메뉴 건너뛰기




Volumn 6, Issue , 2015, Pages

The mitochondrial ubiquitin ligase MARCH5 resolves MAVS aggregates during antiviral signalling

Author keywords

[No Author keywords available]

Indexed keywords

INTERFERON; MARCH5 PROTEIN; MITOCHONDRIAL ANTIVIRAL SIGNALLING PROTEIN; MITOCHONDRIAL ENZYME; PROTEASOME; PROTEIN AGGREGATE; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; IPS-1 PROTEIN, MOUSE; MARCH5 PROTEIN, HUMAN; MARCH5 PROTEIN, MOUSE; MEMBRANE PROTEIN; MITOCHONDRIAL PROTEIN; SIGNAL TRANSDUCING ADAPTOR PROTEIN; UBIQUITIN; UBIQUITIN PROTEIN LIGASE; VISA PROTEIN, HUMAN;

EID: 84938809934     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms8910     Document Type: Article
Times cited : (126)

References (56)
  • 1
    • 56949087771 scopus 로고    scopus 로고
    • Viral and cellular MARCH ubiquitin ligases and cancer
    • Wang, X., Herr, R. A. & Hansen, T. Viral and cellular MARCH ubiquitin ligases and cancer. Semin. Cancer Biol. 18, 441-450 (2008).
    • (2008) Semin. Cancer Biol. , vol.18 , pp. 441-450
    • Wang, X.1    Herr, R.A.2    Hansen, T.3
  • 2
    • 33750369258 scopus 로고    scopus 로고
    • A novel family of membrane-bound E3 ubiquitin ligases
    • Ohmura-Hoshino, M. et al. A novel family of membrane-bound E3 ubiquitin ligases. J. Biochem. 140, 147-154 (2006).
    • (2006) J. Biochem. , vol.140 , pp. 147-154
    • Ohmura-Hoshino, M.1
  • 3
    • 0346373729 scopus 로고    scopus 로고
    • Downregulation of major histocompatibility complex class i by human ubiquitin ligases related to viral immune evasion proteins
    • Bartee, E., Mansouri, M., Hovey Nerenberg, B. T., Gouveia, K. & Fruh, K. Downregulation of major histocompatibility complex class I by human ubiquitin ligases related to viral immune evasion proteins. J. Virol. 78, 1109-1120 (2004).
    • (2004) J. Virol. , vol.78 , pp. 1109-1120
    • Bartee, E.1    Mansouri, M.2    Hovey Nerenberg, B.T.3    Gouveia, K.4    Fruh, K.5
  • 5
    • 67349172917 scopus 로고    scopus 로고
    • The trafficking and regulation of membrane receptors by the RING-CH ubiquitin E3 ligases
    • Nathan, J. A. & Lehner, P. J. The trafficking and regulation of membrane receptors by the RING-CH ubiquitin E3 ligases. Exp. Cell Res. 315, 1593-1600 (2009).
    • (2009) Exp. Cell Res. , vol.315 , pp. 1593-1600
    • Nathan, J.A.1    Lehner, P.J.2
  • 6
    • 84876858943 scopus 로고    scopus 로고
    • Ubiquitination of HLA-DO by MARCH family E3 ligases
    • Jahnke, M., Trowsdale, J. & Kelly, A. P. Ubiquitination of HLA-DO by MARCH family E3 ligases. Eur. J. Immunol. 43, 1153-1161 (2013).
    • (2013) Eur. J. Immunol. , vol.43 , pp. 1153-1161
    • Jahnke, M.1    Trowsdale, J.2    Kelly, A.P.3
  • 7
    • 84879688223 scopus 로고    scopus 로고
    • MARCH1-mediated MHCII ubiquitination promotes dendritic cell selection of natural regulatory T cells
    • Oh, J. et al. MARCH1-mediated MHCII ubiquitination promotes dendritic cell selection of natural regulatory T cells. J. Exp. Med. 210, 1069-1077 (2013).
    • (2013) J. Exp. Med. , vol.210 , pp. 1069-1077
    • Oh, J.1
  • 8
    • 84899806692 scopus 로고    scopus 로고
    • Roles of mitochondrial ubiquitin ligase MITOL/MARCH5 in mitochondrial dynamics and diseases
    • Nagashima, S., Tokuyama, T., Yonashiro, R., Inatome, R. & Yanagi, S. Roles of mitochondrial ubiquitin ligase MITOL/MARCH5 in mitochondrial dynamics and diseases. J. Biochem. 155, 273-279 (2014).
