van Kampen, J.R. Strating, A.E. Gorbalenya, V. Lohmann, H.M. van der Schaar, and F.J. van Kuppeveld. 2015. Modulation of the host lipid landscape to promote RNA virus replication: the picornavirus encephalomyocarditis virus converges on the pathway used by hepatitis C virus. PLoS Pathog. 11:e1005185. http://dx.doi.org/10.1371/journal.ppat.1005185
    • (2015) PLoS Pathog , vol.11
    • Dorobantu, C.M.1    Albulescu, L.2    Harak, C.3    Feng, Q.4    van Kampen, M.5    Strating, J.R.6    Gorbalenya, A.E.7    Lohmann, V.8    van der Schaar, H.M.9    van Kuppeveld, F.J.10
  • 21
    • 84861307200 scopus 로고    scopus 로고
    • Accumulation of autophagosomes in Semliki Forest virus-infected cells is dependent on expression of the viral glycoproteins
    • Eng, K.E., M.D. Panas, D. Murphy, G.B. Karlsson Hedestam, and G.M. McInerney. 2012. Accumulation of autophagosomes in Semliki Forest virus-infected cells is dependent on expression of the viral glycoproteins. J. Virol. 86:5674-5685. http://dx.doi.org/10.1128/JVI.06581-11
    • (2012) J. Virol , vol.86 , pp. 5674-5685
    • Eng, K.E.1    Panas, M.D.2    Murphy, D.3    Karlsson Hedestam, G.B.4    McInerney, G.M.5
  • 22
    • 84892840296 scopus 로고    scopus 로고
    • An essential role for heat shock transcription factor binding protein 1 (HSBP1) during early embryonic development
    • Eroglu, B., J.N. Min, Y. Zhang, E. Szurek, D. Moskophidis, A. Eroglu, and N.F. Mivechi. 2014. An essential role for heat shock transcription factor binding protein 1 (HSBP1) during early embryonic development. Dev. Biol. 386:448-460. http://dx.doi.org/10.1016/j.ydbio.2013.12.038
    • (2014) Dev. Biol , vol.386 , pp. 448-460
    • Eroglu, B.1    Min, J.N.2    Zhang, Y.3    Szurek, E.4    Moskophidis, D.5    Eroglu, A.6    Mivechi, N.F.7
  • 23
    • 84946562067 scopus 로고    scopus 로고
    • Enterovirus 71 induces autophagy by regulating has-miR-30a expression to promote viral replication
    • Fu, Y., W. Xu, D. Chen, C. Feng, L. Zhang, X. Wang, X. Lv, N. Zheng, Y. Jin, and Z. Wu. 2015. Enterovirus 71 induces autophagy by regulating has-miR-30a expression to promote viral replication. Antiviral Res. 124:43-53. http://dx.doi.org/10.1016/j.antiviral.2015.09.016
    • (2015) Antiviral Res , vol.124 , pp. 43-53
    • Fu, Y.1    Xu, W.2    Chen, D.3    Feng, C.4    Zhang, L.5    Wang, X.6    Lv, X.7    Zheng, N.8    Jin, Y.9    Wu, Z.10
  • 24
    • 0032169169 scopus 로고    scopus 로고
    • The role of low pH and disulfide shuffling in the entry and fusion of Semliki Forest virus and Sindbis virus
    • Glomb-Reinmund, S., and M. Kielian. 1998. The role of low pH and disulfide shuffling in the entry and fusion of Semliki Forest virus and Sindbis virus. Virology. 248:372-381. http://dx.doi.org/10.1006/viro.1998.9275
    • (1998) Virology , vol.248 , pp. 372-381
    • Glomb-Reinmund, S.1    Kielian, M.2
  • 25
    • 43149090064 scopus 로고    scopus 로고
    • FIP200, a ULK-interacting protein, is required for autophagosome formation in mammalian cells
    • Hara, T., A. Takamura, C. Kishi, S. Iemura, T. Natsume, J.L. Guan, and N. Mizushima. 2008. FIP200, a ULK-interacting protein, is required for autophagosome formation in mammalian cells. J. Cell Biol. 181:497-510. http://dx.doi.org/10.1083/jcb.200712064
    • (2008) J. Cell Biol , vol.181 , pp. 497-510
    • Hara, T.1    Takamura, A.2    Kishi, C.3    Iemura, S.4    Natsume, T.5    Guan, J.L.6    Mizushima, N.7
  • 26
    • 35948982216 scopus 로고    scopus 로고
    • The mengovirus leader protein blocks interferon-alpha/beta gene transcription and inhibits activation of interferon regulatory factor 3
