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Volumn 47, Issue 3, 2015, Pages 149-155

Regulation of cellular innate antiviral signaling by ubiquitin modification

Author keywords

Cellular innate antiviral signaling; Pattern recognition receptor; Ubiquitin modification

Indexed keywords

DEUBIQUITINASE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERFERON REGULATORY FACTOR 3; IRF3 PROTEIN, HUMAN; PATHOGEN ASSOCIATED MOLECULAR PATTERN; PATTERN RECOGNITION RECEPTOR; TOLL LIKE RECEPTOR;

EID: 84941559613     PISSN: 16729145     EISSN: 17457270     Source Type: Journal    
DOI: 10.1093/abbs/gmu133     Document Type: Review
Times cited : (13)

References (102)
  • 1
    • 77950343791 scopus 로고    scopus 로고
    • Pattern recognition receptors and inflammation
    • Takeuchi O, Akira S. Pattern recognition receptors and inflammation. Cell 2010, 140: 805-820.
    • (2010) Cell , vol.140 , pp. 805-820
    • Takeuchi, O.1    Akira, S.2
  • 2
    • 46249115827 scopus 로고    scopus 로고
    • Interferon-inducible antiviral effectors
    • Sadler AJ, Williams BR. Interferon-inducible antiviral effectors. Nat Rev Immunol 2008, 8: 559-568.
    • (2008) Nat Rev Immunol , vol.8 , pp. 559-568
    • Sadler, A.J.1    Williams, B.R.2
  • 3
    • 0034698739 scopus 로고    scopus 로고
    • Immune cell activation by bacterial CpG-DNA through myeloid differentiation marker 88 and tumor necrosis factor receptor-associated factor (TRAF) 6
    • Hacker H, Vabulas RM, Takeuchi O, Hoshino K, Akira S, Wagner H. Immune cell activation by bacterial CpG-DNA through myeloid differentiation marker 88 and tumor necrosis factor receptor-associated factor (TRAF) 6. J Exp Med 2000, 192: 595-600.
    • (2000) J Exp Med , vol.192 , pp. 595-600
    • Hacker, H.1    Vabulas, R.M.2    Takeuchi, O.3    Hoshino, K.4    Akira, S.5    Wagner, H.6
  • 5
    • 0034699340 scopus 로고    scopus 로고
    • Recognition of CpG DNA is mediated by signaling pathways dependent on the adaptor protein MyD88
    • Schnare M, Holt AC, Takeda K, Akira S, Medzhitov R. Recognition of CpG DNA is mediated by signaling pathways dependent on the adaptor protein MyD88. Curr Biol 2000, 10: 1139-1142.
    • (2000) Curr Biol , vol.10 , pp. 1139-1142
    • Schnare, M.1    Holt, A.C.2    Takeda, K.3    Akira, S.4    Medzhitov, R.5
  • 6
    • 0043176281 scopus 로고    scopus 로고
    • Role of adaptor TRIF in the MyD88-independent tolllike receptor signaling pathway
    • Yamamoto M, Sato S, Hemmi H, Hoshino K, Kaisho T, Sanjo H, Takeuchi O, et al. Role of adaptor TRIF in the MyD88-independent tolllike receptor signaling pathway. Science 2003, 301: 640-643.
    • (2003) Science , vol.301 , pp. 640-643
    • Yamamoto, M.1    Sato, S.2    Hemmi, H.3    Hoshino, K.4    Kaisho, T.5    Sanjo, H.6    Takeuchi, O.7
  • 7
    • 0035909372 scopus 로고    scopus 로고
    • Recognition of double-stranded RNA and activation of NF-kappaB by Toll-like receptor 3
    • Alexopoulou L, Holt AC, Medzhitov R, Flavell RA. Recognition of double-stranded RNA and activation of NF-kappaB by Toll-like receptor 3. Nature 2001, 413: 732-738.
    • (2001) Nature , vol.413 , pp. 732-738
    • Alexopoulou, L.1    Holt, A.C.2    Medzhitov, R.3    Flavell, R.A.4
  • 8
    • 0036008014 scopus 로고    scopus 로고
    • Small anti-viral compounds activate immune cells via the TLR7 MyD88-dependent signaling pathway
    • Hemmi H, Kaisho T, Takeuchi O, Sato S, Sanjo H, Hoshino K, Horiuchi T, et al. Small anti-viral compounds activate immune cells via the TLR7 MyD88-dependent signaling pathway. Nat Immunol 2002, 3: 196-200.
    • (2002) Nat Immunol , vol.3 , pp. 196-200
    • Hemmi, H.1    Kaisho, T.2    Takeuchi, O.3    Sato, S.4    Sanjo, H.5    Hoshino, K.6    Horiuchi, T.7
  • 9
    • 10344259136 scopus 로고    scopus 로고
    • The V proteins of paramyxoviruses bind the IFN-inducible RNA helicase, mda-5, and inhibit its activation of the IFN-beta promoter
    • Andrejeva J, Childs KS, Young DF, Carlos TS, Stock N, Goodbourn S, Randall RE. The V proteins of paramyxoviruses bind the IFN-inducible RNA helicase, mda-5, and inhibit its activation of the IFN-beta promoter. Proc Natl Acad Sci USA 2004, 101: 17264-17269.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 17264-17269
    • Andrejeva, J.1    Childs, K.S.2    Young, D.F.3    Carlos, T.S.4    Stock, N.5    Goodbourn, S.6    Randall, R.E.7
  • 10
    • 3242813113 scopus 로고    scopus 로고
    • The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses
    • Yoneyama M, Kikuchi M, Natsukawa T, Shinobu N, Imaizumi T, Miyagishi M, Taira K, et al. The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses. Nat Immunol 2004, 5: 730-737.
    • (2004) Nat Immunol , vol.5 , pp. 730-737
    • Yoneyama, M.1    Kikuchi, M.2    Natsukawa, T.3    Shinobu, N.4    Imaizumi, T.5    Miyagishi, M.6    Taira, K.7
  • 11
    • 27144440523 scopus 로고    scopus 로고
    • IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction
    • Kawai T, Takahashi K, Sato S, Coban C, Kumar H, Kato H, Ishii KJ, et al. IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction. Nat Immunol 2005, 6: 981-988.
    • (2005) Nat Immunol , vol.6 , pp. 981-988
    • Kawai, T.1    Takahashi, K.2    Sato, S.3    Coban, C.4    Kumar, H.5    Kato, H.6    Ishii, K.J.7
  • 12
    • 27144440476 scopus 로고    scopus 로고
    • Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus
    • Meylan E, Curran J, Hofmann K, Moradpour D, Binder M, Bartenschlager R, Tschopp J. Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus. Nature 2005, 437: 1167-1172.
    • (2005) Nature , vol.437 , pp. 1167-1172
    • Meylan, E.1    Curran, J.2    Hofmann, K.3    Moradpour, D.4    Binder, M.5    Bartenschlager, R.6    Tschopp, J.7
  • 13
    • 24144461689 scopus 로고    scopus 로고
    • Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-kappaB and IRF 3
    • Seth RB, Sun L, Ea CK, Chen ZJ. Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-kappaB and IRF 3. Cell 2005, 122: 669-682.