    • (2014) J. Biochem. , vol.155 , pp. 273-279
    • Nagashima, S.1    Tokuyama, T.2    Yonashiro, R.3    Inatome, R.4    Yanagi, S.5
  • 9
    • 34347398050 scopus 로고    scopus 로고
    • The mitochondrial E3 ubiquitin ligase MARCH5 is required for Drp1 dependent mitochondrial division
    • Karbowski, M., Neutzner, A. & Youle, R. J. The mitochondrial E3 ubiquitin ligase MARCH5 is required for Drp1 dependent mitochondrial division. J. Cell Biol. 178, 71-84 (2007).
    • (2007) J. Cell Biol. , vol.178 , pp. 71-84
    • Karbowski, M.1    Neutzner, A.2    Youle, R.J.3
  • 10
    • 76649142385 scopus 로고    scopus 로고
    • Loss of MARCH5 mitochondrial E3 ubiquitin ligase induces cellular senescence through dynamin-related protein 1 and mitofusin 1
    • Park, Y. Y. et al. Loss of MARCH5 mitochondrial E3 ubiquitin ligase induces cellular senescence through dynamin-related protein 1 and mitofusin 1. J. Cell Sci. 123, 619-626 (2010).
    • (2010) J. Cell Sci. , vol.123 , pp. 619-626
    • Park, Y.Y.1
  • 11
    • 84871234101 scopus 로고    scopus 로고
    • Mitofusin 1 is degraded at G2/M phase through ubiquitylation by MARCH5
    • Park, Y. Y. & Cho, H. Mitofusin 1 is degraded at G2/M phase through ubiquitylation by MARCH5. Cell Div. 7, 25 (2012).
    • (2012) Cell Div. , vol.7 , pp. 25
    • Park, Y.Y.1    Cho, H.2
  • 12
    • 33747613595 scopus 로고    scopus 로고
    • A novel mitochondrial ubiquitin ligase plays a critical role in mitochondrial dynamics
    • Yonashiro, R. et al. A novel mitochondrial ubiquitin ligase plays a critical role in mitochondrial dynamics. EMBO J. 25, 3618-3626 (2006).
    • (2006) EMBO J. , vol.25 , pp. 3618-3626
    • Yonashiro, R.1
  • 13
    • 84857132601 scopus 로고    scopus 로고
    • Mitochondrial ubiquitin ligase MITOL blocks S-nitrosylated MAP1B-light chain 1-mediated mitochondrial dysfunction and neuronal cell death
    • Yonashiro, R. et al. Mitochondrial ubiquitin ligase MITOL blocks S-nitrosylated MAP1B-light chain 1-mediated mitochondrial dysfunction and neuronal cell death. Proc. Natl Acad. Sci. USA 109, 2382-2387 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 2382-2387
    • Yonashiro, R.1
  • 14
    • 78650007530 scopus 로고    scopus 로고
    • A mitochondrial ubiquitin ligase MITOL controls cell toxicity of polyglutamine-expanded protein
    • Sugiura, A. et al. A mitochondrial ubiquitin ligase MITOL controls cell toxicity of polyglutamine-expanded protein. Mitochondrion 11, 139-146 (2011).
    • (2011) Mitochondrion , vol.11 , pp. 139-146
    • Sugiura, A.1
  • 15
    • 73949112709 scopus 로고    scopus 로고
    • Mitochondrial ubiquitin ligase MITOL ubiquitinates mutant SOD1 and attenuates mutant SOD1-induced reactive oxygen species generation
    • Yonashiro, R. et al. Mitochondrial ubiquitin ligase MITOL ubiquitinates mutant SOD1 and attenuates mutant SOD1-induced reactive oxygen species generation. Mol. Biol. Cell 20, 4524-4530 (2009).
    • (2009) Mol. Biol. Cell , vol.20 , pp. 4524-4530
    • Yonashiro, R.1
  • 16
    • 84901036269 scopus 로고    scopus 로고
    • MARCH5-mediated quality control on acetylated Mfn1 facilitates mitochondrial homeostasis and cell survival
    • Park, Y. Y., Nguyen, O. T., Kang, H. & Cho, H. MARCH5-mediated quality control on acetylated Mfn1 facilitates mitochondrial homeostasis and cell survival. Cell Death Dis. 5, e1172 (2014).
