메뉴 건너뛰기




Volumn 88, Issue 8, 2014, Pages 4572-4585

Hijacking of RIG-I signaling proteins into virus-induced cytoplasmic structures correlates with the inhibition of type I interferon responses

Author keywords

[No Author keywords available]

Indexed keywords

BETA INTERFERON; PROTEIN TBK1; PROTEIN TRIM25; RAB PROTEIN; RETINOIC ACID INDUCIBLE PROTEIN I; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 84896930327     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.03021-13     Document Type: Article
Times cited : (104)

References (74)
  • 1
    • 77950343791 scopus 로고    scopus 로고
    • Pattern recognition receptors and inflammation
    • Takeuchi O, Akira S. 2010. Pattern recognition receptors and inflammation. Cell 140:805-820. http://dx.doi.org/10.1016/j.cell.2010.01.022.
    • (2010) Cell , vol.140 , pp. 805-820
    • Takeuchi, O.1    Akira, S.2
  • 2
    • 32944464648 scopus 로고    scopus 로고
    • Pathogen recognition and innate immunity
    • Akira S, Uematsu S, Takeuchi O. 2006. Pathogen recognition and innate immunity. Cell 124:783-801. http://dx.doi.org/10.1016/j.cell.2006.02.015.
    • (2006) Cell , vol.124 , pp. 783-801
    • Akira, S.1    Uematsu, S.2    Takeuchi, O.3
  • 3
    • 33746028777 scopus 로고    scopus 로고
    • Intracellular pattern recognition receptors in the host response
    • Meylan E, Tschopp J, Karin M. 2006. Intracellular pattern recognition receptors in the host response. Nature 442:39-44. http://dx.doi.org/10.1038/nature04946.
    • (2006) Nature , vol.442 , pp. 39-44
    • Meylan, E.1    Tschopp, J.2    Karin, M.3
  • 4
    • 34548126512 scopus 로고    scopus 로고
    • RIG-I family RNA helicases: cytoplasmic sensor for antiviral innate immunity
    • Yoneyama M, Fujita T. 2007. RIG-I family RNA helicases: cytoplasmic sensor for antiviral innate immunity. Cytokine Growth Factor Rev. 18: 545-551. http://dx.doi.org/10.1016/j.cytogfr.2007.06.023.
    • (2007) Cytokine Growth Factor Rev. , vol.18 , pp. 545-551
    • Yoneyama, M.1    Fujita, T.2
  • 5
    • 77954754505 scopus 로고    scopus 로고
    • Induction of type I interferon by RNA viruses: cellular receptors and their substrates
    • Baum A, García-Sastre A. 2010. Induction of type I interferon by RNA viruses: cellular receptors and their substrates. Amino Acids 38:1283-1299. http://dx.doi.org/10.1007/s00726-009-0374-0.
    • (2010) Amino Acids , vol.38 , pp. 1283-1299
    • Baum, A.1    García-Sastre, A.2
  • 6
    • 58049202272 scopus 로고    scopus 로고
    • Innate immunity to virus infection
    • Takeuchi O, Akira S. 2009. Innate immunity to virus infection. Immunol. Rev. 227:75-86. http://dx.doi.org/10.1111/j.1600-065X.2008.00737.x.
    • (2009) Immunol. Rev. , vol.227 , pp. 75-86
    • Takeuchi, O.1    Akira, S.2
  • 7
    • 48949094095 scopus 로고    scopus 로고
    • Structural mechanism of RNA recognition by the RIG-I-like receptors
    • Yoneyama M, Fujita T. 2008. Structural mechanism of RNA recognition by the RIG-I-like receptors. Immunity 29:178-181. http://dx.doi.org/10.1016/j.immuni.2008.07.009.
    • (2008) Immunity , vol.29 , pp. 178-181
    • Yoneyama, M.1    Fujita, T.2
  • 8
    • 58049217490 scopus 로고    scopus 로고
    • RNA recognition and signal transduction by RIG-I-like receptors
    • Yoneyama M, Fujita T. 2009. RNA recognition and signal transduction by RIG-I-like receptors. Immunol. Rev. 227:54-65. http://dx.doi.org/10.1111/j.1600-065X.2008.00727.x.