    • (2005) Cell , vol.122 , pp. 669-682
    • Seth, R.B.1    Sun, L.2    Ea, C.K.3    Chen, Z.J.4
  • 14
    • 24944538819 scopus 로고    scopus 로고
    • VISA is an adapter protein required for virus-triggered IFN-beta signaling
    • Xu LG, Wang YY, Han KJ, Li LY, Zhai Z, Shu HB. VISA is an adapter protein required for virus-triggered IFN-beta signaling. Mol Cell 2005, 19: 727-740.
    • (2005) Mol Cell , vol.19 , pp. 727-740
    • Xu, L.G.1    Wang, Y.Y.2    Han, K.J.3    Li, L.Y.4    Zhai, Z.5    Shu, H.B.6
  • 15
    • 53349178089 scopus 로고    scopus 로고
    • STING is an endoplasmic reticulum adaptor that facilitates innate immune signalling
    • Ishikawa H, Barber GN. STING is an endoplasmic reticulum adaptor that facilitates innate immune signalling. Nature 2008, 455: 674-678.
    • (2008) Nature , vol.455 , pp. 674-678
    • Ishikawa, H.1    Barber, G.N.2
  • 16
    • 53349168904 scopus 로고    scopus 로고
    • The adaptor protein MITA links virus-sensing receptors to IRF3 transcription factor activation
    • Zhong B, Yang Y, Li S, Wang YY, Li Y, Diao F, Lei C, et al. The adaptor protein MITA links virus-sensing receptors to IRF3 transcription factor activation. Immunity 2008, 29: 538-550.
    • (2008) Immunity , vol.29 , pp. 538-550
    • Zhong, B.1    Yang, Y.2    Li, S.3    Wang, Y.Y.4    Li, Y.5    Diao, F.6    Lei, C.7
  • 17
    • 84873711885 scopus 로고    scopus 로고
    • Cyclic GMP-AMP synthase is a cytosolic DNA sensor that activates the type I interferon pathway
    • Sun L, Wu J, Du F, Chen X, Chen ZJ. Cyclic GMP-AMP synthase is a cytosolic DNA sensor that activates the type I interferon pathway. Science 2013, 339: 786-791.
    • (2013) Science , vol.339 , pp. 786-791
    • Sun, L.1    Wu, J.2    Du, F.3    Chen, X.4    Chen, Z.J.5
  • 18
    • 70349459734 scopus 로고    scopus 로고
    • RIG-I-dependent sensing of poly (dA:dT) through the induction of an RNA polymerase III-transcribed RNA intermediate
    • Ablasser A, Bauernfeind F, Hartmann G, Latz E, Fitzgerald KA, Hornung V. RIG-I-dependent sensing of poly (dA:dT) through the induction of an RNA polymerase III-transcribed RNA intermediate. Nat Immunol 2009, 10: 1065-1072.
    • (2009) Nat Immunol , vol.10 , pp. 1065-1072
    • Ablasser, A.1    Bauernfeind, F.2    Hartmann, G.3    Latz, E.4    Fitzgerald, K.A.5    Hornung, V.6
  • 19
    • 68049092912 scopus 로고    scopus 로고
    • RNA polymerase III detects cytosolic DNA and induces type I interferons through the RIG-I pathway
    • Chiu YH, Macmillan JB, Chen ZJ. RNA polymerase III detects cytosolic DNA and induces type I interferons through the RIG-I pathway.Cell 2009, 138: 576-591.
    • (2009) Cell , vol.138 , pp. 576-591
    • Chiu, Y.H.1    Macmillan, J.B.2    Chen, Z.J.3
  • 21
    • 84869403247 scopus 로고    scopus 로고
    • The helicase DDX41 recognizes the bacterial secondary messengers cyclic di-GMP and cyclic di-AMP to activate a type I interferon immune response
    • Parvatiyar K, Zhang Z, Teles RM, Ouyang S, Jiang Y, Iyer SS, Zaver SA, et al. The helicase DDX41 recognizes the bacterial secondary messengers cyclic di-GMP and cyclic di-AMP to activate a type I interferon immune response. Nat Immunol 2012, 13: 1155-1161.
    • (2012) Nat Immunol , vol.13 , pp. 1155-1161
    • Parvatiyar, K.1    Zhang, Z.2    Teles, R.M.3    Ouyang, S.4    Jiang, Y.5    Iyer, S.S.6    Zaver, S.A.7
  • 22
    • 84863962538 scopus 로고    scopus 로고
    • LSm14A is a processing body-associated sensor of viral nucleic acids that initiates cellular antiviral response in the early phase of viral infection
    • Li Y, Chen R, Zhou Q, Xu Z, Li C, Wang S, Mao A, et al. LSm14A is a processing body-associated sensor of viral nucleic acids that initiates cellular antiviral response in the early phase of viral infection. Proc Natl Acad Sci USA 2012, 109: 11770-11775.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 11770-11775
    • Li, Y.1    Chen, R.2    Zhou, Q.3    Xu, Z.4    Li, C.5    Wang, S.6    Mao, A.7
  • 23
    • 34547143110 scopus 로고    scopus 로고
    • DAI (DLM-1/ZBP1) is a cytosolic DNA sensor and an activator of innate immune response
    • Takaoka A, Wang Z, Choi MK, Yanai H, Negishi H, Ban T, Lu Y, et al. DAI (DLM-1/ZBP1) is a cytosolic DNA sensor and an activator of innate immune response. Nature 2007, 448: 501-505.
    • (2007) Nature , vol.448 , pp. 501-505
    • Takaoka, A.1    Wang, Z.2    Choi, M.K.3    Yanai, H.4    Negishi, H.5    Ban, T.6    Lu, Y.7
  • 24
    • 4344566281 scopus 로고    scopus 로고
    • The roles of two IkappaB kinase-related kinases in lipopolysaccharide and double stranded RNA signaling and viral infection
    • Hemmi H, Takeuchi O, Sato S, Yamamoto M, Kaisho T, Sanjo H, Kawai T, et al. The roles of two IkappaB kinase-related kinases in lipopolysaccharide and double stranded RNA signaling and viral infection. J Exp Med 2004, 199: 1641-1650.
    • (2004) J Exp Med , vol.199 , pp. 1641-1650
    • Hemmi, H.1    Takeuchi, O.2    Sato, S.3    Yamamoto, M.4    Kaisho, T.5    Sanjo, H.6    Kawai, T.7
  • 25
    • 3042647375 scopus 로고    scopus 로고
    • Differential requirement for TANK-binding kinase-1 in type I interferon responses to toll-like receptor activation and viral infection
    • Perry AK, Chow EK, Goodnough JB, Yeh WC, Cheng G. Differential requirement for TANK-binding kinase-1 in type I interferon responses to toll-like receptor activation and viral infection. J Exp Med 2004, 199: 1651-1658.