    • Hato, S.V., C. Ricour, B.M. Schulte, K.H. Lanke, M. de Bruijni, J. Zoll, W.J. Melchers, T. Michiels, and F.J. van Kuppeveld. 2007. The mengovirus leader protein blocks interferon-alpha/beta gene transcription and inhibits activation of interferon regulatory factor 3. Cell. Microbiol. 9:2921-2930. http://dx.doi.org/10.1111/j.1462-5822.2007.01006.x
    • (2007) Cell. Microbiol , vol.9 , pp. 2921-2930
    • Hato, S.V.1    Ricour, C.2    Schulte, B.M.3    Lanke, K.H.4    de Bruijni, M.5    Zoll, J.6    Melchers, W.J.7    Michiels, T.8    van Kuppeveld, F.J.9
  • 27
    • 72549095406 scopus 로고    scopus 로고
    • Regulation mechanisms and signaling pathways of autophagy
    • He, C., and D.J. Klionsky. 2009. Regulation mechanisms and signaling pathways of autophagy. Annu. Rev. Genet. 43:67-93. http://dx.doi.org/10.1146/annurev-genet-102808-114910
    • (2009) Annu. Rev. Genet , vol.43 , pp. 67-93
    • He, C.1    Klionsky, D.J.2
  • 28
    • 84947590219 scopus 로고    scopus 로고
    • Expression of a ULK1/2 binding-deficient ATG13 variant can partially restore autophagic activity in ATG13-deficient cells
    • Hieke, N., A.S. Löffler, T. Kaizuka, N. Berleth, P. Böhler, S. Drießen, F. Stuhldreier, O. Friesen, K. Assani, K. Schmitz, et al. 2015. Expression of a ULK1/2 binding-deficient ATG13 variant can partially restore autophagic activity in ATG13-deficient cells. Autophagy. 11:1471-1483. http://dx.doi.org/10.1080/15548627.2015.1068488
    • (2015) Autophagy , vol.11 , pp. 1471-1483
    • Hieke, N.1    Löffler, A.S.2    Kaizuka, T.3    Berleth, N.4    Böhler, P.5    Drießen, S.6    Stuhldreier, F.7    Friesen, O.8    Assani, K.9    Schmitz, K.10
  • 29
    • 70349644856 scopus 로고    scopus 로고
    • Atg101, a novel mammalian autophagy protein interacting with Atg13
    • Hosokawa, N., T. Sasaki, S. Iemura, T. Natsume, T. Hara, and N. Mizushima. 2009. Atg101, a novel mammalian autophagy protein interacting with Atg13. Autophagy. 5:973-979. http://dx.doi.org/10.4161/auto.5.7.9296
    • (2009) Autophagy , vol.5 , pp. 973-979
    • Hosokawa, N.1    Sasaki, T.2    Iemura, S.3    Natsume, T.4    Hara, T.5    Mizushima, N.6
  • 30
    • 67649989068 scopus 로고    scopus 로고
    • Enterovirus 71-induced autophagy detected in vitro and in vivo promotes viral replication
    • Huang, S.C., C.L. Chang, P.S. Wang, Y. Tsai, and H.S. Liu. 2009. Enterovirus 71-induced autophagy detected in vitro and in vivo promotes viral replication. J. Med. Virol. 81:1241-1252. http://dx.doi.org/10.1002/jmv.21502
    • (2009) J. Med. Virol , vol.81 , pp. 1241-1252
    • Huang, S.C.1    Chang, C.L.2    Wang, P.S.3    Tsai, Y.4    Liu, H.S.5
  • 33
    • 84969135882 scopus 로고    scopus 로고
    • The noncanonical role of ULK/ATG1 in ER-to-Golgi trafficking is essential for cellular homeostasis
    • Joo, J.H., B. Wang, E. Frankel, L. Ge, L. Xu, R. Iyengar, X. Li-Harms, C. Wright, T.I. Shaw, T. Lindsten, et al. 2016. The noncanonical role of ULK/ATG1 in ER-to-Golgi trafficking is essential for cellular homeostasis. Mol. Cell. 62:491-506. http://dx.doi.org/10.1016/j.molcel.2016.04.020
    • (2016) Mol. Cell , vol.62 , pp. 491-506
    • Joo, J.H.1    Wang, B.2    Frankel, E.3    Ge, L.4    Xu, L.5    Iyengar, R.6    Li-Harms, X.7    Wright, C.8    Shaw, T.I.9    Lindsten, T.10
  • 34
    • 65249176304 scopus 로고    scopus 로고
    • ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy machinery
    • Jung, C.H., C.B. Jun, S.H. Ro, Y.M. Kim, N.M. Otto, J. Cao, M. Kundu, and D.H. Kim. 2009. ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy machinery. Mol. Biol. Cell. 20:1992-2003. http://dx.doi.org/10.1091/mbc.E08-12-1249
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1992-2003
    • Jung, C.H.1    Jun, C.B.2    Ro, S.H.3    Kim, Y.M.4    Otto, N.M.5    Cao, J.6    Kundu, M.7    Kim, D.H.8
  • 35
    • 84932638310 scopus 로고    scopus 로고