    • (2014) Cell Death Dis. , vol.5 , pp. e1172
    • Park, Y.Y.1    Nguyen, O.T.2    Kang, H.3    Cho, H.4
  • 17
    • 3242813113 scopus 로고    scopus 로고
    • The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses
    • Yoneyama, M. et al. The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses. Nat. Immunol. 5, 730-737 (2004).
    • (2004) Nat. Immunol. , vol.5 , pp. 730-737
    • Yoneyama, M.1
  • 18
    • 33646342149 scopus 로고    scopus 로고
    • Differential roles of MDA5 and RIG-I helicases in the recognition of RNA viruses
    • Kato, H. et al. Differential roles of MDA5 and RIG-I helicases in the recognition of RNA viruses. Nature 441, 101-105 (2006).
    • (2006) Nature , vol.441 , pp. 101-105
    • Kato, H.1
  • 19
    • 39149107423 scopus 로고    scopus 로고
    • MDA5/RIG-I and virus recognition
    • Takeuchi, O. & Akira, S. MDA5/RIG-I and virus recognition. Curr. Opin. Immunol. 20, 17-22 (2008).
    • (2008) Curr. Opin. Immunol. , vol.20 , pp. 17-22
    • Takeuchi, O.1    Akira, S.2
  • 21
    • 79961133270 scopus 로고    scopus 로고
    • MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune response
    • Hou, F. et al. MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune response. Cell 146, 448-461 (2011).
    • (2011) Cell , vol.146 , pp. 448-461
    • Hou, F.1
  • 22
    • 82655172367 scopus 로고    scopus 로고
    • Prion-like behavior of MAVS in RIG-I signaling
    • Moresco, E. M., Vine, D. L. & Beutler, B. Prion-like behavior of MAVS in RIG-I signaling. Cell Res. 21, 1643-1645 (2011).
    • (2011) Cell Res. , vol.21 , pp. 1643-1645
    • Moresco, E.M.1    Vine, D.L.2    Beutler, B.3
  • 23
    • 84896381627 scopus 로고    scopus 로고
    • Prion-like polymerization underlies signal transduction in antiviral immune defense and inflammasome activation
    • Cai, X. et al. Prion-like polymerization underlies signal transduction in antiviral immune defense and inflammasome activation. Cell 156, 1207-1222 (2014).
    • (2014) Cell , vol.156 , pp. 1207-1222
    • Cai, X.1
  • 24
    • 24144461689 scopus 로고    scopus 로고
    • Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-kappaB and IRF 3
    • Seth, R. B., Sun, L., Ea, C. K. & Chen, Z. J. Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-kappaB and IRF 3. Cell 122, 669-682 (2005).
    • (2005) Cell , vol.122 , pp. 669-682
    • Seth, R.B.1    Sun, L.2    Ea, C.K.3    Chen, Z.J.4
  • 25
    • 27144440523 scopus 로고    scopus 로고
    • IPS-1, an adaptor triggering RIG-I-and Mda5-mediated type i interferon induction
    • Kawai, T. et al. IPS-1, an adaptor triggering RIG-I-and Mda5-mediated type I interferon induction. Nat. Immunol. 6, 981-988 (2005).
    • (2005) Nat. Immunol. , vol.6 , pp. 981-988
    • Kawai, T.1
  • 26
    • 24944538819 scopus 로고    scopus 로고
    • VISA is an adapter protein required for virus-triggered IFN-beta signaling
    • Xu, L. G. et al. VISA is an adapter protein required for virus-triggered IFN-beta signaling. Mol. Cell 19, 727-740 (2005).
    • (2005) Mol. Cell , vol.19 , pp. 727-740
    • Xu, L.G.1
  • 27
    • 38749097018 scopus 로고    scopus 로고
    • NLRX1 is a regulator of mitochondrial antiviral immunity
    • Moore, C. B. et al. NLRX1 is a regulator of mitochondrial antiviral immunity. Nature 451, 573-577 (2008).
    • (2008) Nature , vol.451 , pp. 573-577
    • Moore, C.B.1
  • 28
    • 70449726455 scopus 로고    scopus 로고
    • PCBP2 mediates degradation of the adaptor MAVS via the HECT ubiquitin ligase AIP4
    • You, F. et al. PCBP2 mediates degradation of the adaptor MAVS via the HECT ubiquitin ligase AIP4. Nat. Immunol. 10, 1300-1308 (2009).
