메뉴 건너뛰기




Volumn 89, Issue 15, 2015, Pages 8026-8041

Dengue virus inhibition of autophagic flux and dependency of viral replication on proteasomal degradation of the autophagy receptor p62

Author keywords

[No Author keywords available]

Indexed keywords

CELL RECEPTOR; MAMMALIAN TARGET OF RAPAMYCIN INHIBITOR; PROTEASOME; PROTEIN P62; PROTEIN SQSTM1; TORIN1; UNCLASSIFIED DRUG; SIGNAL TRANSDUCING ADAPTOR PROTEIN; SQSTM1 PROTEIN, HUMAN;

EID: 84937699264     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00787-15     Document Type: Article
Times cited : (100)

References (60)
  • 1
    • 77249096377 scopus 로고    scopus 로고
    • Small interference RNA profiling reveals the essential role of human membrane trafficking genes in mediating the infectious entry of dengue virus
    • Ang F, Wong AP, Ng MM, Chu JJ. 2010. Small interference RNA profiling reveals the essential role of human membrane trafficking genes in mediating the infectious entry of dengue virus. Virol J 7:24. http://dx.doi.org/10.1186/1743-422X-7-24.
    • (2010) Virol J , vol.7 , pp. 24
    • Ang, F.1    Wong, A.P.2    Ng, M.M.3    Chu, J.J.4
  • 3
    • 0029941322 scopus 로고    scopus 로고
    • Immunolocalization of the dengue virus nonstructural glycoprotein NS1 suggests a role in viral RNA replication
    • Mackenzie JM, Jones MK, Young PR. 1996. Immunolocalization of the dengue virus nonstructural glycoprotein NS1 suggests a role in viral RNA replication. Virology 220:232-240. http://dx.doi.org/10.1006/viro.1996.0307.
    • (1996) Virology , vol.220 , pp. 232-240
    • Mackenzie, J.M.1    Jones, M.K.2    Young, P.R.3
  • 5
    • 62749134544 scopus 로고    scopus 로고
    • Colocalization of constituents of the dengue virus translation and replication machinery with amphisomes
    • Panyasrivanit M, Khakpoor A, Wikan N, Smith DR. 2009. Colocalization of constituents of the dengue virus translation and replication machinery with amphisomes. J Gen Virol 90:448-456. http://dx.doi.org/10.1099/vir.0.005355-0.
    • (2009) J Gen Virol , vol.90 , pp. 448-456
    • Panyasrivanit, M.1    Khakpoor, A.2    Wikan, N.3    Smith, D.R.4
  • 6
    • 67449086380 scopus 로고    scopus 로고
    • A role for autophagolysosomes in dengue virus 3 production in HepG2 cells
    • Khakpoor A, Panyasrivanit M, Wikan N, Smith DR. 2009. A role for autophagolysosomes in dengue virus 3 production in HepG2 cells. J Gen Virol 90:1093-1103. http://dx.doi.org/10.1099/vir.0.007914-0.
    • (2009) J Gen Virol , vol.90 , pp. 1093-1103
    • Khakpoor, A.1    Panyasrivanit, M.2    Wikan, N.3    Smith, D.R.4
  • 7
    • 78349237370 scopus 로고    scopus 로고
    • Dengue virus-induced autophagy regulates lipid metabolism
    • Heaton NS, Randall G. 2010. Dengue virus-induced autophagy regulates lipid metabolism. Cell Host Microbe 8:422-432. http://dx.doi.org/10.1016/j.chom.2010.10.006.
    • (2010) Cell Host Microbe , vol.8 , pp. 422-432
    • Heaton, N.S.1    Randall, G.2
  • 8
    • 79959344614 scopus 로고    scopus 로고
    • Flavivirus NS4A-induced autophagy protects cells against death and enhances virus replication
    • McLean JE, Wudzinska A, Datan E, Quaglino D, Zakeri Z. 2011. Flavivirus NS4A-induced autophagy protects cells against death and enhances virus replication. J Biol Chem 286:22147-22159. http://dx.doi.org/10.1074/jbc.M110.192500.