    • (2009) Immunol. Rev. , vol.227 , pp. 54-65
    • Yoneyama, M.1    Fujita, T.2
  • 9
    • 44449125726 scopus 로고    scopus 로고
    • MDA5 participates in the detection of paramyxovirus infection and is essential for the early activation of dendritic cells in response to Sendai virus defective interfering particles
    • Yount JS, Gitlin L, Moran TM, López CB. 2008. MDA5 participates in the detection of paramyxovirus infection and is essential for the early activation of dendritic cells in response to Sendai virus defective interfering particles. J. Immunol. 180:4910-4918.
    • (2008) J. Immunol. , vol.180 , pp. 4910-4918
    • Yount, J.S.1    Gitlin, L.2    Moran, T.M.3    López, C.B.4
  • 10
    • 26444539685 scopus 로고    scopus 로고
    • Activation of innate defense against a paramyxovirus is mediated by RIG-I and TLR7 and TLR8 in a cell-type-specific manner
    • Melchjorsen J, Jensen SB, Malmgaard L, Rasmussen SB, Weber F, Bowie AG, Matikainen S, Paludan SR. 2005. Activation of innate defense against a paramyxovirus is mediated by RIG-I and TLR7 and TLR8 in a cell-type-specific manner. J. Virol. 79:12944-12951. http://dx.doi.org/10.1128/JVI.79.20.12944-12951.2005.
    • (2005) J. Virol. , vol.79 , pp. 12944-12951
    • Melchjorsen, J.1    Jensen, S.B.2    Malmgaard, L.3    Rasmussen, S.B.4    Weber, F.5    Bowie, A.G.6    Matikainen, S.7    Paludan, S.R.8
  • 17
    • 80052143412 scopus 로고    scopus 로고
    • RIG-I-like receptors: cytoplasmic sensors for non-self RNA
    • Kato H, Takahasi K, Fujita T. 2011. RIG-I-like receptors: cytoplasmic sensors for non-self RNA. Immunol. Rev. 243:91-98. http://dx.doi.org/10.1111/j.1600-065X.2011.01052.x.
    • (2011) Immunol. Rev. , vol.243 , pp. 91-98
    • Kato, H.1    Takahasi, K.2    Fujita, T.3
  • 19
    • 31344461659 scopus 로고    scopus 로고
    • Innate immune recognition of viral infection
    • Kawai T, Akira S. 2006. Innate immune recognition of viral infection. Nat. Immunol. 7:131-137. http://dx.doi.org/10.1038/ni1303.
    • (2006) Nat. Immunol. , vol.7 , pp. 131-137
    • Kawai, T.1    Akira, S.2
  • 20
    • 84883324602 scopus 로고    scopus 로고
    • A distinct role of Riplet-mediated K63-linked polyubiquitination of the RIG-I repressor domain in human antiviral innate immune responses
    • Oshiumi H, Miyashita M, Matsumoto M, Seya T. 2013. A distinct role of Riplet-mediated K63-linked polyubiquitination of the RIG-I repressor domain in human antiviral innate immune responses. PLoS Pathog. 9:e1003533. http://dx.doi.org/10.1371/journal.ppat.1003533.
    • (2013) PLoS Pathog. , vol.9
    • Oshiumi, H.1    Miyashita, M.2    Matsumoto, M.3    Seya, T.4
  • 23
    • 77951708374 scopus 로고    scopus 로고
    • Reconstitution of the RIG-I pathway reveals a signaling role of unanchored polyubiquitin chains in innate immunity
    • Zeng W, Sun L, Jiang X, Chen X, Hou F, Adhikari A, Xu M, Chen ZJ. 2010. Reconstitution of the RIG-I pathway reveals a signaling role of unanchored polyubiquitin chains in innate immunity. Cell 141:315-330. http://dx.doi.org/10.1016/j.cell.2010.03.029.
    • (2010) Cell , vol.141 , pp. 315-330
    • Zeng, W.1    Sun, L.2    Jiang, X.3    Chen, X.4    Hou, F.5    Adhikari, A.6    Xu, M.7    Chen, Z.J.8
  • 24
    • 33646555810 scopus 로고    scopus 로고
    • Type 1 interferons and the virus-host relationship: a lesson in détente
    • García-Sastre A, Biron CA. 2006. Type 1 interferons and the virus-host relationship: a lesson in détente. Science 312:879-882. http://dx.doi.org/10.1126/science.1125676.