    • (2009) Nat. Immunol. , vol.10 , pp. 1300-1308
    • You, F.1
  • 29
    • 70449725290 scopus 로고    scopus 로고
    • Negative regulation of MAVS-mediated innate immune response by PSMA7
    • Jia, Y. et al. Negative regulation of MAVS-mediated innate immune response by PSMA7. J. Immunol. 183, 4241-4248 (2009).
    • (2009) J. Immunol. , vol.183 , pp. 4241-4248
    • Jia, Y.1
  • 30
    • 79960049196 scopus 로고    scopus 로고
    • A functional C-terminal TRAF3-binding site in MAVS participates in positive and negative regulation of the IFN antiviral response
    • Paz, S. et al. A functional C-terminal TRAF3-binding site in MAVS participates in positive and negative regulation of the IFN antiviral response. Cell Res. 21, 895-910 (2011).
    • (2011) Cell Res. , vol.21 , pp. 895-910
    • Paz, S.1
  • 31
    • 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. 189, 5304-5313 (2012).
    • (2012) J. Immunol. , vol.189 , pp. 5304-5313
    • Wang, Y.1    Tong, X.2    Ye, X.3
  • 32
    • 84876980686 scopus 로고    scopus 로고
    • UBXN1 interferes with Rig-I-like receptor-mediated antiviral immune response by targeting MAVS
    • Wang, P. et al. UBXN1 interferes with Rig-I-like receptor-mediated antiviral immune response by targeting MAVS. Cell Rep. 3, 1057-1070 (2013).
    • (2013) Cell Rep. , vol.3 , pp. 1057-1070
    • Wang, P.1
  • 33
    • 84901260895 scopus 로고    scopus 로고
    • Smurf2 negatively modulates RIG-I-dependent antiviral response by targeting VISA/MAVS for ubiquitination and degradation
    • Pan, Y. et al. Smurf2 negatively modulates RIG-I-dependent antiviral response by targeting VISA/MAVS for ubiquitination and degradation. J. Immunol. 192, 4758-4764 (2014).
    • (2014) J. Immunol. , vol.192 , pp. 4758-4764
    • Pan, Y.1
  • 34
    • 84894177433 scopus 로고    scopus 로고
    • A bicistronic MAVS transcript highlights a class of truncated variants in antiviral immunity
    • Brubaker, S. W., Gauthier, A. E., Mills, E. W., Ingolia, N. T. & Kagan, J. C. A bicistronic MAVS transcript highlights a class of truncated variants in antiviral immunity. Cell 156, 800-811 (2014).
    • (2014) Cell , vol.156 , pp. 800-811
    • Brubaker, S.W.1    Gauthier, A.E.2    Mills, E.W.3    Ingolia, N.T.4    Kagan, J.C.5
  • 35
    • 84891685535 scopus 로고    scopus 로고
    • MITOL regulates endoplasmic reticulum-mitochondria contacts via Mitofusin2
    • Sugiura, A. et al. MITOL regulates endoplasmic reticulum-mitochondria contacts via Mitofusin2. Mol. Cell 51, 20-34 (2013).
    • (2013) Mol. Cell , vol.51 , pp. 20-34
    • Sugiura, A.1
  • 36
    • 84898747432 scopus 로고    scopus 로고
    • Structural basis for the prion-like MAVS filaments in antiviral innate immunity
    • Xu, H. et al. Structural basis for the prion-like MAVS filaments in antiviral innate immunity. eLife 3, e01489 (2014).
    • (2014) ELife , vol.3
    • Xu, H.1
  • 37
    • 84906342978 scopus 로고    scopus 로고
    • Molecular imprinting as a signal-activation mechanism of the viral RNA sensor RIG-I
    • Wu, B. et al. Molecular imprinting as a signal-activation mechanism of the viral RNA sensor RIG-I. Mol. Cell 55, 511-523 (2014).
    • (2014) Mol. Cell , vol.55 , pp. 511-523
    • Wu, B.1
  • 38
    • 0036711122 scopus 로고    scopus 로고
    • Immune evasion by a novel family of viral PHD/LAP-finger proteins of gamma-2 herpesviruses and poxviruses
    • Fruh, K., Bartee, E., Gouveia, K. & Mansouri, M. Immune evasion by a novel family of viral PHD/LAP-finger proteins of gamma-2 herpesviruses and poxviruses. Virus Res. 88, 55-69 (2002).