    • (2011) J Biol Chem , vol.286 , pp. 22147-22159
    • McLean, J.E.1    Wudzinska, A.2    Datan, E.3    Quaglino, D.4    Zakeri, Z.5
  • 9
    • 84863428905 scopus 로고    scopus 로고
    • Autophagy regulation and integration with cell signaling
    • Hamacher-Brady A. 2012. Autophagy regulation and integration with cell signaling. Antioxid Redox Signal 17:756-765. http://dx.doi.org/10.1089/ars.2011.4410.
    • (2012) Antioxid Redox Signal , vol.17 , pp. 756-765
    • Hamacher-Brady, A.1
  • 10
    • 84881552168 scopus 로고    scopus 로고
    • The role of 'eat-me' signals and autophagy cargo receptors in innate immunity
    • Boyle KBand Randow F. 2013. The role of 'eat-me' signals and autophagy cargo receptors in innate immunity. Curr Opin Microbiol 16:339-348. http://dx.doi.org/10.1016/j.mib.2013.03.010.
    • (2013) Curr Opin Microbiol , vol.16 , pp. 339-348
    • Boyle, K.B.1    Randow, F.2
  • 11
    • 79952355107 scopus 로고    scopus 로고
    • Selective autophagy mediated by autophagic adapter proteins
    • Johansen T, Lamark T. 2011. Selective autophagy mediated by autophagic adapter proteins. Autophagy 7:279-296. http://dx.doi.org/10.4161/auto.7.3.14487.
    • (2011) Autophagy , vol.7 , pp. 279-296
    • Johansen, T.1    Lamark, T.2
  • 12
    • 84906043176 scopus 로고    scopus 로고
    • Targeting SQSTM1/p62 induces cargo loading failure and converts autophagy to apoptosis via NBK/Bik
    • Chen S, Zhou L, Zhang Y, Leng Y, Pei XY, Lin H, Jones R, Orlowski RZ, Dai Y, Grant S. 2014. Targeting SQSTM1/p62 induces cargo loading failure and converts autophagy to apoptosis via NBK/Bik. Mol Cell Biol 34:3435-3449. http://dx.doi.org/10.1128/MCB.01383-13.
    • (2014) Mol Cell Biol , vol.34 , pp. 3435-3449
    • Chen, S.1    Zhou, L.2    Zhang, Y.3    Leng, Y.4    Pei, X.Y.5    Lin, H.6    Jones, R.7    Orlowski, R.Z.8    Dai, Y.9    Grant, S.10
  • 14
    • 67549139899 scopus 로고    scopus 로고
    • Toll-like receptors in control of immunological autophagy
    • Delgado MAand Deretic V. 2009. Toll-like receptors in control of immunological autophagy. Cell Death Differ 16:976-983. http://dx.doi.org/10.1038/cdd.2009.40.
    • (2009) Cell Death Differ , vol.16 , pp. 976-983
    • Delgado, M.A.1    Deretic, V.2
  • 15
    • 79953155924 scopus 로고    scopus 로고
    • MHC presentation via autophagy and how viruses escape from it
    • Gannage Mand Munz C. 2010. MHC presentation via autophagy and how viruses escape from it. Semin Immunopathol 32:373-381. http://dx.doi.org/10.1007/s00281-010-0227-7.
    • (2010) Semin Immunopathol , vol.32 , pp. 373-381
    • Gannage Mand Munz, C.1
  • 16
    • 77953597957 scopus 로고    scopus 로고
    • Viruses and the autophagy machinery
    • Dreux M, Chisari FV. 2010. Viruses and the autophagy machinery. Cell Cycle 9:1295-1307. http://dx.doi.org/10.4161/cc.9.7.11109.
    • (2010) Cell Cycle , vol.9 , pp. 1295-1307
    • Dreux, M.1    Chisari, F.V.2
  • 17
    • 39749116856 scopus 로고    scopus 로고
    • Hepatitis C virus genotype 1a growth and induction of autophagy
    • Ait-Goughoulte M, Kanda T, Meyer K, Ryerse JS, Ray RB, Ray R. 2008. Hepatitis C virus genotype 1a growth and induction of autophagy. J Virol 82:2241-2249. http://dx.doi.org/10.1128/JVI.02093-07.