    • (2004) J Exp Med , vol.199 , pp. 1651-1658
    • Perry, A.K.1    Chow, E.K.2    Goodnough, J.B.3    Yeh, W.C.4    Cheng, G.5
  • 26
    • 84899125841 scopus 로고    scopus 로고
    • Recruitment of phosphatase PP2A by RACK1 adaptor protein deactivates transcription factor IRF3 and limits type I interferon signaling
    • Long L, Deng Y, Yao F, Guan D, Feng Y, Jiang H, Li X, et al. Recruitment of phosphatase PP2A by RACK1 adaptor protein deactivates transcription factor IRF3 and limits type I interferon signaling. Immunity 2014, 40: 515-529.
    • (2014) Immunity , vol.40 , pp. 515-529
    • Long, L.1    Deng, Y.2    Yao, F.3    Guan, D.4    Feng, Y.5    Jiang, H.6    Li, X.7
  • 28
    • 68049084674 scopus 로고    scopus 로고
    • Breaking the chains: Structure and function of the deubiquitinases
    • Komander D, Clague MJ, Urbe S. Breaking the chains: Structure and function of the deubiquitinases. Nat Rev Mol Cell Biol 2009, 10: 550-563.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 550-563
    • Komander, D.1    Clague, M.J.2    Urbe, S.3
  • 29
    • 30544451546 scopus 로고    scopus 로고
    • Specificity in Toll-like receptor signalling through distinct effector functions of TRAF3 and TRAF6
    • Hacker H, Redecke V, Blagoev B, Kratchmarova I, Hsu LC, Wang GG, Kamps MP, et al. Specificity in Toll-like receptor signalling through distinct effector functions of TRAF3 and TRAF6. Nature 2006, 439: 204-207.
    • (2006) Nature , vol.439 , pp. 204-207
    • Hacker, H.1    Redecke, V.2    Blagoev, B.3    Kratchmarova, I.4    Hsu, L.C.5    Wang, G.G.6    Kamps, M.P.7
  • 30
    • 30544447047 scopus 로고    scopus 로고
    • Critical role of TRAF3 in the Toll-like receptor-dependent and -independent antiviral response
    • Oganesyan G, Saha SK, Guo B, He JQ, Shahangian A, Zarnegar B, Perry A, et al. Critical role of TRAF3 in the Toll-like receptor-dependent and -independent antiviral response. Nature 2006, 439: 208-211.
    • (2006) Nature , vol.439 , pp. 208-211
    • Oganesyan, G.1    Saha, S.K.2    Guo, B.3    He, J.Q.4    Shahangian, A.5    Zarnegar, B.6    Perry, A.7
  • 31
    • 2442643942 scopus 로고    scopus 로고
    • Triad3A, an E3 ubiquitin-protein ligase regulating Toll-like receptors
    • Chuang TH, Ulevitch RJ. Triad3A, an E3 ubiquitin-protein ligase regulating Toll-like receptors. Nat Immunol 2004, 5: 495-502.
    • (2004) Nat Immunol , vol.5 , pp. 495-502
    • Chuang, T.H.1    Ulevitch, R.J.2
  • 32
    • 77951247349 scopus 로고    scopus 로고
    • Virus-triggered ubiquitination of TRAF3/6 by cIAP1/2 is essential for induction of interferon-beta (IFN-beta) and cellular antiviral response
    • Mao AP, Li S, Zhong B, Li Y, Yan J, Li Q, Teng C, et al. Virus-triggered ubiquitination of TRAF3/6 by cIAP1/2 is essential for induction of interferon-beta (IFN-beta) and cellular antiviral response. J Biol Chem 2010, 285: 9470-9476.
    • (2010) J Biol Chem , vol.285 , pp. 9470-9476
    • Mao, A.P.1    Li, S.2    Zhong, B.3    Li, Y.4    Yan, J.5    Li, Q.6    Teng, C.7
  • 33
    • 70349472923 scopus 로고    scopus 로고
    • Peli1 facilitates TRIF-dependent Toll-like receptor signaling and proinflammatory cytokine production
    • Chang M, JinW, Sun SC. Peli1 facilitates TRIF-dependent Toll-like receptor signaling and proinflammatory cytokine production. Nat Immunol 2009, 10: 1089-1095.
    • (2009) Nat Immunol , vol.10 , pp. 1089-1095
    • Chang, M.1    JinW Sun, S.C.2
  • 34
    • 84875549688 scopus 로고    scopus 로고
    • E3 ligase WWP2 negatively regulates TLR3-mediated innate immune response by targeting TRIF for ubiquitination and degradation
    • Yang Y, Liao B, Wang S, Yan B, Jin Y, Shu HB, Wang YY. E3 ligase WWP2 negatively regulates TLR3-mediated innate immune response by targeting TRIF for ubiquitination and degradation. Proc Natl Acad Sci USA 2013, 110: 5115-5120.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 5115-5120
    • Yang, Y.1    Liao, B.2    Wang, S.3    Yan, B.4    Jin, Y.5    Shu, H.B.6    Wang, Y.Y.7
  • 35
    • 84867308377 scopus 로고    scopus 로고
    • TRIM38 negatively regulates TLR3-mediated IFN-beta signaling by targeting TRIF for degradation
    • Xue Q, Zhou Z, Lei X, Liu X, He B,Wang J, Hung T. TRIM38 negatively regulates TLR3-mediated IFN-beta signaling by targeting TRIF for degradation. PLoS One 2012, 7: E46825.
    • (2012) PLoS One , vol.7 , pp. e46825
    • Xue, Q.1    Zhou, Z.2    Lei, X.3    Liu, X.4    He, B.5    Wang, J.6    Hung, T.7
  • 36
    • 67649229630 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase Nrdp1 'preferentially' promotes TLR-mediated production of type I interferon
    • Wang C, Chen T, Zhang J, Yang M, Li N, Xu X, Cao X. The E3 ubiquitin ligase Nrdp1 'preferentially' promotes TLR-mediated production of type I interferon. Nat Immunol 2009, 10: 744-752.
    • (2009) Nat Immunol , vol.10 , pp. 744-752
    • Wang, C.1    Chen, T.2    Zhang, J.3    Yang, M.4    Li, N.5    Xu, X.6    Cao, X.7
  • 37
    • 60749124538 scopus 로고    scopus 로고
    • Cytosolic viral sensor RIG-I is a 5'-triphosphate-dependent translocase on double-stranded RNA
    • Myong S, Cui S, Cornish PV, Kirchhofer A, Gack MU, Jung JU, Hopfner KP, et al. Cytosolic viral sensor RIG-I is a 5'-triphosphate-dependent translocase on double-stranded RNA. Science 2009, 323: 1070-1074.
    • (2009) Science , vol.323 , pp. 1070-1074
    • Myong, S.1    Cui, S.2    Cornish, P.V.3    Kirchhofer, A.4    Gack, M.U.5    Jung, J.U.6    Hopfner, K.P.7
  • 41
    • 68049089651 scopus 로고    scopus 로고
    • Recognition of 5' triphosphate by RIG-I helicase requires short blunt double-stranded RNA as contained in panhandle of negative-strand virus
    • Schlee M, Roth A, Hornung V, Hagmann CA, Wimmenauer V, BarchetW, Coch C, et al. Recognition of 5' triphosphate by RIG-I helicase requires short blunt double-stranded RNA as contained in panhandle of negative-strand virus. Immunity 2009, 31: 25-34.