    • (2002) Virus Res. , vol.88 , pp. 55-69
    • Fruh, K.1    Bartee, E.2    Gouveia, K.3    Mansouri, M.4
  • 39
    • 0038352134 scopus 로고    scopus 로고
    • C-MIR, a human E3 ubiquitin ligase, is a functional homolog of herpesvirus proteins MIR1 and MIR2 and has similar activity
    • Goto, E. et al. c-MIR, a human E3 ubiquitin ligase, is a functional homolog of herpesvirus proteins MIR1 and MIR2 and has similar activity. J. Biol. Chem. 278, 14657-14668 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 14657-14668
    • Goto, E.1
  • 40
    • 26244468727 scopus 로고    scopus 로고
    • Downregulation of cell surface receptors by the K3 family of viral and cellular ubiquitin E3 ligases
    • Lehner, P. J., Hoer, S., Dodd, R. & Duncan, L. M. Downregulation of cell surface receptors by the K3 family of viral and cellular ubiquitin E3 ligases. Immunol. Rev. 207, 112-125 (2005).
    • (2005) Immunol. Rev. , vol.207 , pp. 112-125
    • Lehner, P.J.1    Hoer, S.2    Dodd, R.3    Duncan, L.M.4
  • 41
    • 0034682472 scopus 로고    scopus 로고
    • Inhibition of MHC class I-restricted antigen presentation by gamma 2-herpesviruses
    • Stevenson, P. G., Efstathiou, S., Doherty, P. C. & Lehner, P. J. Inhibition of MHC class I-restricted antigen presentation by gamma 2-herpesviruses. Proc. Natl Acad. Sci. USA 97, 8455-8460 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 8455-8460
    • Stevenson, P.G.1    Efstathiou, S.2    Doherty, P.C.3    Lehner, P.J.4
  • 42
    • 0034608951 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus encodes two proteins that block cell surface display of MHC class i chains by enhancing their endocytosis
    • Coscoy, L. & Ganem, D. Kaposi's sarcoma-associated herpesvirus encodes two proteins that block cell surface display of MHC class I chains by enhancing their endocytosis. Proc. Natl Acad. Sci. USA 97, 8051-8056 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 8051-8056
    • Coscoy, L.1    Ganem, D.2
  • 43
    • 34249951376 scopus 로고    scopus 로고
    • The Kaposi's sarcoma-associated herpesvirus K5 E3 ubiquitin ligase modulates targets by multiple molecular mechanisms
    • Means, R. E., Lang, S. M. & Jung, J. U. The Kaposi's sarcoma-associated herpesvirus K5 E3 ubiquitin ligase modulates targets by multiple molecular mechanisms. J. Virol. 81, 6573-6583 (2007).
    • (2007) J. Virol. , vol.81 , pp. 6573-6583
    • Means, R.E.1    Lang, S.M.2    Jung, J.U.3
  • 44
    • 33845618137 scopus 로고    scopus 로고
    • MARCH-IX mediates ubiquitination and downregulation of ICAM-1
    • Hoer, S., Smith, L. & Lehner, P. J. MARCH-IX mediates ubiquitination and downregulation of ICAM-1. FEBS Lett. 581, 45-51 (2007).
    • (2007) FEBS Lett. , vol.581 , pp. 45-51
    • Hoer, S.1    Smith, L.2    Lehner, P.J.3
  • 45
    • 84865562042 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase MARCH8 negatively regulates IL-1beta-induced NF-kappaB activation by targeting the IL1RAP coreceptor for ubiquitination and degradation
    • Chen, R., Li, M., Zhang, Y., Zhou, Q. & Shu, H. B. The E3 ubiquitin ligase MARCH8 negatively regulates IL-1beta-induced NF-kappaB activation by targeting the IL1RAP coreceptor for ubiquitination and degradation. Proc. Natl Acad. Sci. USA 109, 14128-14133 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 14128-14133
    • Chen, R.1    Li, M.2    Zhang, Y.3    Zhou, Q.4    Shu, H.B.5
  • 46
    • 79958042278 scopus 로고    scopus 로고
    • Mitochondrial ubiquitin ligase MARCH5 promotes TLR7 signaling by attenuating TANK action
    • Shi, H. X. et al. Mitochondrial ubiquitin ligase MARCH5 promotes TLR7 signaling by attenuating TANK action. PLoS Pathog. 7, e1002057 (2011).