    • (2006) Science , vol.312 , pp. 879-882
    • García-Sastre, A.1    Biron, C.A.2
  • 25
    • 29144501207 scopus 로고    scopus 로고
    • The interferon response circuit: induction and suppression by pathogenic viruses
    • Haller O, Kochs G, Weber F. 2006. The interferon response circuit: induction and suppression by pathogenic viruses. Virology 344:119-130. http://dx.doi.org/10.1016/j.virol.2005.09.024.
    • (2006) Virology , vol.344 , pp. 119-130
    • Haller, O.1    Kochs, G.2    Weber, F.3
  • 26
    • 0035895227 scopus 로고    scopus 로고
    • Bunyamwera bunyavirus nonstructural protein NSs is a nonessential gene product that contributes to viral pathogenesis
    • Bridgen A, Weber F, Fazakerley JK, Elliott RM. 2001. Bunyamwera bunyavirus nonstructural protein NSs is a nonessential gene product that contributes to viral pathogenesis. Proc. Natl. Acad. Sci. U. S. A. 98:664-669. http://dx.doi.org/10.1073/pnas.98.2.664.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 664-669
    • Bridgen, A.1    Weber, F.2    Fazakerley, J.K.3    Elliott, R.M.4
  • 28
    • 77957554950 scopus 로고    scopus 로고
    • Bunyaviruses and the type I interferon system
    • Elliott RM, Weber F. 2009. Bunyaviruses and the type I interferon system. Viruses 1:1003-1021. http://dx.doi.org/10.3390/v1031003.
    • (2009) Viruses , vol.1 , pp. 1003-1021
    • Elliott, R.M.1    Weber, F.2
  • 29
    • 70350435722 scopus 로고    scopus 로고
    • Dual functions of Rift Valley fever virus NSs protein: inhibition of host mRNA transcription and post-transcriptional downregulation of protein kinase PKR
    • Ikegami T, Narayanan K, Won S, Kamitani W, Peters CJ, Makino S. 2009. Dual functions of Rift Valley fever virus NSs protein: inhibition of host mRNA transcription and post-transcriptional downregulation of protein kinase PKR. Ann. N. Y. Acad. Sci. 1171(Suppl. 1):E75-E85. http://dx.doi.org/10.1111/j.1749-6632.2009.05054.x.
    • (2009) Ann. N. Y. Acad. Sci. , vol.1171 , Issue.SUPPL. 1
    • Ikegami, T.1    Narayanan, K.2    Won, S.3    Kamitani, W.4    Peters, C.J.5    Makino, S.6
  • 31
    • 1342264311 scopus 로고    scopus 로고
    • TFIIH transcription factor, a target for the Rift Valley hemorrhagic fever virus
    • Le May N, Dubaele S, Proietti De Santis L, Billecocq A, Bouloy M, Egly JM. 2004. TFIIH transcription factor, a target for the Rift Valley hemorrhagic fever virus. Cell 116:541-550. http://dx.doi.org/10.1016/S0092-8674(04)00132-1.
    • (2004) Cell , vol.116 , pp. 541-550
    • Le May, N.1    Dubaele, S.2    Proietti De Santis, L.3    Billecocq, A.4    Bouloy, M.5    Egly, J.M.6
  • 32
    • 66149086445 scopus 로고    scopus 로고
    • NSs protein of Rift Valley fever virus induces the specific degradation of the double-stranded RNAdependent protein kinase
    • Habjan M, Pichlmair A, Elliott RM, Overby AK, Glatter T, Gstaiger M, Superti-Furga G, Unger H, Weber F. 2009. NSs protein of Rift Valley fever virus induces the specific degradation of the double-stranded RNAdependent protein kinase. J. Virol. 83:4365-4375. http://dx.doi.org/10.1128/JVI.02148-08.