    • (2009) Immunity , vol.31 , pp. 25-34
    • Schlee, M.1    Roth, A.2    Hornung, V.3    Hagmann, C.A.4    Wimmenauer, V.5    BarchetW Coch, C.6
  • 42
    • 46949097299 scopus 로고    scopus 로고
    • Length-dependent recognition of double-stranded ribonucleic acids by retinoic acid-inducible gene-I and melanoma differentiation-associated gene 5
    • Kato H, Takeuchi O, Mikamo-Satoh E, Hirai R, Kawai T, Matsushita K, Hiiragi A, et al. Length-dependent recognition of double-stranded ribonucleic acids by retinoic acid-inducible gene-I and melanoma differentiation-associated gene 5. J Exp Med 2008, 205: 1601-1610.
    • (2008) J Exp Med , vol.205 , pp. 1601-1610
    • Kato, H.1    Takeuchi, O.2    Mikamo-Satoh, E.3    Hirai, R.4    Kawai, T.5    Matsushita, K.6    Hiiragi, A.7
  • 44
    • 34247341367 scopus 로고    scopus 로고
    • TRIM25 RING-finger E3 ubiquitin ligase is essential for RIG-I-mediated antiviral activity
    • Gack MU, Shin YC, Joo CH, Urano T, Liang C, Sun L, Takeuchi O, et al. TRIM25 RING-finger E3 ubiquitin ligase is essential for RIG-I-mediated antiviral activity. Nature 2007, 446: 916-920.
    • (2007) Nature , vol.446 , pp. 916-920
    • Gack, M.U.1    Shin, Y.C.2    Joo, C.H.3    Urano, T.4    Liang, C.5    Sun, L.6    Takeuchi, O.7
  • 45
    • 78650189572 scopus 로고    scopus 로고
    • The ubiquitin ligase Riplet is essential for RIG-I-dependent innate immune responses to RNA virus infection
    • Oshiumi H, Miyashita M, Inoue N, Okabe M, Matsumoto M, Seya T. The ubiquitin ligase Riplet is essential for RIG-I-dependent innate immune responses to RNA virus infection. Cell Host Microbe 2010, 8: 496-509.
    • (2010) Cell Host Microbe , vol.8 , pp. 496-509
    • Oshiumi, H.1    Miyashita, M.2    Inoue, N.3    Okabe, M.4    Matsumoto, M.5    Seya, T.6
  • 46
    • 66749142359 scopus 로고    scopus 로고
    • REUL is a novel E3 ubiquitin ligase and stimulator of retinoic-acid-inducible gene-I
    • Gao D, Yang YK, Wang RP, Zhou X, Diao FC, Li MD, Zhai ZH, et al. REUL is a novel E3 ubiquitin ligase and stimulator of retinoic-acid-inducible gene-I. PLoS One 2009, 4: E5760.
    • (2009) PLoS One , vol.4 , pp. e5760
    • Gao, D.1    Yang, Y.K.2    Wang, R.P.3    Zhou, X.4    Diao, F.C.5    Li, M.D.6    Zhai, Z.H.7
  • 47
    • 84899698672 scopus 로고    scopus 로고
    • TRIM4 modulates type I interferon induction and cellular antiviral response by targeting RIG-I for K63-linked ubiquitination
    • Yan J, Li Q, Mao AP, Hu MM, Shu HB. TRIM4 modulates type I interferon induction and cellular antiviral response by targeting RIG-I for K63-linked ubiquitination. J Mol Cell Biol 2014, 6: 154-163.
    • (2014) J Mol Cell Biol , vol.6 , pp. 154-163
    • Yan, J.1    Li, Q.2    Mao, A.P.3    Hu, M.M.4    Shu, H.B.5
  • 49
    • 77951708374 scopus 로고    scopus 로고
    • Reconstitution of the RIG-I pathway reveals a signaling role of unanchored polyubiquitin chains in innate immunity
    • ZengW, Sun L, Jiang X, Chen X, Hou F, Adhikari A, Xu M, et al. Reconstitution of the RIG-I pathway reveals a signaling role of unanchored polyubiquitin chains in innate immunity. Cell 2010, 141: 315-330.
    • (2010) Cell , vol.141 , pp. 315-330
    • ZengW Sun, L.1    Jiang, X.2    Chen, X.3    Hou, F.4    Adhikari, A.5    Xu, M.6
  • 51
    • 84873320976 scopus 로고    scopus 로고
    • Induction of Siglec-G by RNA viruses inhibits the innate immune response by promoting RIG-I degradation
    • Chen W, Han C, Xie B, Hu X, Yu Q, Shi L, Wang Q, et al. Induction of Siglec-G by RNA viruses inhibits the innate immune response by promoting RIG-I degradation. Cell 2013, 152: 467-478.
    • (2013) Cell , vol.152 , pp. 467-478
    • Chen, W.1    Han, C.2    Xie, B.3    Hu, X.4    Yu, Q.5    Shi, L.6    Wang, Q.7
  • 52
    • 84894545130 scopus 로고    scopus 로고
    • Interferon-inducible protein IFI35 negatively regulates RIG-I antiviral signaling and supports vesicular stomatitis virus replication
    • Das A, Dinh PX, Panda D, Pattnaik AK. Interferon-inducible protein IFI35 negatively regulates RIG-I antiviral signaling and supports vesicular stomatitis virus replication. J Virol 2014, 88: 3103-3113.
    • (2014) J Virol , vol.88 , pp. 3103-3113
    • Das, A.1    Dinh, P.X.2    Panda, D.3    Pattnaik, A.K.4
  • 53
    • 79961133270 scopus 로고    scopus 로고
    • MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune response
    • Hou F, Sun L, Zheng H, Skaug B, Jiang QX, Chen ZJ. MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune response. Cell 2011, 146: 448-461.
    • (2011) Cell , vol.146 , pp. 448-461
    • Hou, F.1    Sun, L.2    Zheng, H.3    Skaug, B.4    Jiang, Q.X.5    Chen, Z.J.6
  • 54
    • 67649214539 scopus 로고    scopus 로고
    • Ubiquitin-regulated recruitment of IkappaB kinase epsilon to the MAVS interferon signaling adapter
    • Paz S, Vilasco M, Arguello M, Sun Q, Lacoste J, Nguyen TL, Zhao T, et al. Ubiquitin-regulated recruitment of IkappaB kinase epsilon to the MAVS interferon signaling adapter. Mol Cell Biol 2009, 29: 3401-3412.
    • (2009) Mol Cell Biol , vol.29 , pp. 3401-3412
    • Paz, S.1    Vilasco, M.2    Arguello, M.3    Sun, Q.4    Lacoste, J.5    Nguyen, T.L.6    Zhao, T.7
  • 55
    • 84861330800 scopus 로고    scopus 로고
    • MAVS ubiquitination by the E3 ligase TRIM25 and degradation by the proteasome is involved in type I interferon production after activation of the antiviral RIG-I-like receptors
    • Castanier C, Zemirli N, Portier A, Garcin D, Bidere N, Vazquez A, Arnoult D. MAVS ubiquitination by the E3 ligase TRIM25 and degradation by the proteasome is involved in type I interferon production after activation of the antiviral RIG-I-like receptors. BMC Biol 2012, 10: 44.