    • Amino Acid-Dependent mTORC1 Regulation by the Lysosomal Membrane Protein SLC38A9
    • Jung, J., H.M. Genau, and C. Behrends. 2015. Amino Acid-Dependent mTORC1 Regulation by the Lysosomal Membrane Protein SLC38A9. Mol. Cell. Biol. 35:2479-2494. http://dx.doi.org/10.1128/MCB.00125-15
    • (2015) Mol. Cell. Biol , vol.35 , pp. 2479-2494
    • Jung, J.1    Genau, H.M.2    Behrends, C.3
  • 36
    • 84957900248 scopus 로고    scopus 로고
    • Atg13 is essential for autophagy and cardiac development in mice
    • Kaizuka, T., and N. Mizushima. 2015. Atg13 is essential for autophagy and cardiac development in mice. Mol. Cell. Biol. 36:585-595. http://dx.doi.org/10.1128/MCB.01005-15
    • (2015) Mol. Cell. Biol , vol.36 , pp. 585-595
    • Kaizuka, T.1    Mizushima, N.2
  • 37
    • 43149125546 scopus 로고    scopus 로고
    • Organization of the pre-autophagosomal structure responsible for autophagosome formation
    • Kawamata, T., Y. Kamada, Y. Kabeya, T. Sekito, and Y. Ohsumi. 2008. Organization of the pre-autophagosomal structure responsible for autophagosome formation. Mol. Biol. Cell. 19:2039-2050. http://dx.doi.org/10.1091/mbc.E07-10-1048
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2039-2050
    • Kawamata, T.1    Kamada, Y.2    Kabeya, Y.3    Sekito, T.4    Ohsumi, Y.5
  • 38
    • 78049513713 scopus 로고    scopus 로고
    • Coxsackievirus infection induces autophagy-like vesicles and megaphagosomes in pancreatic acinar cells in vivo
    • Kemball, C.C., M. Alirezaei, C.T. Flynn, M.R. Wood, S. Harkins, W.B. Kiosses, and J.L. Whitton. 2010. Coxsackievirus infection induces autophagy-like vesicles and megaphagosomes in pancreatic acinar cells in vivo. J. Virol. 84:12110-12124. http://dx.doi.org/10.1128/JVI.01417-10
    • (2010) J. Virol , vol.84 , pp. 12110-12124
    • Kemball, C.C.1    Alirezaei, M.2    Flynn, C.T.3    Wood, M.R.4    Harkins, S.5    Kiosses, W.B.6    Whitton, J.L.7
  • 39
    • 84926519013 scopus 로고    scopus 로고
    • HIS AT: a fast spliced aligner with low memory requirements
    • Kim, D., B. Langmead, and S.L. Salzberg. 2015. HIS AT: a fast spliced aligner with low memory requirements. Nat. Methods. 12:357-360. http://dx.doi.org/10.1038/nmeth.3317
    • (2015) Nat. Methods , vol.12 , pp. 357-360
    • Kim, D.1    Langmead, B.2    Salzberg, S.L.3
  • 40
    • 84951336143 scopus 로고    scopus 로고
    • Unique role for ATG5 in neutrophil-mediated immunopathology during M. tuberculosis infection
    • Kimmey, J.M., J.P. Huynh, L.A. Weiss, S. Park, A. Kambal, J. Debnath, H.W. Virgin, and C.L. Stallings. 2015. Unique role for ATG5 in neutrophil-mediated immunopathology during M. tuberculosis infection. Nature. 528:565-569. http://dx.doi.org/10.1038/nature16451
    • (2015) Nature , vol.528 , pp. 565-569
    • Kimmey, J.M.1    Huynh, J.P.2    Weiss, L.A.3    Park, S.4    Kambal, A.5    Debnath, J.6    Virgin, H.W.7    Stallings, C.L.8
  • 43
    • 78649338141 scopus 로고    scopus 로고
    • Autophagy and the integrated stress response
    • Kroemer, G., G. Mariño, and B. Levine. 2010. Autophagy and the integrated stress response. Mol. Cell. 40:280-293. http://dx.doi.org/10.1016/j.molcel.2010.09.023
    • (2010) Mol. Cell , vol.40 , pp. 280-293
    • Kroemer, G.1    Mariño, G.2    Levine, B.3
  • 44
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:680-685. http://dx.doi.org/10.1038/227680a0
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 45
    • 0030795068 scopus 로고    scopus 로고
    • Translational enhancement of mdm2 oncogene expression in human tumor cells containing a stabilized wild-type p53 protein
    • Landers, J.E., S.L. Cassel, and D.L. George. 1997. Translational enhancement of mdm2 oncogene expression in human tumor cells containing a stabilized wild-type p53 protein. Cancer Res. 57:3562-3568.