    • (2009) J. Virol. , vol.83 , pp. 4365-4375
    • Habjan, M.1    Pichlmair, A.2    Elliott, R.M.3    Overby, A.K.4    Glatter, T.5    Gstaiger, M.6    Superti-Furga, G.7    Unger, H.8    Weber, F.9
  • 33
    • 61449213995 scopus 로고    scopus 로고
    • Rift Valley fever virus NSs protein promotes post-transcriptional downregulation of protein kinase PKR and inhibits eIF2alpha phosphorylation
    • Ikegami T, Narayanan K, Won S, Kamitani W, Peters CJ, Makino S. 2009. Rift Valley fever virus NSs protein promotes post-transcriptional downregulation of protein kinase PKR and inhibits eIF2alpha phosphorylation. PLoS Pathog. 5:e1000287. http://dx.doi.org/10.1371/journal.ppat.1000287.
    • (2009) PLoS Pathog. , vol.5
    • Ikegami, T.1    Narayanan, K.2    Won, S.3    Kamitani, W.4    Peters, C.J.5    Makino, S.6
  • 34
    • 80052073169 scopus 로고    scopus 로고
    • NSs protein of Rift Valley fever virus promotes posttranslational downregulation of the TFIIH subunit p62
    • Kalveram B, Lihoradova O, Ikegami T. 2011. NSs protein of Rift Valley fever virus promotes posttranslational downregulation of the TFIIH subunit p62. J. Virol. 85:6234-6243. http://dx.doi.org/10.1128/JVI.02255-10.
    • (2011) J. Virol. , vol.85 , pp. 6234-6243
    • Kalveram, B.1    Lihoradova, O.2    Ikegami, T.3
  • 41
    • 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
  • 44
    • 84883487585 scopus 로고    scopus 로고
    • ATPase-driven oligomerization of RIG-I on RNA allows optimal activation of type-I interferon
    • Patel JR, Jain A, Chou YY, Baum A, Ha T, García-Sastre A. 2013. ATPase-driven oligomerization of RIG-I on RNA allows optimal activation of type-I interferon. EMBO Rep. 14:780-787. http://dx.doi.org/10.1038/embor.2013.102.
    • (2013) EMBO Rep. , vol.14 , pp. 780-787
    • Patel, J.R.1    Jain, A.2    Chou, Y.Y.3    Baum, A.4    Ha, T.5    García-Sastre, A.6
  • 45
    • 34247137987 scopus 로고    scopus 로고
    • Capsid protein of eastern equine encephalitis virus inhibits host cell gene expression
    • Aguilar PV, Weaver SC, Basler CF. 2007. Capsid protein of eastern equine encephalitis virus inhibits host cell gene expression. J. Virol. 81: 3866-3876. http://dx.doi.org/10.1128/JVI.02075-06.
    • (2007) J. Virol. , vol.81 , pp. 3866-3876
    • Aguilar, P.V.1    Weaver, S.C.2    Basler, C.F.3
  • 49
    • 33646748294 scopus 로고    scopus 로고
    • Ebola virus VP35 protein binds double-stranded RNA and inhibits alpha/beta interferon production in-duced by RIG-I signaling
    • Cárdenas WB, Loo YM, Gale M, Hartman AL, Kimberlin CR, Martínez-Sobrido L, Saphire EO, Basler CF. 2006. Ebola virus VP35 protein binds double-stranded RNA and inhibits alpha/beta interferon production in-duced by RIG-I signaling. J. Virol. 80:5168-5178. http://dx.doi.org/10.1128/JVI.02199-05.
    • (2006) J. Virol. , vol.80 , pp. 5168-5178
    • Cárdenas, W.B.1    Loo, Y.M.2    Gale, M.3    Hartman, A.L.4    Kimberlin, C.R.5    Martínez-Sobrido, L.6    Saphire, E.O.7    Basler, C.F.8
  • 50
    • 63149113399 scopus 로고    scopus 로고
    • Ebola virus protein VP35 impairs the function of interferon regulatory factor-activating kinases IKKepsilon and TBK-1
    • Prins KC, Cárdenas WB, Basler CF. 2009. Ebola virus protein VP35 impairs the function of interferon regulatory factor-activating kinases IKKepsilon and TBK-1. J. Virol. 83:3069-3077. http://dx.doi.org/10.1128/JVI.01875-08.
    • (2009) J. Virol. , vol.83 , pp. 3069-3077
    • Prins, K.C.1    Cárdenas, W.B.2    Basler, C.F.3
  • 51
    • 0035808446 scopus 로고    scopus 로고
    • Identification of distinct signaling pathways leading to the phosphorylation of interferon regulatory factor 3
    • Servant MJ, ten Oever B, LePage C, Conti L, Gessani S, Julkunen I, Lin R, Hiscott J. 2001. Identification of distinct signaling pathways leading to the phosphorylation of interferon regulatory factor 3. J. Biol. Chem. 276: 355-363. http://dx.doi.org/10.1074/jbc. M007790200.