    • (2012) BMC Biol , vol.10 , pp. 44
    • Castanier, C.1    Zemirli, N.2    Portier, A.3    Garcin, D.4    Bidere, N.5    Vazquez, A.6    Arnoult, D.7
  • 56
    • 77953445772 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase RNF5 targets virus-induced signaling adaptor for ubiquitination and degradation
    • Zhong B, Zhang Y, Tan B, Liu TT, Wang YY, Shu HB. The E3 ubiquitin ligase RNF5 targets virus-induced signaling adaptor for ubiquitination and degradation. J Immunol 2010, 184: 6249-6255.
    • (2010) J Immunol , vol.184 , pp. 6249-6255
    • Zhong, B.1    Zhang, Y.2    Tan, B.3    Liu, T.T.4    Wang, Y.Y.5    Shu, H.B.6
  • 57
    • 70449726455 scopus 로고    scopus 로고
    • PCBP2 mediates degradation of the adaptor MAVS via the HECT ubiquitin ligase AIP 4
    • You F, Sun H, Zhou X, SunW, Liang S, Zhai Z, Jiang Z. PCBP2 mediates degradation of the adaptor MAVS via the HECT ubiquitin ligase AIP4. Nat Immunol 2009, 10: 1300-1308.
    • (2009) Nat Immunol , vol.10 , pp. 1300-1308
    • You, F.1    Sun, H.2    Zhou, X.3    SunW Liang, S.4    Zhai, Z.5    Jiang, Z.6
  • 58
    • 70449725290 scopus 로고    scopus 로고
    • Negative regulation of MAVS-mediated innate immune response by PSMA7
    • Jia Y, Song T, Wei C, Ni C, Zheng Z, Xu Q, Ma H, et al. Negative regulation of MAVS-mediated innate immune response by PSMA7. J Immunol 2009, 183: 4241-4248.
    • (2009) J Immunol , vol.183 , pp. 4241-4248
    • Jia, Y.1    Song, T.2    Wei, C.3    Ni, C.4    Zheng, Z.5    Xu, Q.6    Ma, H.7
  • 59
    • 84869748782 scopus 로고    scopus 로고
    • Ndfip1 negatively regulates RIG-I-dependent immune signaling by enhancing E3 ligase Smurf1-mediated MAVS degradation
    • Wang Y, Tong X, Ye X. Ndfip1 negatively regulates RIG-I-dependent immune signaling by enhancing E3 ligase Smurf1-mediated MAVS degradation. J Immunol 2012, 189: 5304-5313.
    • (2012) J Immunol , vol.189 , pp. 5304-5313
    • Wang, Y.1    Tong, X.2    Ye, X.3
  • 60
    • 84901260895 scopus 로고    scopus 로고
    • Smurf2 negatively modulates RIG-I-dependent antiviral response by targeting VISA/MAVS for ubiquitination and degradation
    • Pan Y, Li R, Meng JL, Mao HT, Zhang Y, Zhang J. Smurf2 negatively modulates RIG-I-dependent antiviral response by targeting VISA/MAVS for ubiquitination and degradation. J Immunol 2014, 192: 4758-4764.
    • (2014) J Immunol , vol.192 , pp. 4758-4764
    • Pan, Y.1    Li, R.2    Meng, J.L.3    Mao, H.T.4    Zhang, Y.5    Zhang, J.6
  • 61
    • 84882705934 scopus 로고    scopus 로고
    • MAVS recruits multiple ubiquitin E3 ligases to activate antiviral signaling cascades
    • Liu S, Chen J, Cai X, Wu J, Chen X, Wu YT, Sun L, et al. MAVS recruits multiple ubiquitin E3 ligases to activate antiviral signaling cascades. Elife 2013, 2: E00785.
    • (2013) Elife , vol.2 , pp. e00785
    • Liu, S.1    Chen, J.2    Cai, X.3    Wu, J.4    Chen, X.5    Wu, Y.T.6    Sun, L.7
  • 62
    • 73549097331 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase Triad3A negatively regulates the RIG-I/ MAVS signaling pathway by targeting TRAF3 for degradation
    • Nakhaei P, Mesplede T, Solis M, Sun Q, Zhao T, Yang L, Chuang TH, et al. The E3 ubiquitin ligase Triad3A negatively regulates the RIG-I/ MAVS signaling pathway by targeting TRAF3 for degradation. PLoS Pathog 2009, 5: E1000650.
    • (2009) PLoS Pathog , vol.5 , pp. e1000650
    • Nakhaei, P.1    Mesplede, T.2    Solis, M.3    Sun, Q.4    Zhao, T.5    Yang, L.6    Chuang, T.H.7
  • 63
    • 84875255449 scopus 로고    scopus 로고
    • RAD23A negatively regulates RIG-I/MDA5 signaling through promoting TRAF2 polyubiquitination and degradation
    • Fang DF,He K,Wang J, Mu R, Tan B, Jian Z, LiHY, et al. RAD23A negatively regulates RIG-I/MDA5 signaling through promoting TRAF2 polyubiquitination and degradation. Biochem Biophys Res Commun 2013, 431: 686-692.
    • (2013) Biochem Biophys Res Commun , vol.431 , pp. 686-692
    • Fang, D.F.1    He, K.2    Wang, J.3    Mu, R.4    Tan, B.5    Jian, Z.6    Li, H.Y.7
  • 64
    • 84907978513 scopus 로고    scopus 로고
    • Lysine 63-linked TANKbinding kinase 1 ubiquitination by mindbomb E3 ubiquitin protein ligase 2 is mediated by the mitochondrial antiviral signaling protein
    • Ye JS, Kim N, Lee KJ, Nam YR, Lee U, Joo CH. Lysine 63-linked TANKbinding kinase 1 ubiquitination by mindbomb E3 ubiquitin protein ligase 2 is mediated by the mitochondrial antiviral signaling protein. J Virol 2014, 88: 12765-12776.
    • (2014) J Virol , vol.88 , pp. 12765-12776
    • Ye, J.S.1    Kim, N.2    Lee, K.J.3    Nam, Y.R.4    Lee, U.5    Joo, C.H.6
  • 65
    • 84868554937 scopus 로고    scopus 로고
    • TRAF-interacting protein (TRIP) negatively regulates IFN-beta production and antiviral response by promoting proteasomal degradation of TANK-binding kinase 1
    • Zhang M, Wang L, Zhao X, Zhao K, Meng H, Zhao W, Gao C. TRAF-interacting protein (TRIP) negatively regulates IFN-beta production and antiviral response by promoting proteasomal degradation of TANK-binding kinase 1. J Exp Med 2012, 209: 1703-1711.
    • (2012) J Exp Med , vol.209 , pp. 1703-1711
    • Zhang, M.1    Wang, L.2    Zhao, X.3    Zhao, K.4    Meng, H.5    Zhao, W.6    Gao, C.7
  • 66
    • 84862815491 scopus 로고    scopus 로고
    • NLRP4 negatively regulates type I interferon signaling by targeting the kinase TBK1 for degradation via the ubiquitin ligase DTX4
    • Cui J, Li Y, Zhu L, Liu D, Songyang Z,WangHY,Wang RF. NLRP4 negatively regulates type I interferon signaling by targeting the kinase TBK1 for degradation via the ubiquitin ligase DTX4. Nat Immunol 2012, 13: 387-395.