    • (2008) J Virol , vol.82 , pp. 2241-2249
    • Ait-Goughoulte, M.1    Kanda, T.2    Meyer, K.3    Ryerse, J.S.4    Ray, R.B.5    Ray, R.6
  • 18
    • 54449101892 scopus 로고    scopus 로고
    • Induction of incomplete autophagic response by hepatitis C virus via the unfolded protein response
    • Sir D, Chen WL, Choi J, Wakita T, Yen TS, Ou JH. 2008. Induction of incomplete autophagic response by hepatitis C virus via the unfolded protein response. Hepatology 48:1054-1061. http://dx.doi.org/10.1002/hep.22464.
    • (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
  • 19
    • 50249087889 scopus 로고    scopus 로고
    • Perturbation of autophagic pathway by hepatitis C virus
    • Sir D, Liang C, Chen WL, Jung JU, Ou JH. 2008. Perturbation of autophagic pathway by hepatitis C virus. Autophagy 4:830-831. http://dx.doi.org/10.4161/auto.6566.
    • (2008) Autophagy , vol.4 , pp. 830-831
    • Sir, D.1    Liang, C.2    Chen, W.L.3    Jung, J.U.4    Ou, J.H.5
  • 20
    • 70349634804 scopus 로고    scopus 로고
    • Knockdown of autophagy-related gene decreases the production of infectious hepatitis C virus particles
    • Tanida I, Fukasawa M, Ueno T, Kominami E, Wakita T, Hanada K. 2009. Knockdown of autophagy-related gene decreases the production of infectious hepatitis C virus particles. Autophagy 5:937-945. http://dx.doi.org/10.4161/auto.5.7.9243.
    • (2009) Autophagy , vol.5 , pp. 937-945
    • Tanida, I.1    Fukasawa, M.2    Ueno, T.3    Kominami, E.4    Wakita, T.5    Hanada, K.6
  • 21
    • 77955515860 scopus 로고    scopus 로고
    • Autophagy protein ATG5 interacts transiently with the hepatitis C virus RNA polymerase (NS5B) early during infection
    • Guevin C, Manna D, Belanger C, Konan KV, Mak P, Labonte P. 2010. Autophagy protein ATG5 interacts transiently with the hepatitis C virus RNA polymerase (NS5B) early during infection. Virology 405:1-7. http://dx.doi.org/10.1016/j.virol.2010.05.032.
    • (2010) Virology , vol.405 , pp. 1-7
    • Guevin, C.1    Manna, D.2    Belanger, C.3    Konan, K.V.4    Mak, P.5    Labonte, P.6
  • 22
    • 79251512287 scopus 로고    scopus 로고
    • Knockdown of autophagy enhances the innate immune response in hepatitis C virus-infected hepatocytes
    • Shrivastava S, Raychoudhuri A, Steele R, Ray R, Ray RB. 2011. Knockdown of autophagy enhances the innate immune response in hepatitis C virus-infected hepatocytes. Hepatology 53:406-414. http://dx.doi.org/10.1002/hep.24073.
    • (2011) Hepatology , vol.53 , pp. 406-414
    • Shrivastava, S.1    Raychoudhuri, A.2    Steele, R.3    Ray, R.4    Ray, R.B.5
  • 23
    • 84870776595 scopus 로고    scopus 로고
    • Intracellular vesicle acidification promotes maturation of infectious poliovirus particles
    • Richards AL, Jackson WT. 2012. Intracellular vesicle acidification promotes maturation of infectious poliovirus particles. PLoS Pathog 8:e1003046. http://dx.doi.org/10.1371/journal.ppat.1003046.