    • (1997) Cancer Res , vol.57 , pp. 3562-3568
    • Landers, J.E.1    Cassel, S.L.2    George, D.L.3
  • 46
    • 84878171308 scopus 로고    scopus 로고
    • MDA5 localizes to stress granules, but this localization is not required for the induction of type I interferon
    • Langereis, M.A., Q. Feng, and F.J. van Kuppeveld. 2013. MDA5 localizes to stress granules, but this localization is not required for the induction of type I interferon. J. Virol. 87:6314-6325. http://dx.doi.org/10.1128/JVI.03213-12
    • (2013) J. Virol , vol.87 , pp. 6314-6325
    • Langereis, M.A.1    Feng, Q.2    van Kuppeveld, F.J.3
  • 48
    • 84925884548 scopus 로고    scopus 로고
    • Enterovirus 71-induced autophagy increases viral replication and pathogenesis in a suckling mouse model
    • Lee, Y.R., P.S. Wang, J.R. Wang, and H.S. Liu. 2014. Enterovirus 71-induced autophagy increases viral replication and pathogenesis in a suckling mouse model. J. Biomed. Sci. 21:80. http://dx.doi.org/10.1186/s12929-014-0080-4
    • (2014) J. Biomed. Sci , vol.21 , pp. 80
    • Lee, Y.R.1    Wang, P.S.2    Wang, J.R.3    Liu, H.S.4
  • 49
    • 1842583789 scopus 로고    scopus 로고
    • Development by self-digestion: molecular mechanisms and biological functions of autophagy
    • Levine, B., and D.J. Klionsky. 2004. Development by self-digestion: molecular mechanisms and biological functions of autophagy. Dev. Cell. 6:463-477. http://dx.doi.org/10.1016/S1534-5807(04)00099-1
    • (2004) Dev. Cell , vol.6 , pp. 463-477
    • Levine, B.1    Klionsky, D.J.2
  • 50
    • 78751672975 scopus 로고    scopus 로고
    • Autophagy in immunity and inflammation
    • Levine, B., N. Mizushima, and H.W. Virgin. 2011. Autophagy in immunity and inflammation. Nature. 469:323-335. http://dx.doi.org/10.1038/nature09782
    • (2011) Nature , vol.469 , pp. 323-335
    • Levine, B.1    Mizushima, N.2    Virgin, H.W.3
  • 51
    • 84897081288 scopus 로고    scopus 로고
    • AUT OPH AGY-REL ATED11 plays a critical role in general autophagy-and senescence-induced mitophagy in Arabidopsis
    • Li, F., T. Chung, and R.D. Vierstra. 2014. AUT OPH AGY-REL ATED11 plays a critical role in general autophagy-and senescence-induced mitophagy in Arabidopsis. Plant Cell. 26:788-807. http://dx.doi.org/10.1105/tpc.113.120014
    • (2014) Plant Cell , vol.26 , pp. 788-807
    • Li, F.1    Chung, T.2    Vierstra, R.D.3
  • 53
    • 80455132064 scopus 로고    scopus 로고
    • The transformation of enterovirus replication structures: a three-dimensional study of single-and doublemembrane compartments
    • Limpens, R.W., H.M. van der Schaar, D. Kumar, A.J. Koster, E.J. Snijder, F.J. van Kuppeveld, and M. Bárcena. 2011. The transformation of enterovirus replication structures: a three-dimensional study of single-and doublemembrane compartments. MBio. 2:e00166-11. http://dx.doi.org/10.1128/mBio.00166-11
    • (2011) MBio , vol.2
    • Limpens, R.W.1    van der Schaar, H.M.2    Kumar, D.3    Koster, A.J.4    Snijder, E.J.5    van Kuppeveld, F.J.6    Bárcena, M.7
  • 54
    • 80051474094 scopus 로고    scopus 로고
    • The WD40 repeat PtdIns(3)P-binding protein EPG-6 regulates progression of omegasomes to autophagosomes
    • Lu, Q., P. Yang, X. Huang, W. Hu, B. Guo, F. Wu, L. Lin, A.L. Kovács, L. Yu, and H. Zhang. 2011. The WD40 repeat PtdIns(3)P-binding protein EPG-6 regulates progression of omegasomes to autophagosomes. Dev. Cell. 21:343-357. http://dx.doi.org/10.1016/j.devcel.2011.06.024
    • (2011) Dev. Cell , vol.21 , pp. 343-357
    • Lu, Q.1    Yang, P.2    Huang, X.3    Hu, W.4    Guo, B.5    Wu, F.6    Lin, L.7    Kovács, A.L.8    Yu, L.9    Zhang, H.10
  • 55
    • 84923359391 scopus 로고    scopus 로고
    • Loss of Atg12, but not Atg5, in pro-opiomelanocortin neurons exacerbates diet-induced obesity
    • Malhotra, R., J.P. Warne, E. Salas, A.W. Xu, and J. Debnath. 2015. Loss of Atg12, but not Atg5, in pro-opiomelanocortin neurons exacerbates diet-induced obesity. Autophagy. 11:145-154. http://dx.doi.org/10.1080/15548627.2014.998917
    • (2015) Autophagy , vol.11 , pp. 145-154
    • Malhotra, R.1    Warne, J.P.2    Salas, E.3    Xu, A.W.4    Debnath, J.5
  • 56
    • 82955193292 scopus 로고    scopus 로고
    • The puzzling origin of the autophagosomal membrane
    • Mari, M., S.A. Tooze, and F. Reggiori. 2011. The puzzling origin of the autophagosomal membrane. F1000 Biol. Rep. 3:25. http://dx.doi.org/10.3410/B3-25
    • (2011) F1000 Biol. Rep , vol.3 , pp. 25
    • Mari, M.1    Tooze, S.A.2    Reggiori, F.3
  • 57
    • 4344595626 scopus 로고    scopus 로고