    • (2012) Nat Immunol , vol.13 , pp. 387-395
    • Cui, J.1    Li, Y.2    Zhu, L.3    Liu, D.4    Songyang, Z.5    Wang, H.Y.6    Wang, R.F.7
  • 67
    • 84865119303 scopus 로고    scopus 로고
    • Linear ubiquitination of NEMO negatively regulates the interferon antiviral response through disruption of the MAVS-TRAF3 complex
    • Belgnaoui SM, Paz S, Samuel S, Goulet ML, Sun Q, Kikkert M, Iwai K, et al. Linear ubiquitination of NEMO negatively regulates the interferon antiviral response through disruption of the MAVS-TRAF3 complex. Cell Host Microbe 2012, 12: 211-222.
    • (2012) Cell Host Microbe , vol.12 , pp. 211-222
    • Belgnaoui, S.M.1    Paz, S.2    Samuel, S.3    Goulet, M.L.4    Sun, Q.5    Kikkert, M.6    Iwai, K.7
  • 68
    • 79251550124 scopus 로고    scopus 로고
    • Linear ubiquitin assembly complex negatively regulates RIG-I- and TRIM25- mediated type I interferon induction
    • Inn KS, Gack MU, Tokunaga F, Shi M,Wong LY, Iwai K, Jung JU. Linear ubiquitin assembly complex negatively regulates RIG-I- and TRIM25- mediated type I interferon induction. Mol Cell 2011, 41: 354-365.
    • (2011) Mol Cell , vol.41 , pp. 354-365
    • Inn, K.S.1    Gack, M.U.2    Tokunaga, F.3    Shi, M.4    Wong, L.Y.5    Iwai, K.6    Jung, J.U.7
  • 69
    • 55549146091 scopus 로고    scopus 로고
    • Negative feedback regulation of cellular antiviral signaling by RBCK1-mediated degradation of IRF3
    • Zhang M, Tian Y, Wang RP, Gao D, Zhang Y, Diao FC, Chen DY, et al. Negative feedback regulation of cellular antiviral signaling by RBCK1-mediated degradation of IRF3. Cell Res 2008, 18: 1096-1104.
    • (2008) Cell Res , vol.18 , pp. 1096-1104
    • Zhang, M.1    Tian, Y.2    Wang, R.P.3    Gao, D.4    Zhang, Y.5    Diao, F.C.6    Chen, D.Y.7
  • 70
    • 84877117404 scopus 로고    scopus 로고
    • FoxO1 negatively regulates cellular antiviral response by promoting degradation of IRF3
    • Lei CQ, Zhang Y, Xia T, Jiang LQ, Zhong B, Shu HB. FoxO1 negatively regulates cellular antiviral response by promoting degradation of IRF3. J Biol Chem 2013, 288: 12596-12604.
    • (2013) J Biol Chem , vol.288 , pp. 12596-12604
    • Lei, C.Q.1    Zhang, Y.2    Xia, T.3    Jiang, L.Q.4    Zhong, B.5    Shu, H.B.6
  • 71
    • 78650130030 scopus 로고    scopus 로고
    • The ubiquitin E3 ligase RAUL negatively regulates type i interferon through ubiquitination of the transcription factors IRF7 and IRF3
    • Yu Y, Hayward GS. The ubiquitin E3 ligase RAUL negatively regulates type i interferon through ubiquitination of the transcription factors IRF7 and IRF3. Immunity 2010, 33: 863-877.
    • (2010) Immunity , vol.33 , pp. 863-877
    • Yu, Y.1    Hayward, G.S.2
  • 72
    • 55549102621 scopus 로고    scopus 로고
    • PLP2, a potent deubiquitinase from murine hepatitis virus, strongly inhibits cellular type I interferon production
    • Zheng D, Chen G, Guo B, Cheng G, Tang H. PLP2, a potent deubiquitinase from murine hepatitis virus, strongly inhibits cellular type I interferon production. Cell Res 2008, 18: 1105-1113.
    • (2008) Cell Res , vol.18 , pp. 1105-1113
    • Zheng, D.1    Chen, G.2    Guo, B.3    Cheng, G.4    Tang, H.5
  • 73
    • 84899131835 scopus 로고    scopus 로고
    • The cGAS-cGAMP-STING pathway of cytosolic DNA sensing and signaling
    • Cai X, Chiu YH, Chen ZJ. The cGAS-cGAMP-STING pathway of cytosolic DNA sensing and signaling. Mol Cell 2014, 54: 289-296.
    • (2014) Mol Cell , vol.54 , pp. 289-296
    • Cai, X.1    Chiu, Y.H.2    Chen, Z.J.3
  • 74
    • 84873724533 scopus 로고    scopus 로고
    • Cyclic GMP-AMP is an endogenous second messenger in innate immune signaling by cytosolic DNA
    • Wu J, Sun L, Chen X, Du F, Shi H, Chen C, Chen ZJ. Cyclic GMP-AMP is an endogenous second messenger in innate immune signaling by cytosolic DNA. Science 2013, 339: 826-830.
    • (2013) Science , vol.339 , pp. 826-830
    • Wu, J.1    Sun, L.2    Chen, X.3    Du, F.4    Shi, H.5    Chen, C.6    Chen, Z.J.7
  • 75
    • 78650214109 scopus 로고    scopus 로고
    • The ubiquitin ligase TRIM56 regulates innate immune responses to intracellular double-stranded DNA
    • Tsuchida T, Zou J, Saitoh T, Kumar H, Abe T, Matsuura Y, Kawai T, et al. The ubiquitin ligase TRIM56 regulates innate immune responses to intracellular double-stranded DNA. Immunity 2010, 33: 765-776.
    • (2010) Immunity , vol.33 , pp. 765-776
    • Tsuchida, T.1    Zou, J.2    Saitoh, T.3    Kumar, H.4    Abe, T.5    Matsuura, Y.6    Kawai, T.7
  • 76
    • 84865270570 scopus 로고    scopus 로고
    • TRIM32 protein modulates type I interferon induction and cellular antiviral response by targeting MITA/ STING protein for K63-linked ubiquitination
    • Zhang J, Hu MM, Wang YY, Shu HB. TRIM32 protein modulates type I interferon induction and cellular antiviral response by targeting MITA/ STING protein for K63-linked ubiquitination. J Biol Chem 2012, 287: 28646-28655.
    • (2012) J Biol Chem , vol.287 , pp. 28646-28655
    • Zhang, J.1    Hu, M.M.2    Wang, Y.Y.3    Shu, H.B.4
  • 77
    • 62049084519 scopus 로고    scopus 로고
    • The ubiquitin ligase RNF5 regulates antiviral responses by mediating degradation of the adaptor protein MITA
    • Zhong B, Zhang L, Lei C, Li Y, Mao AP, Yang Y, Wang YY, et al. The ubiquitin ligase RNF5 regulates antiviral responses by mediating degradation of the adaptor protein MITA. Immunity 2009, 30: 397-407.