    • (2001) J. Biol. Chem. , vol.276 , pp. 355-363
    • Servant, M.J.1    ten Oever, B.2    LePage, C.3    Conti, L.4    Gessani, S.5    Julkunen, I.6    Lin, R.7    Hiscott, J.8
  • 52
    • 0031932892 scopus 로고    scopus 로고
    • Interferon regulatory factor 3 and CREB-binding protein/p300 are subunits of double-stranded RNAactivated transcription factor DRAF1
    • Weaver BK, Kumar KP, Reich NC. 1998. Interferon regulatory factor 3 and CREB-binding protein/p300 are subunits of double-stranded RNAactivated transcription factor DRAF1. Mol. Cell. Biol. 18:1359-1368.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1359-1368
    • Weaver, B.K.1    Kumar, K.P.2    Reich, N.C.3
  • 53
    • 33745785300 scopus 로고    scopus 로고
    • Visualization of molecular interactions by fluorescence complementation
    • Kerppola TK. 2006. Visualization of molecular interactions by fluorescence complementation. Nat. Rev. Mol. Cell Biol. 7:449-456. http://dx.doi.org/10.1038/nrm1929.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 449-456
    • Kerppola, T.K.1
  • 54
    • 42349086670 scopus 로고    scopus 로고
    • Modification of intracellular membrane structures for virus replication
    • Miller S, Krijnse-Locker J. 2008. Modification of intracellular membrane structures for virus replication. Nat. Rev. Microbiol. 6:363-374. http://dx.doi.org/10.1038/nrmicro1890.
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 363-374
    • Miller, S.1    Krijnse-Locker, J.2
  • 55
    • 0020085816 scopus 로고
    • Inhibition of La Crosse virus replication by monensin, monovalent ionophore
    • Cash P. 1982. Inhibition of La Crosse virus replication by monensin, monovalent ionophore. J. Gen. Virol. 59:193-196. http://dx.doi.org/10.1099/0022-1317-59-1-193.
    • (1982) J. Gen. Virol. , vol.59 , pp. 193-196
    • Cash, P.1
  • 56
    • 0027248391 scopus 로고
    • Expression of the Bunyamwera virus M genome segment and intracellular localization of NSm
    • Nakitare GW, Elliott RM. 1993. Expression of the Bunyamwera virus M genome segment and intracellular localization of NSm. Virology 195:511-520. http://dx.doi.org/10.1006/viro.1993.1402.
    • (1993) Virology , vol.195 , pp. 511-520
    • Nakitare, G.W.1    Elliott, R.M.2
  • 57
    • 0028618252 scopus 로고
    • Localization of Bunyamwera bunyavirus G1 glycoprotein to the Golgi requires association with G2 but not with NSm
    • Lappin DF, Nakitare GW, Palfreyman JW, Elliott RM. 1994. Localization of Bunyamwera bunyavirus G1 glycoprotein to the Golgi requires association with G2 but not with NSm. J. Gen. Virol. 75(Pt 12):3441-3451. http://dx.doi.org/10.1099/0022-1317-75-12-3441.
    • (1994) J. Gen. Virol. , vol.75 , Issue.PART 12 , pp. 3441-3451
    • Lappin, D.F.1    Nakitare, G.W.2    Palfreyman, J.W.3    Elliott, R.M.4
  • 59
    • 0034279791 scopus 로고    scopus 로고
    • Biogenesis of the sorting endosome: the role of Rab5
    • Woodman PG. 2000. Biogenesis of the sorting endosome: the role of Rab5. Traffic 1:695-701. http://dx.doi.org/10.1034/j.1600-0854.2000.010902.x.
    • (2000) Traffic , vol.1 , pp. 695-701
    • Woodman, P.G.1
  • 60
    • 34247559591 scopus 로고    scopus 로고
    • Participation of Rab5, an early endosome protein, in hepatitis C virus RNA replication machinery
    • Stone M, Jia S, Heo WD, Meyer T, Konan KV. 2007. Participation of Rab5, an early endosome protein, in hepatitis C virus RNA replication machinery. J. Virol. 81:4551-4563. http://dx.doi.org/10.1128/JVI.01366-06.
