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Volumn 11, Issue 3, 2015, Pages 1-26

PPM1A Regulates Antiviral Signaling by Antagonizing TBK1-Mediated STING Phosphorylation and Aggregation

Author keywords

[No Author keywords available]

Indexed keywords

BETA INTERFERON; GAMMA INTERFERON INDUCIBLE PROTEIN 10; INTERFERON; INTERFERON REGULATORY FACTOR; INTERFERON STIMULATED RESPONSE ELEMENT; PROTEIN KINASE; PROTEIN PHOSPHATASE 1A (MAGNESIUM MANGANESE); RANTES; TANK BINDING KINASE 1; UNCLASSIFIED DRUG; MEMBRANE PROTEIN; MPYS PROTEIN, HUMAN; MPYS PROTEIN, MOUSE; PHOSPHOPROTEIN PHOSPHATASE; PPM1A PROTEIN, HUMAN; PPM1A PROTEIN, MOUSE; PROTEIN PHOSPHATASE 2C; PROTEIN SERINE THREONINE KINASE; TBK1 PROTEIN, HUMAN; TBK1 PROTEIN, MOUSE;

EID: 84926450646     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1004783     Document Type: Article
Times cited : (96)

References (45)
  • 1
    • 80052164116 scopus 로고    scopus 로고
    • Cytoplasmic DNA innate immune pathways
    • Barber GN, (2011) Cytoplasmic DNA innate immune pathways. Immunol Rev 243: 99–108. doi: 10.1111/j.1600-065X.2011.01051.x 21884170
    • (2011) Immunol Rev , vol.243 , pp. 99-108
    • Barber, G.N.1
  • 2
    • 56549116047 scopus 로고    scopus 로고
    • Toll-like receptor and RIG-I-like receptor signaling
    • Kawai T, Akira S, (2008) Toll-like receptor and RIG-I-like receptor signaling. Ann N Y Acad Sci 1143: 1–20. doi: 10.1196/annals.1443.020 19076341
    • (2008) Ann N Y Acad Sci , vol.1143 , pp. 1-20
    • Kawai, T.1    Akira, S.2
  • 3
    • 32644456874 scopus 로고    scopus 로고
    • Antiviral innate immunity pathways
    • Seth RB, Sun L, Chen ZJ, (2006) Antiviral innate immunity pathways. Cell Res 16: 141–147. 16474426
    • (2006) Cell Res , vol.16 , pp. 141-147
    • Seth, R.B.1    Sun, L.2    Chen, Z.J.3
  • 4
    • 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, (2005) Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-kappaB and IRF 3. Cell 122: 669–682. 16125763
    • (2005) Cell , vol.122 , pp. 669-682
    • Seth, R.B.1    Sun, L.2    Ea, C.K.3    Chen, Z.J.4
  • 5
    • 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, et al. (2005) IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction. Nat Immunol 6: 981–988. 16127453
    • (2005) Nat Immunol , vol.6 , pp. 981-988
    • Kawai, T.1    Takahashi, K.2    Sato, S.3    Coban, C.4    Kumar, H.5
  • 6
    • 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, et al. (2005) VISA is an adapter protein required for virus-triggered IFN-beta signaling. Mol Cell 19: 727–740. 16153868
    • (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
  • 7
    • 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, et al. (2005) Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus. Nature 437: 1167–1172. 16177806
    • (2005) Nature , vol.437 , pp. 1167-1172
    • Meylan, E.1    Curran, J.2    Hofmann, K.3    Moradpour, D.4    Binder, M.5
  • 8
    • 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, et al. (2011) MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune response. Cell 146: 448–461. doi: 10.1016/j.cell.2011.06.041 21782231
    • (2011) Cell , vol.146 , pp. 448-461
    • Hou, F.1    Sun, L.2    Zheng, H.3    Skaug, B.4    Jiang, Q.X.5
  • 9
    • 63649133278 scopus 로고    scopus 로고
    • AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC
    • Hornung V, Ablasser A, Charrel-Dennis M, Bauernfeind F, Horvath G, et al. (2009) AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC. Nature 458: 514–518. doi: 10.1038/nature07725 19158675
    • (2009) Nature , vol.458 , pp. 514-518
    • Hornung, V.1    Ablasser, A.2    Charrel-Dennis, M.3    Bauernfeind, F.4    Horvath, G.5
  • 10
    • 60749136484 scopus 로고    scopus 로고
    • An orthogonal proteomic-genomic screen identifies AIM2 as a cytoplasmic DNA sensor for the inflammasome
    • Burckstummer T, Baumann C, Bluml S, Dixit E, Durnberger G, et al. (2009) An orthogonal proteomic-genomic screen identifies AIM2 as a cytoplasmic DNA sensor for the inflammasome. Nat Immunol 10: 266–272. doi: 10.1038/ni.1702 19158679
    • (2009) Nat Immunol , vol.10 , pp. 266-272