    • (2009) Immunity , vol.30 , pp. 397-407
    • Zhong, B.1    Zhang, L.2    Lei, C.3    Li, Y.4    Mao, A.P.5    Yang, Y.6    Wang, Y.Y.7
  • 78
    • 84907587749 scopus 로고    scopus 로고
    • RNF26 temporally regulates virus-triggered type I interferon induction by two distinct mechanisms
    • Qin Y, Zhou MT, Hu MM, Hu YH, Zhang J, Guo L, Zhong B, et al. RNF26 temporally regulates virus-triggered type I interferon induction by two distinct mechanisms. PLoS Pathog 2014, 10: E1004358.
    • (2014) PLoS Pathog , vol.10 , pp. e1004358
    • Qin, Y.1    Zhou, M.T.2    Hu, M.M.3    Hu, Y.H.4    Zhang, J.5    Guo, L.6    Zhong, B.7
  • 79
    • 84872683702 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase TRIM21 negatively regulates the innate immune response to intracellular double-stranded DNA
    • Zhang Z, Bao M, Lu N, Weng L, Yuan B, Liu YJ. The E3 ubiquitin ligase TRIM21 negatively regulates the innate immune response to intracellular double-stranded DNA. Nat Immunol 2013, 14: 172-178.
    • (2013) Nat Immunol , vol.14 , pp. 172-178
    • Zhang, Z.1    Bao, M.2    Lu, N.3    Weng, L.4    Yuan, B.5    Liu, Y.J.6
  • 80
    • 49649123561 scopus 로고    scopus 로고
    • Regulation of IkappaB kinase-related kinases and antiviral responses by tumor suppressor CYLD
    • Zhang M, Wu X, Lee AJ, Jin W, Chang M, Wright A, Imaizumi T, et al. Regulation of IkappaB kinase-related kinases and antiviral responses by tumor suppressor CYLD. J Biol Chem 2008, 283: 18621-18626.
    • (2008) J Biol Chem , vol.283 , pp. 18621-18626
    • Zhang, M.1    Wu, X.2    Lee, A.J.3    Jin, W.4    Chang, M.5    Wright, A.6    Imaizumi, T.7
  • 81
    • 77955710477 scopus 로고    scopus 로고
    • The ubiquitin-specific protease 17 is involved in virus-triggered type I IFN signaling
    • Chen R, Zhang L, Zhong B, Tan B, Liu Y, Shu HB. The ubiquitin-specific protease 17 is involved in virus-triggered type I IFN signaling. Cell Res 2010, 20: 802-811.
    • (2010) Cell Res , vol.20 , pp. 802-811
    • Chen, R.1    Zhang, L.2    Zhong, B.3    Tan, B.4    Liu, Y.5    Shu, H.B.6
  • 82
    • 84892428607 scopus 로고    scopus 로고
    • The ubiquitin-specific protease USP15 promotes RIG-Imediated antiviral signaling by deubiquitylating TRIM25
    • Pauli EK, Chan YK, Davis ME, Gableske S, Wang MK, Feister KF, Gack MU. The ubiquitin-specific protease USP15 promotes RIG-Imediated antiviral signaling by deubiquitylating TRIM25. Sci Signal 2014, 7: Ra3.
    • (2014) Sci Signal , vol.7 , pp. ra3
    • Pauli, E.K.1    Chan, Y.K.2    Davis, M.E.3    Gableske, S.4    Wang, M.K.5    Feister, K.F.6    Gack, M.U.7
  • 83
    • 84875789033 scopus 로고    scopus 로고
    • USP4 positively regulates RIG-I-mediated antiviral response through deubiquitination and stablilization of RIG-I
    • Wang L, Zhao W, Zhang M, Wang P, Zhao K, Zhao X, Yang S, et al. USP4 positively regulates RIG-I-mediated antiviral response through deubiquitination and stablilization of RIG-I. J Virol 2013, 87: 4507-4515.
    • (2013) J Virol , vol.87 , pp. 4507-4515
    • Wang, L.1    Zhao, W.2    Zhang, M.3    Wang, P.4    Zhao, K.5    Zhao, X.6    Yang, S.7
  • 84
    • 84898040489 scopus 로고    scopus 로고
    • USP3 inhibits type I interferon signaling by deubiquitinating RIG-I-like receptors
    • Cui J, Song Y, Li Y, Zhu Q, Tan P, Qin Y, Wang HY, et al. USP3 inhibits type I interferon signaling by deubiquitinating RIG-I-like receptors. Cell Res 2014, 24: 400-416.
    • (2014) Cell Res , vol.24 , pp. 400-416
    • Cui, J.1    Song, Y.2    Li, Y.3    Zhu, Q.4    Tan, P.5    Qin, Y.6    Wang, H.Y.7
  • 85
    • 84893721948 scopus 로고    scopus 로고
    • USP21 negatively regulates antiviral response by acting as a RIG-I deubiquitinase
    • Fan Y, Mao R, Yu Y, Liu S, Shi Z, Cheng J, Zhang H, et al. USP21 negatively regulates antiviral response by acting as a RIG-I deubiquitinase. J Exp Med 2014, 211: 313-328.
    • (2014) J Exp Med , vol.211 , pp. 313-328
    • Fan, Y.1    Mao, R.2    Yu, Y.3    Liu, S.4    Shi, Z.5    Cheng, J.6    Zhang, H.7
  • 86
  • 87
    • 80055007460 scopus 로고    scopus 로고
    • Inhibition of RIG-I-mediated signaling by Kaposi's sarcoma-associated herpesvirus-encoded deubiquitinase ORF64
    • Inn KS, Lee SH, Rathbun JY,Wong LY, Toth Z, Machida K, Ou JH, et al. Inhibition of RIG-I-mediated signaling by Kaposi's sarcoma-associated herpesvirus-encoded deubiquitinase ORF64. J Virol 2011, 85: 10899-10904.
    • (2011) J Virol , vol.85 , pp. 10899-10904
    • Inn, K.S.1    Lee, S.H.2    Rathbun, J.Y.3    Wong, L.Y.4    Toth, Z.5    Machida, K.6    Ou, J.H.7
  • 88
    • 79952837091 scopus 로고    scopus 로고
    • The leader proteinase of foot-and-mouth disease virus negatively regulates the type I interferon pathway by acting as a viral deubiquitinase
    • Wang D, Fang L, Li P, Sun L, Fan J, Zhang Q, Luo R, et al. The leader proteinase of foot-and-mouth disease virus negatively regulates the type I interferon pathway by acting as a viral deubiquitinase. J Virol 2011, 85: 3758-3766.
    • (2011) J Virol , vol.85 , pp. 3758-3766
    • Wang, D.1    Fang, L.2    Li, P.3    Sun, L.4    Fan, J.5    Zhang, Q.6    Luo, R.7
  • 89
    • 84907445220 scopus 로고    scopus 로고
    • Hepatitis E virus inhibits type I interferon induction by ORF1 products
    • Nan Y, Yu Y, Ma Z, Khattar SK, Fredericksen B, Zhang YJ. Hepatitis E virus inhibits type I interferon induction by ORF1 products. J Virol 2014, 88: 11924-11932.