    • (2012) PLoS Pathog , vol.8
    • Richards, A.L.1    Jackson, W.T.2
  • 24
    • 69549135689 scopus 로고    scopus 로고
    • The autophagy machinery is required to initiate hepatitis C virus replication
    • Dreux M, Gastaminza P, Wieland SF, Chisari FV. 2009. The autophagy machinery is required to initiate hepatitis C virus replication. Proc Natl Acad Sci USA 106:14046-14051. http://dx.doi.org/10.1073/pnas.0907344106.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 14046-14051
    • Dreux, M.1    Gastaminza, P.2    Wieland, S.F.3    Chisari, F.V.4
  • 26
    • 78650961487 scopus 로고    scopus 로고
    • Activation of the unfolded protein response and autophagy after hepatitis C virus infection suppresses innate antiviral immunity in vitro
    • Ke PYand Chen SS. 2011. Activation of the unfolded protein response and autophagy after hepatitis C virus infection suppresses innate antiviral immunity in vitro. J Clin Invest 121:37-56. http://dx.doi.org/10.1172/JCI41474.
    • (2011) J Clin Invest , vol.121 , pp. 37-56
    • Ke, P.Y.1    Chen, S.S.2
  • 27
    • 84891914134 scopus 로고    scopus 로고
    • Single-virus tracking approach to reveal the interaction of dengue virus with autophagy during the early stage of infection
    • Chu LW, Huang YL, Lee JH, Huang LY, Chen WJ, Lin YH, Chen JY, Xiang R, Lee CH, Ping YH. 2014. Single-virus tracking approach to reveal the interaction of dengue virus with autophagy during the early stage of infection. J Biomed Opt 19:011018. http://dx.doi.org/10.1117/1.JBO.19.1.011018.
    • (2014) J Biomed Opt , vol.19 , pp. 011018
    • Chu, L.W.1    Huang, Y.L.2    Lee, J.H.3    Huang, L.Y.4    Chen, W.J.5    Lin, Y.H.6    Chen, J.Y.7    Xiang, R.8    Lee, C.H.9    Ping, Y.H.10
  • 30
    • 79957792406 scopus 로고    scopus 로고
    • Concurrent detection of autolysosome formation and lysosomal degradation by flow cytometry in a high-content screen for inducers of autophagy
    • Hundeshagen P, Hamacher-Brady A, Eils R, Brady NR. 2011. Concurrent detection of autolysosome formation and lysosomal degradation by flow cytometry in a high-content screen for inducers of autophagy. BMC Biol 9:38. http://dx.doi.org/10.1186/1741-7007-9-38.
    • (2011) BMC Biol , vol.9 , pp. 38
    • Hundeshagen, P.1    Hamacher-Brady, A.2    Eils, R.3    Brady, N.R.4
  • 31
    • 33646851580 scopus 로고    scopus 로고
    • Subcellular localization and membrane topology of the dengue virus type 2 nonstructural protein 4B
    • Miller S, Sparacio S, Bartenschlager R. 2006. Subcellular localization and membrane topology of the dengue virus type 2 nonstructural protein 4B. J Biol Chem 281:8854-8863. http://dx.doi.org/10.1074/jbc.M512697200.
    • (2006) J Biol Chem , vol.281 , pp. 8854-8863
    • Miller, S.1    Sparacio, S.2    Bartenschlager, R.3
  • 32
    • 0019966544 scopus 로고
    • Growth of human hepatoma cells lines with differentiated functions in chemically defined medium
    • Nakabayashi H, Taketa K, Miyano K, Yamane T, Sato J. 1982. Growth of human hepatoma cells lines with differentiated functions in chemically defined medium. Cancer Res 42:3858-3863.
    • (1982) Cancer Res , vol.42 , pp. 3858-3863
    • Nakabayashi, H.1    Taketa, K.2    Miyano, K.3    Yamane, T.4    Sato, J.5
  • 34
    • 84863205849 scopus 로고    scopus 로고
    • NIH Image to ImageJ: 25 years of image analysis
    • Schneider CA, Rasband WS, Eliceiri KW. 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
  • 35
    • 0034329418 scopus 로고    scopus 로고
    • LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing
    • Kabeya Y, Mizushima N, Ueno T, Yamamoto A, Kirisako T, Noda T, Kominami E, Ohsumi Y, Yoshimori T. 2000. LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing. EMBO J 19:5720-5728. http://dx.doi.org/10.1093/emboj/19.21.5720.