    • Regulation and role of autophagy in mammalian cells
    • Meijer, A.J., and P. Codogno. 2004. Regulation and role of autophagy in mammalian cells. Int. J. Biochem. Cell Biol. 36:2445-2462. http://dx.doi.org/10.1016/j.biocel.2004.02.002
    • (2004) Int. J. Biochem. Cell Biol , vol.36 , pp. 2445-2462
    • Meijer, A.J.1    Codogno, P.2
  • 60
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • Mizushima, N., B. Levine, A.M. Cuervo, and D.J. Klionsky. 2008. Autophagy fights disease through cellular self-digestion. Nature. 451:1069-1075. http://dx.doi.org/10.1038/nature06639
    • (2008) Nature , vol.451 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 61
    • 82855170843 scopus 로고    scopus 로고
    • Vaccinia virus leads to ATG12-ATG3 conjugation and deficiency in autophagosome formation
    • Moloughney, J.G., C.E. Monken, H. Tao, H. Zhang, J.D. Thomas, E.C. Lattime, and S. Jin. 2011. Vaccinia virus leads to ATG12-ATG3 conjugation and deficiency in autophagosome formation. Autophagy. 7:1434-1447. http://dx.doi.org/10.4161/auto.7.12.17793
    • (2011) Autophagy , vol.7 , pp. 1434-1447
    • Moloughney, J.G.1    Monken, C.E.2    Tao, H.3    Zhang, H.4    Thomas, J.D.5    Lattime, E.C.6    Jin, S.7
  • 62
    • 84917706134 scopus 로고    scopus 로고
    • Tissue tropism, pathology and pathogenesis of enterovirus infection
    • Muehlenbachs, A., J. Bhatnagar, and S.R. Zaki. 2015. Tissue tropism, pathology and pathogenesis of enterovirus infection. J. Pathol. 235:217-228. http://dx.doi.org/10.1002/path.4438
    • (2015) J. Pathol , vol.235 , pp. 217-228
    • Muehlenbachs, A.1    Bhatnagar, J.2    Zaki, S.R.3
  • 63
    • 0016680603 scopus 로고
    • 5'-Terminal 7-methylguanosine in eukaryotic mRNA is required for translation
    • Muthukrishnan, S., G.W. Both, Y. Furuichi, and A.J. Shatkin. 1975. 5'-Terminal 7-methylguanosine in eukaryotic mRNA is required for translation. Nature. 255:33-37. http://dx.doi.org/10.1038/255033a0
    • (1975) Nature , vol.255 , pp. 33-37
    • Muthukrishnan, S.1    Both, G.W.2    Furuichi, Y.3    Shatkin, A.J.4
  • 64
    • 0029115399 scopus 로고
    • Inhibitory effect of bafilomycin A1, a specific inhibitor of vacuolartype proton pump, on the growth of influenza A and B viruses in MDCK cells
    • Ochiai, H., S. Sakai, T. Hirabayashi, Y. Shimizu, and K. Terasawa. 1995. Inhibitory effect of bafilomycin A1, a specific inhibitor of vacuolartype proton pump, on the growth of influenza A and B viruses in MDCK cells. Antiviral Res. 27:425-430. http://dx.doi.org/10.1016/0166-3542(95)00040-S
    • (1995) Antiviral Res , vol.27 , pp. 425-430
    • Ochiai, H.1    Sakai, S.2    Hirabayashi, T.3    Shimizu, Y.4    Terasawa, K.5
  • 65
    • 0023720048 scopus 로고
    • Internal initiation of translation of eukaryotic mRNA directed by a sequence derived from poliovirus RNA
    • Pelletier, J., and N. Sonenberg. 1988. Internal initiation of translation of eukaryotic mRNA directed by a sequence derived from poliovirus RNA. Nature. 334:320-325. http://dx.doi.org/10.1038/334320a0
    • (1988) Nature , vol.334 , pp. 320-325
    • Pelletier, J.1    Sonenberg, N.2
  • 67
    • 83655212354 scopus 로고    scopus 로고
    • Inhibitors of alphavirus entry and replication identified with a stable Chikungunya replicon cell line and virus-based assays
    • Pohjala, L., A. Utt, M. Varjak, A. Lulla, A. Merits, T. Ahola, and P. Tammela. 2011. Inhibitors of alphavirus entry and replication identified with a stable Chikungunya replicon cell line and virus-based assays. PLoS One. 6:e28923. http://dx.doi.org/10.1371/journal.pone.0028923
    • (2011) PLoS One , vol.6
    • Pohjala, L.1    Utt, A.2    Varjak, M.3    Lulla, A.4    Merits, A.5    Ahola, T.6    Tammela, P.7
  • 68
    • 77953726483 scopus 로고    scopus 로고
    • Mammalian Atg18 (WIPI2) localizes to omegasomeanchored phagophores and positively regulates LC3 lipidation
    • Polson, H.E., J. de Lartigue, D.J. Rigden, M. Reedijk, S. Urbé, M.J. Clague, and S.A. Tooze. 2010. Mammalian Atg18 (WIPI2) localizes to omegasomeanchored phagophores and positively regulates LC3 lipidation. Autophagy. 6:506-522. http://dx.doi.org/10.4161/auto.6.4.11863
    • (2010) Autophagy , vol.6 , pp. 506-522
    • Polson, H.E.1    de Lartigue, J.2    Rigden, D.J.3    Reedijk, M.4    Urbé, S.5    Clague, M.J.6    Tooze, S.A.7
  • 69
    • 33745158157 scopus 로고
    • A simple method of estimating fifty per cent endpoint
    • Reed, L.J., and H. Muench. 1938. A simple method of estimating fifty per cent endpoint. Am. J. Epidemiol. 27:493-497.