    • (2007) J. Virol. , vol.81 , pp. 4551-4563
    • Stone, M.1    Jia, S.2    Heo, W.D.3    Meyer, T.4    Konan, K.V.5
  • 61
    • 84870691165 scopus 로고    scopus 로고
    • Bovine ephemeral fever virus uses a clathrin-mediated and dynamin 2-dependent endocytosis pathway that requires Rab5 and Rab7 as well as microtubules
    • Cheng CY, Shih WL, Huang WR, Chi PI, Wu MH, Liu HJ. 2012. Bovine ephemeral fever virus uses a clathrin-mediated and dynamin 2-dependent endocytosis pathway that requires Rab5 and Rab7 as well as microtubules. J. Virol. 86:13653-13661. http://dx.doi.org/10.1128/JVI.01073-12.
    • (2012) J. Virol. , vol.86 , pp. 13653-13661
    • Cheng, C.Y.1    Shih, W.L.2    Huang, W.R.3    Chi, P.I.4    Wu, M.H.5    Liu, H.J.6
  • 62
    • 80052249258 scopus 로고    scopus 로고
    • Cell entry of avian reovirus follows a caveolin-1-mediated and dynamin-2-dependent endocytic pathway that requires activation of p38 mitogen-activated protein kinase (MAPK) and Src signaling pathways as well as microtubules and small GTPase Rab5 protein
    • Huang WR, Wang YC, Chi PI, Wang L, Wang CY, Lin CH, Liu HJ. 2011. Cell entry of avian reovirus follows a caveolin-1-mediated and dynamin-2-dependent endocytic pathway that requires activation of p38 mitogen-activated protein kinase (MAPK) and Src signaling pathways as well as microtubules and small GTPase Rab5 protein. J. Biol. Chem. 286: 30780-30794. http://dx.doi.org/10.1074/jbc. M111.257154.
    • (2011) J. Biol. Chem. , vol.286 , pp. 30780-30794
    • Huang, W.R.1    Wang, Y.C.2    Chi, P.I.3    Wang, L.4    Wang, C.Y.5    Lin, C.H.6    Liu, H.J.7
  • 65
    • 0034986111 scopus 로고    scopus 로고
    • The Rab GTPase family
    • REVIEWS3007
    • Stenmark H, Olkkonen VM. 2001. The Rab GTPase family. Genome Biol. 2:REVIEWS3007. http://dx.doi.org/10.1186/gb-2001-2-5-reviews3007.
    • (2001) Genome Biol. , vol.2
    • Stenmark, H.1    Olkkonen, V.M.2
  • 70
    • 77953524763 scopus 로고    scopus 로고
    • Autophagy takes an alternative pathway
    • Shimizu S, Arakawa S, Nishida Y. 2010. Autophagy takes an alternative pathway. Autophagy 6:290-291. http://dx.doi.org/10.4161/auto.6.2.11127.
    • (2010) Autophagy , vol.6 , pp. 290-291
    • Shimizu, S.1    Arakawa, S.2    Nishida, Y.3
  • 71
    • 77957685199 scopus 로고    scopus 로고
    • Autophagy-independent LC3 function in vesicular traffic
    • de Haan CA, Molinari M, Reggiori F. 2010. Autophagy-independent LC3 function in vesicular traffic. Autophagy 6:994-996. http://dx.doi.org/10.4161/auto.6.7.13309.
    • (2010) Autophagy , vol.6 , pp. 994-996
    • de Haan, C.A.1    Molinari, M.2    Reggiori, F.3
  • 72
    • 80053315490 scopus 로고    scopus 로고
    • Unconventional use of LC3 by coronaviruses through the alleged subversion of the ERAD tuning pathway
    • Reggiori F, de Haan CA, Molinari M. 2011. Unconventional use of LC3 by coronaviruses through the alleged subversion of the ERAD tuning pathway. Viruses 3:1610-1623. http://dx.doi.org/10.3390/v3091610.
    • (2011) Viruses , vol.3 , pp. 1610-1623
    • Reggiori, F.1    de Haan, C.A.2    Molinari, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.