    • (2000) EMBO J , vol.19 , pp. 5720-5728
    • Kabeya, Y.1    Mizushima, N.2    Ueno, T.3    Yamamoto, A.4    Kirisako, T.5    Noda, T.6    Kominami, E.7    Ohsumi, Y.8    Yoshimori, T.9
  • 36
    • 33749570745 scopus 로고    scopus 로고
    • Enhancing macroautophagy protects against ischemia/reperfusion injury in cardiac myocytes
    • Hamacher-Brady A, Brady NR, Gottlieb RA. 2006. Enhancing macroautophagy protects against ischemia/reperfusion injury in cardiac myocytes. J Biol Chem 281:29776-29787. http://dx.doi.org/10.1074/jbc.M603783200.
    • (2006) J Biol Chem , vol.281 , pp. 29776-29787
    • Hamacher-Brady, A.1    Brady, N.R.2    Gottlieb, R.A.3
  • 37
    • 53549084325 scopus 로고    scopus 로고
    • Does bafilomycin A1 block the fusion of autophagosomes with lysosomes?
    • Klionsky DJ, Elazar Z, Seglen PO, Rubinsztein DC. 2008. Does bafilomycin A1 block the fusion of autophagosomes with lysosomes?. Autophagy 4:849-850. http://dx.doi.org/10.4161/auto.6845.
    • (2008) Autophagy , vol.4 , pp. 849-850
    • Klionsky, D.J.1    Elazar, Z.2    Seglen, P.O.3    Rubinsztein, D.C.4
  • 41
    • 84924407537 scopus 로고    scopus 로고
    • Applications of flow cytometry for measurement of autophagy
    • Demishtein A, Porat Z, Elazar Z, Shvets E. 2015. Applications of flow cytometry for measurement of autophagy. Methods 75:87-95. http://dx.doi.org/10.1016/j.ymeth.2014.12.020.
    • (2015) Methods , vol.75 , pp. 87-95
    • Demishtein, A.1    Porat, Z.2    Elazar, Z.3    Shvets, E.4
  • 43
    • 82755161948 scopus 로고    scopus 로고
    • Cysteine cathepsins: from structure, function, and regulation to new frontiers
    • Turk V, Stoka V, Vasiljeva O, Renko M, Sun T, Turk B, Turk D. 2012. Cysteine cathepsins: from structure, function, and regulation to new frontiers. Biochim Biophys Acta 1824:68-88. http://dx.doi.org/10.1016/j.bbapap.2011.10.002.
    • (2012) Biochim Biophys Acta , vol.1824 , pp. 68-88
    • Turk, V.1    Stoka, V.2    Vasiljeva, O.3    Renko, M.4    Sun, T.5    Turk, B.6    Turk, D.7
  • 44
    • 84862611041 scopus 로고    scopus 로고
    • TBC1D14 regulates autophagosome formation via Rab11-and ULK1-positive recycling endosomes
    • Longatti A, Lamb CA, Razi M, Yoshimura S, Barr FA, Tooze SA. 2012. TBC1D14 regulates autophagosome formation via Rab11-and ULK1-positive recycling endosomes. J Cell Biol 197:659-675. http://dx.doi.org/10.1083/jcb.201111079.
    • (2012) J Cell Biol , vol.197 , pp. 659-675
    • Longatti, A.1    Lamb, C.A.2    Razi, M.3    Yoshimura, S.4    Barr, F.A.5    Tooze, S.A.6
  • 45
    • 84861396483 scopus 로고    scopus 로고
    • Rab GTPase-activating proteins in autophagy: regulation of endocytic and autophagy pathways by direct binding to human ATG8 modifiers
    • Popovic D, Akutsu M, Novak I, Harper JW, Behrends C, Dikic I. 2012. Rab GTPase-activating proteins in autophagy: regulation of endocytic and autophagy pathways by direct binding to human ATG8 modifiers. Mol Cell Biol 32:1733-1744. http://dx.doi.org/10.1128/MCB.06717-11.