    • (1938) Am. J. Epidemiol , vol.27 , pp. 493-497
    • Reed, L.J.1    Muench, H.2
  • 70
    • 77956525570 scopus 로고    scopus 로고
    • Coronaviruses Hijack the LC3-I-positive EDEMosomes, ER-derived vesicles exporting short-lived ERAD regulators, for replication
    • Reggiori, F., I. Monastyrska, M.H. Verheije, T. Calì, M. Ulasli, S. Bianchi, R. Bernasconi, C.A. de Haan, and M. Molinari. 2010. Coronaviruses Hijack the LC3-I-positive EDEMosomes, ER-derived vesicles exporting short-lived ERAD regulators, for replication. Cell Host Microbe. 7:500-508. http://dx.doi.org/10.1016/j.chom.2010.05.013
    • (2010) Cell Host Microbe , vol.7 , pp. 500-508
    • Reggiori, F.1    Monastyrska, I.2    Verheije, M.H.3    Calì, T.4    Ulasli, M.5    Bianchi, S.6    Bernasconi, R.7    de Haan, C.A.8    Molinari, M.9
  • 71
    • 84890812887 scopus 로고    scopus 로고
    • Distinct functions of Ulk1 and Ulk2 in the regulation of lipid metabolism in adipocytes
    • Ro, S.H., C.H. Jung, W.S. Hahn, X. Xu, Y.M. Kim, Y.S. Yun, J.M. Park, K.H. Kim, M. Seo, T.Y. Ha, et al. 2013. Distinct functions of Ulk1 and Ulk2 in the regulation of lipid metabolism in adipocytes. Autophagy. 9:2103-2114. http://dx.doi.org/10.4161/auto.26563
    • (2013) Autophagy , vol.9 , pp. 2103-2114
    • Ro, S.H.1    Jung, C.H.2    Hahn, W.S.3    Xu, X.4    Kim, Y.M.5    Yun, Y.S.6    Park, J.M.7    Kim, K.H.8    Seo, M.9    Ha, T.Y.10
  • 72
    • 0023968084 scopus 로고
    • Expression of the firefly luciferase gene in vaccinia virus: a highly sensitive gene marker to follow virus dissemination in tissues of infected animals
    • Rodriguez, J.F., D. Rodriguez, J.R. Rodriguez, E.B. McGowan, and M. Esteban. 1988. Expression of the firefly luciferase gene in vaccinia virus: a highly sensitive gene marker to follow virus dissemination in tissues of infected animals. Proc. Natl. Acad. Sci. USA. 85:1667-1671. http://dx.doi.org/10.1073/pnas.85.5.1667
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1667-1671
    • Rodriguez, J.F.1    Rodriguez, D.2    Rodriguez, J.R.3    McGowan, E.B.4    Esteban, M.5
  • 73
    • 0025953696 scopus 로고
    • The state of the p53 and retinoblastoma genes in human cervical carcinoma cell lines
    • Scheffner, M., K. Münger, J.C. Byrne, and P.M. Howley. 1991. The state of the p53 and retinoblastoma genes in human cervical carcinoma cell lines. Proc. Natl. Acad. Sci. USA. 88:5523-5527. http://dx.doi.org/10.1073/pnas.88.13.5523
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5523-5527
    • Scheffner, M.1    Münger, K.2    Byrne, J.C.3    Howley, P.M.4
  • 74
    • 84863205849 scopus 로고    scopus 로고
    • NIH Image to ImageJ: 25 years of image analysis
    • Schneider, C.A., W.S. Rasband, and K.W. Eliceiri. 2012. NIH Image to ImageJ: 25 years of image analysis. Nat. Methods. 9:671-675. http://dx.doi.org/10.1038/nmeth.2089
    • (2012) Nat. Methods , vol.9 , pp. 671-675
    • Schneider, C.A.1    Rasband, W.S.2    Eliceiri, K.W.3
  • 75
    • 8344242220 scopus 로고    scopus 로고
    • Autophagy in health and disease: a doubleedged sword
    • Shintani, T., and D.J. Klionsky. 2004. Autophagy in health and disease: a doubleedged sword. Science. 306:990-995. http://dx.doi.org/10.1126/science.1099993
    • (2004) Science , vol.306 , pp. 990-995
    • Shintani, T.1    Klionsky, D.J.2
  • 76
    • 67649634849 scopus 로고    scopus 로고
    • Defining the human deubiquitinating enzyme interaction landscape
    • Sowa, M.E., E.J. Bennett, S.P. Gygi, and J.W. Harper. 2009. Defining the human deubiquitinating enzyme interaction landscape. Cell. 138:389-403. http://dx.doi.org/10.1016/j.cell.2009.04.042
    • (2009) Cell , vol.138 , pp. 389-403
    • Sowa, M.E.1    Bennett, E.J.2    Gygi, S.P.3    Harper, J.W.4
  • 77
    • 84873407151 scopus 로고    scopus 로고