    • (2011) PLoS Pathog. , vol.7
    • Shi, H.X.1
  • 47
    • 34247341367 scopus 로고    scopus 로고
    • TRIM25 RING-finger E3 ubiquitin ligase is essential for RIGI-mediated antiviral activity
    • Gack, M. U. et al. TRIM25 RING-finger E3 ubiquitin ligase is essential for RIGI-mediated antiviral activity. Nature 446, 916-920 (2007).
    • (2007) Nature , vol.446 , pp. 916-920
    • Gack, M.U.1
  • 48
    • 62049084519 scopus 로고    scopus 로고
    • The ubiquitin ligase RNF5 regulates antiviral responses by mediating degradation of the adaptor protein MITA
    • Zhong, B. et al. The ubiquitin ligase RNF5 regulates antiviral responses by mediating degradation of the adaptor protein MITA. Immunity 30, 397-407 (2009).
    • (2009) Immunity , vol.30 , pp. 397-407
    • Zhong, B.1
  • 49
    • 59749085907 scopus 로고    scopus 로고
    • MAVS dimer is a crucial signaling component of innate immunity and the target of hepatitis C virus NS3/4A protease
    • Baril, M., Racine, M. E., Penin, F. & Lamarre, D. MAVS dimer is a crucial signaling component of innate immunity and the target of hepatitis C virus NS3/4A protease. J. Virol. 83, 1299-1311 (2009).
    • (2009) J. Virol. , vol.83 , pp. 1299-1311
    • Baril, M.1    Racine, M.E.2    Penin, F.3    Lamarre, D.4
  • 50
    • 79961133534 scopus 로고    scopus 로고
    • A prion-like trigger of antiviral signaling
    • Ye, J. & Maniatis, T. A prion-like trigger of antiviral signaling. Cell 146, 348-350 (2011).
    • (2011) Cell , vol.146 , pp. 348-350
    • Ye, J.1    Maniatis, T.2
  • 51
    • 84899957213 scopus 로고    scopus 로고
    • Structural basis for ubiquitinmediated antiviral signal activation by RIG-I
    • Peisley, A., Wu, B., Xu, H., Chen, Z. J. & Hur, S. Structural basis for ubiquitinmediated antiviral signal activation by RIG-I. Nature 509, 110-114 (2014).
    • (2014) Nature , vol.509 , pp. 110-114
    • Peisley, A.1    Wu, B.2    Xu, H.3    Chen, Z.J.4    Hur, S.5
  • 52
    • 84882705934 scopus 로고    scopus 로고
    • MAVS recruits multiple ubiquitin E3 ligases to activate antiviral signaling cascades
    • Liu, S. et al. MAVS recruits multiple ubiquitin E3 ligases to activate antiviral signaling cascades. eLife 2, e00785 (2013).
    • (2013) ELife , vol.2
    • Liu, S.1
  • 53
    • 67649214539 scopus 로고    scopus 로고
    • Ubiquitin-regulated recruitment of IkappaB kinase epsilon to the MAVS interferon signaling adapter
    • Paz, S. et al. Ubiquitin-regulated recruitment of IkappaB kinase epsilon to the MAVS interferon signaling adapter. Mol. Cell Biol. 29, 3401-3412 (2009).
    • (2009) Mol. Cell Biol. , vol.29 , pp. 3401-3412
    • Paz, S.1
  • 54
    • 29444455712 scopus 로고    scopus 로고
    • An antiviral role for the RNA interference machinery in Caenorhabditis elegans
    • Schott, D. H., Cureton, D. K., Whelan, S. P. & Hunter, C. P. An antiviral role for the RNA interference machinery in Caenorhabditis elegans. Proc. Natl Acad. Sci. USA 102, 18420-18424 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 18420-18424
    • Schott, D.H.1    Cureton, D.K.2    Whelan, S.P.3    Hunter, C.P.4
  • 56
    • 84875157258 scopus 로고    scopus 로고
    • A library of TAL effector nucleases spanning the human genome
    • Kim, Y. et al. A library of TAL effector nucleases spanning the human genome. Nature biotechnology 31, 251-258 (2013).
    • (2013) Nature Biotechnology , vol.31 , pp. 251-258
    • Kim, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.