    • (2012) Mol Cell Biol , vol.32 , pp. 1733-1744
    • Popovic, D.1    Akutsu, M.2    Novak, I.3    Harper, J.W.4    Behrends, C.5    Dikic, I.6
  • 46
    • 38149044992 scopus 로고    scopus 로고
    • Induction of autophagy promotes fusion of multivesicular bodies with autophagic vacuoles in k562 cells
    • Fader CM, Sanchez D, Furlan M, Colombo MI. 2008. Induction of autophagy promotes fusion of multivesicular bodies with autophagic vacuoles in k562 cells. Traffic 9:230-250. http://dx.doi.org/10.1111/j.1600-0854.2007.00677.x.
    • (2008) Traffic , vol.9 , pp. 230-250
    • Fader, C.M.1    Sanchez, D.2    Furlan, M.3    Colombo, M.I.4
  • 47
    • 27944504351 scopus 로고    scopus 로고
    • p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
    • Bjorkoy G, Lamark T, Brech A, Outzen H, Perander M, Overvatn A, Stenmark H, Johansen T. 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. http://dx.doi.org/10.1083/jcb.200507002.
    • (2005) J Cell Biol , vol.171 , pp. 603-614
    • Bjorkoy, G.1    Lamark, T.2    Brech, A.3    Outzen, H.4    Perander, M.5    Overvatn, A.6    Stenmark, H.7    Johansen, T.8
  • 48
    • 70350450808 scopus 로고    scopus 로고
    • The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitin-coated bacteria
    • Thurston TL, Ryzhakov G, Bloor S, von Muhlinen N, Randow F. 2009. The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitin-coated bacteria. Nat Immunol 10:1215-1221. http://dx.doi.org/10.1038/ni.1800.
    • (2009) Nat Immunol , vol.10 , pp. 1215-1221
    • Thurston, T.L.1    Ryzhakov, G.2    Bloor, S.3    von Muhlinen, N.4    Randow, F.5
  • 50
    • 84872199305 scopus 로고    scopus 로고
    • The proteomic analysis of endogenous FAT10 substrates identifies p62/SQSTM1 as a substrate of FAT10ylation
    • Aichem A, Kalveram B, Spinnenhirn V, Kluge K, Catone N, Johansen T, Groettrup M. 2012. The proteomic analysis of endogenous FAT10 substrates identifies p62/SQSTM1 as a substrate of FAT10ylation. J Cell Sci 125:4576-4585. http://dx.doi.org/10.1242/jcs.107789.
    • (2012) J Cell Sci , vol.125 , pp. 4576-4585
    • Aichem, A.1    Kalveram, B.2    Spinnenhirn, V.3    Kluge, K.4    Catone, N.5    Johansen, T.6    Groettrup, M.7
  • 51
    • 84880152406 scopus 로고    scopus 로고
    • Divergent roles of autophagy in virus infection
    • Chiramel AI, Brady NR, Bartenschlager R. 2013. Divergent roles of autophagy in virus infection. Cells 2:83-104. http://dx.doi.org/10.3390/cells2010083.
    • (2013) Cells , vol.2 , pp. 83-104
    • Chiramel, A.I.1    Brady, N.R.2    Bartenschlager, R.3
  • 52
    • 84901034931 scopus 로고    scopus 로고
    • Phosphoprotein of human parainfluenza virus type 3 blocks autophagosome-lysosome fusion to increase virus production
    • Ding B, Zhang G, Yang X, Zhang S, Chen L, Yan Q, Xu M, Banerjee AK, Chen M. 2014. Phosphoprotein of human parainfluenza virus type 3 blocks autophagosome-lysosome fusion to increase virus production. Cell Host Microbe 15:564-577. http://dx.doi.org/10.1016/j.chom.2014.04.004.