    • Non-autophagic roles of autophagyrelated proteins
    • Subramani, S., and V. Malhotra. 2013. Non-autophagic roles of autophagyrelated proteins. EMBO Rep. 14:143-151. http://dx.doi.org/10.1038/embor.2012.220
    • (2013) EMBO Rep , vol.14 , pp. 143-151
    • Subramani, S.1    Malhotra, V.2
  • 78
    • 85000814397 scopus 로고    scopus 로고
    • The ALS/FTLD associated protein C9orf72 associates with SMCR8 and WDR41 to regulate the autophagy-lysosome pathway
    • Sullivan, P.M., X. Zhou, A.M. Robins, D.H. Paushter, D. Kim, M.B. Smolka, and F. Hu. 2016. The ALS/FTLD associated protein C9orf72 associates with SMCR8 and WDR41 to regulate the autophagy-lysosome pathway. Acta Neuropathol. Commun. 4:51. http://dx.doi.org/10.1186/s40478-016-0324-5
    • (2016) Acta Neuropathol. Commun , vol.4 , pp. 51
    • Sullivan, P.M.1    Zhou, X.2    Robins, A.M.3    Paushter, D.H.4    Kim, D.5    Smolka, M.B.6    Hu, F.7
  • 79
    • 84936846861 scopus 로고    scopus 로고
    • Structure of the Atg101-Atg13 complex reveals essential roles of Atg101 in autophagy initiation
    • Suzuki, H., T. Kaizuka, N. Mizushima, and N.N. Noda. 2015a. Structure of the Atg101-Atg13 complex reveals essential roles of Atg101 in autophagy initiation. Nat. Struct. Mol. Biol. 22:572-580. http://dx.doi.org/10.1038/nsmb.3036
    • (2015) Nat. Struct. Mol. Biol , vol.22 , pp. 572-580
    • Suzuki, H.1    Kaizuka, T.2    Mizushima, N.3    Noda, N.N.4
  • 81
    • 84864871729 scopus 로고    scopus 로고
    • The role of autophagy during coxsackievirus infection of neural progenitor and stem cells
    • Tabor-Godwin, J.M., G. Tsueng, M.R. Sayen, R.A. Gottlieb, and R. Feuer. 2012. The role of autophagy during coxsackievirus infection of neural progenitor and stem cells. Autophagy. 8:938-953. http://dx.doi.org/10.4161/auto.19781
    • (2012) Autophagy , vol.8 , pp. 938-953
    • Tabor-Godwin, J.M.1    Tsueng, G.2    Sayen, M.R.3    Gottlieb, R.A.4    Feuer, R.5
  • 82
    • 67349175979 scopus 로고    scopus 로고
    • Enterovirus infections in neonates
    • Tebruegge, M., and N. Curtis. 2009. Enterovirus infections in neonates. Semin. Fetal Neonatal Med. 14:222-227. http://dx.doi.org/10.1016/j.siny.2009.02.002
    • (2009) Semin. Fetal Neonatal Med , vol.14 , pp. 222-227
    • Tebruegge, M.1    Curtis, N.2
  • 84
    • 84926472896 scopus 로고    scopus 로고
    • The RNA template channel of the RNA-dependent RNA polymerase as a target for development of antiviral therapy of multiple genera within a virus family
    • van der Linden, L., L. Vives-Adrián, B. Selisko, C. Ferrer-Orta, X. Liu, K. Lanke, R. Ulferts, A.M. De Palma, F. Tanchis, N. Goris, et al. 2015. The RNA template channel of the RNA-dependent RNA polymerase as a target for development of antiviral therapy of multiple genera within a virus family. PLoS Pathog. 11:e1004733. http://dx.doi.org/10.1371/journal.ppat.1004733
    • (2015) PLoS Pathog , vol.11
    • van der Linden, L.1    Vives-Adrián, L.2    Selisko, B.3    Ferrer-Orta, C.4    Liu, X.5    Lanke, K.6    Ulferts, R.7    De Palma, A.M.8    Tanchis, F.9    Goris, N.10
  • 86
    • 84857844643 scopus 로고    scopus 로고
    • Mammalian Atg2 proteins are essential for autophagosome formation and important for regulation of size and distribution of lipid droplets
    • Velikkakath, A.K., T. Nishimura, E. Oita, N. Ishihara, and N. Mizushima. 2012. Mammalian Atg2 proteins are essential for autophagosome formation and important for regulation of size and distribution of lipid droplets. Mol. Biol. Cell. 23:896-909. http://dx.doi.org/10.1091/mbc.E11-09-0785
    • (2012) Mol. Biol. Cell , vol.23 , pp. 896-909
    • Velikkakath, A.K.1    Nishimura, T.2    Oita, E.3    Ishihara, N.4    Mizushima, N.5
  • 88
    • 16244408648 scopus 로고    scopus 로고