    • (2014) J Virol , vol.88 , pp. 11924-11932
    • Nan, Y.1    Yu, Y.2    Ma, Z.3    Khattar, S.K.4    Fredericksen, B.5    Zhang, Y.J.6
  • 90
    • 84880120792 scopus 로고    scopus 로고
    • Human bocavirus VP2 upregulates IFN-beta pathway by inhibiting ring finger protein 125-mediated ubiquitination of retinoic acid-inducible gene-I
    • Luo H, Zhang Z, Zheng Z, Ke X, Zhang X, Li Q, Liu Y, et al. Human bocavirus VP2 upregulates IFN-beta pathway by inhibiting ring finger protein 125-mediated ubiquitination of retinoic acid-inducible gene-I. J Immunol 2013, 191: 660-669.
    • (2013) J Immunol , vol.191 , pp. 660-669
    • Luo, H.1    Zhang, Z.2    Zheng, Z.3    Ke, X.4    Zhang, X.5    Li, Q.6    Liu, Y.7
  • 91
    • 80053336032 scopus 로고    scopus 로고
    • A protein-kinase, IFN-inducible double-stranded RNA dependent inhibitor and repressor of p58 (PRKRIR) enhances type I IFNmediated antiviral response through the stability control of RIG-I protein
    • Now H, Yoo JY. A protein-kinase, IFN-inducible double-stranded RNA dependent inhibitor and repressor of p58 (PRKRIR) enhances type I IFNmediated antiviral response through the stability control of RIG-I protein. Biochem Biophys Res Commun 2011, 413: 487-493.
    • (2011) Biochem Biophys Res Commun , vol.413 , pp. 487-493
    • Now, H.1    Yoo, J.Y.2
  • 94
    • 77951168849 scopus 로고    scopus 로고
    • Regulation of virus-triggered signaling by OTUB1- and OTUB2-mediated deubiquitination of TRAF3 and TRAF6
    • Li S, Zheng H, Mao AP, Zhong B, Li Y, Liu Y, Gao Y, et al. Regulation of virus-triggered signaling by OTUB1- and OTUB2-mediated deubiquitination of TRAF3 and TRAF6. J Biol Chem 2010, 285: 4291-4297.
    • (2010) J Biol Chem , vol.285 , pp. 4291-4297
    • Li, S.1    Zheng, H.2    Mao, A.P.3    Zhong, B.4    Li, Y.5    Liu, Y.6    Gao, Y.7
  • 95
    • 84875514442 scopus 로고    scopus 로고
    • Epstein-Barr virus deubiquitinase downregulates TRAF6-mediated NF-kappaB signaling during productive replication
    • Saito S, Murata T, Kanda T, Isomura H, Narita Y, Sugimoto A, Kawashima D, et al. Epstein-Barr virus deubiquitinase downregulates TRAF6-mediated NF-kappaB signaling during productive replication. J Virol 2013, 87: 4060-4070.
    • (2013) J Virol , vol.87 , pp. 4060-4070
    • Saito, S.1    Murata, T.2    Kanda, T.3    Isomura, H.4    Narita, Y.5    Sugimoto, A.6    Kawashima, D.7
  • 96
    • 84863338304 scopus 로고    scopus 로고
    • Ubiquitination in signaling to and activation of IKK
    • Chen ZJ. Ubiquitination in signaling to and activation of IKK. Immunol Rev 2012, 246: 95-106.
    • (2012) Immunol Rev , vol.246 , pp. 95-106
    • Chen, Z.J.1
  • 97
    • 84872147132 scopus 로고    scopus 로고
    • RING finger protein 11 targets TBK1/IKKi kinases to inhibit antiviral signaling
    • Charoenthongtrakul S, Gao L, Parvatiyar K, Lee D, HarhajEW. RING finger protein 11 targets TBK1/IKKi kinases to inhibit antiviral signaling. PLoS One 2013, 8: E53717.
    • (2013) PLoS One , vol.8 , pp. e53717
    • Charoenthongtrakul, S.1    Gao, L.2    Parvatiyar, K.3    Lee, D.4    Harhaj, E.W.5
  • 98
    • 79951989445 scopus 로고    scopus 로고
    • PLP2 of mouse hepatitis virus A59 (MHV-A59) targets TBK1 to negatively regulate cellular type I interferon signaling pathway
    • Wang G, Chen G, Zheng D, Cheng G, Tang H. PLP2 of mouse hepatitis virus A59 (MHV-A59) targets TBK1 to negatively regulate cellular type I interferon signaling pathway. PLoS One 2011, 6: E17192.
    • (2011) PLoS One , vol.6 , pp. e17192
    • Wang, G.1    Chen, G.2    Zheng, D.3    Cheng, G.4    Tang, H.5
  • 99
    • 80455129191 scopus 로고    scopus 로고
    • SENP2 negatively regulates cellular antiviral response by deSUMOylating IRF3 and conditioning it for ubiquitination and degradation
    • Ran Y, Liu TT, Zhou Q, Li S, Mao AP, Li Y, Liu LJ, et al. SENP2 negatively regulates cellular antiviral response by deSUMOylating IRF3 and conditioning it for ubiquitination and degradation. J Mol Cell Biol 2011, 3: 283-292.
    • (2011) J Mol Cell Biol , vol.3 , pp. 283-292
    • Ran, Y.1    Liu, T.T.2    Zhou, Q.3    Li, S.4    Mao, A.P.5    Li, Y.6    Liu, L.J.7
  • 100
    • 79953162495 scopus 로고    scopus 로고
    • SUMOylation of RIG-I positively regulates the type I interferon signaling
    • Mi Z, Fu J, Xiong Y, Tang H. SUMOylation of RIG-I positively regulates the type I interferon signaling. Protein Cell 2010, 1: 275-283.
    • (2010) Protein Cell , vol.1 , pp. 275-283
    • Mi, Z.1    Fu, J.2    Xiong, Y.3    Tang, H.4
  • 101
    • 78650609675 scopus 로고    scopus 로고
    • MDA5 is SUMOylated by PIAS2- beta in the upregulation of type I interferon signaling
    • Fu J, Xiong Y, Xu Y, Cheng G, Tang H. MDA5 is SUMOylated by PIAS2- beta in the upregulation of type I interferon signaling. Mol Immunol 2011, 48: 415-422.
    • (2011) Mol Immunol , vol.48 , pp. 415-422
    • Fu, J.1    Xiong, Y.2    Xu, Y.3    Cheng, G.4    Tang, H.5
  • 102
    • 35548943169 scopus 로고    scopus 로고
    • UbcH8 regulates ubiquitin and ISG15 conjugation to RIG-I
    • Arimoto K, Konishi H, Shimotohno K. UbcH8 regulates ubiquitin and ISG15 conjugation to RIG-I. Mol Immunol 2008, 45: 1078-1084.
    • (2008) Mol Immunol , vol.45 , pp. 1078-1084
    • Arimoto, K.1    Konishi, H.2    Shimotohno, K.3


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