    • (2014) Cell Host Microbe , vol.15 , pp. 564-577
    • Ding, B.1    Zhang, G.2    Yang, X.3    Zhang, S.4    Chen, L.5    Yan, Q.6    Xu, M.7    Banerjee, A.K.8    Chen, M.9
  • 53
    • 77953712951 scopus 로고    scopus 로고
    • Autophagy by hepatitis B virus and for hepatitis B virus
    • Sir D, Ann DK, Ou JH. 2010. Autophagy by hepatitis B virus and for hepatitis B virus. Autophagy 6:548-549. http://dx.doi.org/10.4161/auto.6.4.11669.
    • (2010) Autophagy , vol.6 , pp. 548-549
    • Sir, D.1    Ann, D.K.2    Ou, J.H.3
  • 54
    • 50949133741 scopus 로고    scopus 로고
    • Autophagosome supports coxsackievirus B3 replication in host cells
    • Wong J, Zhang J, Si X, Gao G, Mao I, McManus BM, Luo H. 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
  • 55
    • 35848956344 scopus 로고    scopus 로고
    • Aggresomes and pericentriolar sites of virus assembly: cellular defense or viral design?
    • Wileman T. 2007. Aggresomes and pericentriolar sites of virus assembly: cellular defense or viral design?. Annu Rev Microbiol 61:149-167. http://dx.doi.org/10.1146/annurev.micro.57.030502.090836.
    • (2007) Annu Rev Microbiol , vol.61 , pp. 149-167
    • Wileman, T.1
  • 56
    • 77951217000 scopus 로고    scopus 로고
    • Dual role of 3-methyladenine in modulation of autophagy via different temporal patterns of inhibition on class I and III phosphoinositide 3-kinase
    • Wu YT, Tan HL, Shui G, Bauvy C, Huang Q, Wenk MR, Ong CN, Codogno P, Shen HM. 2010. Dual role of 3-methyladenine in modulation of autophagy via different temporal patterns of inhibition on class I and III phosphoinositide 3-kinase. J Biol Chem 285:10850-10861. http://dx.doi.org/10.1074/jbc.M109.080796.
    • (2010) J Biol Chem , vol.285 , pp. 10850-10861
    • Wu, Y.T.1    Tan, H.L.2    Shui, G.3    Bauvy, C.4    Huang, Q.5    Wenk, M.R.6    Ong, C.N.7    Codogno, P.8    Shen, H.M.9
  • 58
    • 78049271501 scopus 로고    scopus 로고
    • A phosphatidylinositol 3-kinase class III subcomplex containing VPS15, VPS34, Beclin 1, UVRAG and BIF-1 regulates cytokinesis and degradative endocytic traffic
    • Thoresen SB, Pedersen NM, Liestol K, Stenmark H. 2010. A phosphatidylinositol 3-kinase class III subcomplex containing VPS15, VPS34, Beclin 1, UVRAG and BIF-1 regulates cytokinesis and degradative endocytic traffic. Exp Cell Res 316:3368-3378. http://dx.doi.org/10.1016/j.yexcr.2010.07.008.
    • (2010) Exp Cell Res , vol.316 , pp. 3368-3378
    • Thoresen, S.B.1    Pedersen, N.M.2    Liestol, K.3    Stenmark, H.4
  • 59
    • 4444220680 scopus 로고    scopus 로고
    • Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation
    • Seibenhener ML, Babu JR, Geetha T, Wong HC, Krishna NR, Wooten MW. 2004. Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation. Mol Cell Biol 24:8055-8068. http://dx.doi.org/10.1128/MCB.24.18.8055-8068.2004.
    • (2004) Mol Cell Biol , vol.24 , pp. 8055-8068
    • Seibenhener, M.L.1    Babu, J.R.2    Geetha, T.3    Wong, H.C.4    Krishna, N.R.5    Wooten, M.W.6
  • 60
    • 84857039937 scopus 로고    scopus 로고
    • Autophagy as an innate immunity paradigm: expanding the scope and repertoire of pattern recognition receptors
    • Deretic V. 2012. Autophagy as an innate immunity paradigm: expanding the scope and repertoire of pattern recognition receptors. Curr Opin Immunol 24:21-31. http://dx.doi.org/10.1016/j.coi.2011.10.006.
    • (2012) Curr Opin Immunol , vol.24 , pp. 21-31
    • Deretic, V.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.