    • A proline-rich region in the coxsackievirus 3A protein is required for the protein to inhibit endoplasmic reticulum-to-golgi transport
    • Wessels, E., D. Duijsings, R.A. Notebaart, W.J. Melchers, and F.J. van Kuppeveld. 2005. A proline-rich region in the coxsackievirus 3A protein is required for the protein to inhibit endoplasmic reticulum-to-golgi transport. J. Virol. 79:5163-5173. http://dx.doi.org/10.1128/JVI.79.8.5163-5173.2005
    • (2005) J. Virol , vol.79 , pp. 5163-5173
    • Wessels, E.1    Duijsings, D.2    Notebaart, R.A.3    Melchers, W.J.4    van Kuppeveld, F.J.5
  • 89
    • 84897508939 scopus 로고    scopus 로고
    • Identification and characterization of a proteolytically primed form of the murine coronavirus spike proteins after fusion with the target cell
    • Wicht, O., C. Burkard, C.A. de Haan, F.J. van Kuppeveld, P.J. Rottier, and B.J. Bosch. 2014. Identification and characterization of a proteolytically primed form of the murine coronavirus spike proteins after fusion with the target cell. J. Virol. 88:4943-4952. http://dx.doi.org/10.1128/JVI.03451-13
    • (2014) J. Virol , vol.88 , pp. 4943-4952
    • Wicht, O.1    Burkard, C.2    de Haan, C.A.3    van Kuppeveld, F.J.4    Rottier, P.J.5    Bosch, B.J.6
  • 90
    • 50949133741 scopus 로고    scopus 로고
    • Autophagosome supports coxsackievirus B3 replication in host cells
    • Wong, J., J. Zhang, X. Si, G. Gao, I. Mao, B.M. McManus, and H. Luo. 2008. Autophagosome supports coxsackievirus B3 replication in host cells. J. Virol. 82:9143-9153. http://dx.doi.org/10.1128/JVI.00641-08
    • (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
  • 91
    • 84873675067 scopus 로고    scopus 로고
    • The ULK1 complex: sensing nutrient signals for autophagy activation
    • Wong, P.M., C. Puente, I.G. Ganley, and X. Jiang. 2013. The ULK1 complex: sensing nutrient signals for autophagy activation. Autophagy. 9:124-137. http://dx.doi.org/10.4161/auto.23323
    • (2013) Autophagy , vol.9 , pp. 124-137
    • Wong, P.M.1    Puente, C.2    Ganley, I.G.3    Jiang, X.4
  • 92
    • 84938866111 scopus 로고    scopus 로고
    • Basal autophagy is required for herpes simplex virus-2 infection
    • Yakoub, A.M., and D. Shukla. 2015. Basal autophagy is required for herpes simplex virus-2 infection. Sci. Rep. 5:12985. http://dx.doi.org/10.1038/srep12985
    • (2015) Sci. Rep , vol.5 , pp. 12985
    • Yakoub, A.M.1    Shukla, D.2
  • 93
    • 77951214016 scopus 로고    scopus 로고
    • Mammalian autophagy: core molecular machinery and signaling regulation
    • Yang, Z., and D.J. Klionsky. 2010. Mammalian autophagy: core molecular machinery and signaling regulation. Curr. Opin. Cell Biol. 22:124-131. http://dx.doi.org/10.1016/j.ceb.2009.11.014
    • (2010) Curr. Opin. Cell Biol , vol.22 , pp. 124-131
    • Yang, Z.1    Klionsky, D.J.2
  • 94
    • 33645946032 scopus 로고    scopus 로고
    • Cellular autophagy machinery is not required for vaccinia virus replication and maturation
    • Zhang, H., C.E. Monken, Y. Zhang, J. Lenard, N. Mizushima, E.C. Lattime, and S. Jin. 2006. Cellular autophagy machinery is not required for vaccinia virus replication and maturation. Autophagy. 2:91-95. http://dx.doi.org/10.4161/auto.2.2.2297
    • (2006) Autophagy , vol.2 , pp. 91-95
    • Zhang, H.1    Monken, C.E.2    Zhang, Y.3    Lenard, J.4    Mizushima, N.5    Lattime, E.C.6    Jin, S.7
  • 95
    • 79957926128 scopus 로고    scopus 로고
    • Autophagy promotes the replication of encephalomyocarditis virus in host cells
    • Zhang, Y., Z. Li, X. Ge, X. Guo, and H. Yang. 2011. Autophagy promotes the replication of encephalomyocarditis virus in host cells. Autophagy. 7:613-628. http://dx.doi.org/10.4161/auto.7.6.15267
    • (2011) Autophagy , vol.7 , pp. 613-628
    • Zhang, Y.1    Li, Z.2    Ge, X.3    Guo, X.4    Yang, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.