    • Burckstummer, T.1    Baumann, C.2    Bluml, S.3    Dixit, E.4    Durnberger, G.5
  • 11
    • 63649145255 scopus 로고    scopus 로고
    • AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA
    • Fernandes-Alnemri T, Yu JW, Datta P, Wu J, Alnemri ES, (2009) AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA. Nature 458: 509–513. doi: 10.1038/nature07710 19158676
    • (2009) Nature , vol.458 , pp. 509-513
    • Fernandes-Alnemri, T.1    Yu, J.W.2    Datta, P.3    Wu, J.4    Alnemri, E.S.5
  • 12
    • 60749104535 scopus 로고    scopus 로고
    • HIN-200 proteins regulate caspase activation in response to foreign cytoplasmic DNA
    • Roberts TL, Idris A, Dunn JA, Kelly GM, Burnton CM, et al. (2009) HIN-200 proteins regulate caspase activation in response to foreign cytoplasmic DNA. Science 323: 1057–1060. doi: 10.1126/science.1169841 19131592
    • (2009) Science , vol.323 , pp. 1057-1060
    • Roberts, T.L.1    Idris, A.2    Dunn, J.A.3    Kelly, G.M.4    Burnton, C.M.5
  • 13
    • 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, et al. (2007) DAI (DLM-1/ZBP1) is a cytosolic DNA sensor and an activator of innate immune response. Nature 448: 501–505. 17618271
    • (2007) Nature , vol.448 , pp. 501-505
    • Takaoka, A.1    Wang, Z.2    Choi, M.K.3    Yanai, H.4    Negishi, H.5
  • 14
  • 15
    • 80052969639 scopus 로고    scopus 로고
    • The helicase DDX41 senses intracellular DNA mediated by the adaptor STING in dendritic cells
    • Zhang Z, Yuan B, Bao M, Lu N, Kim T, et al. (2011) The helicase DDX41 senses intracellular DNA mediated by the adaptor STING in dendritic cells. Nat Immunol 12: 959–965. doi: 10.1038/ni.2091 21892174
    • (2011) Nat Immunol , vol.12 , pp. 959-965
    • Zhang, Z.1    Yuan, B.2    Bao, M.3    Lu, N.4    Kim, T.5
  • 16
    • 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, (2013) Cyclic GMP-AMP synthase is a cytosolic DNA sensor that activates the type I interferon pathway. Science 339: 786–791. doi: 10.1126/science.1232458 23258413
    • (2013) Science , vol.339 , pp. 786-791
    • Sun, L.1    Wu, J.2    Du, F.3    Chen, X.4    Chen, Z.J.5
  • 17
    • 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, et al. (2008) The adaptor protein MITA links virus-sensing receptors to IRF3 transcription factor activation. Immunity 29: 538–550. doi: 10.1016/j.immuni.2008.09.003 18818105
    • (2008) Immunity , vol.29 , pp. 538-550
    • Zhong, B.1    Yang, Y.2    Li, S.3    Wang, Y.Y.4    Li, Y.5
  • 18
    • 66649109939 scopus 로고    scopus 로고
    • ERIS, an endoplasmic reticulum IFN stimulator, activates innate immune signaling through dimerization
    • Sun W, Li Y, Chen L, Chen H, You F, et al. (2009) ERIS, an endoplasmic reticulum IFN stimulator, activates innate immune signaling through dimerization. Proc Natl Acad Sci U S A 106: 8653–8658. doi: 10.1073/pnas.0900850106 19433799
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 8653-8658
    • Sun, W.1    Li, Y.2    Chen, L.3    Chen, H.4    You, F.5
  • 19
    • 84869794842 scopus 로고    scopus 로고
    • STING manifests self DNA-dependent inflammatory disease
    • Ahn J, Gutman D, Saijo S, Barber GN, (2012) STING manifests self DNA-dependent inflammatory disease. Proc Natl Acad Sci U S A 109: 19386–19391. doi: 10.1073/pnas.1215006109 23132945
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 19386-19391
    • Ahn, J.1    Gutman, D.2    Saijo, S.3    Barber, G.N.4
  • 20
    • 84856301080 scopus 로고    scopus 로고
    • Autoimmunity initiates in nonhematopoietic cells and progresses via lymphocytes in an interferon-dependent autoimmune disease
    • Gall A, Treuting P, Elkon KB, Loo YM, Gale M, Jr.et al. (2012) Autoimmunity initiates in nonhematopoietic cells and progresses via lymphocytes in an interferon-dependent autoimmune disease. Immunity 36: 120–131. doi: 10.1016/j.immuni.2011.11.018 22284419
    • (2012) Immunity , vol.36 , pp. 120-131
    • Gall, A.1    Treuting, P.2    Elkon, K.B.3    Loo, Y.M.4    Gale, M.5
  • 21
    • 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, et al. (2009) The ubiquitin ligase RNF5 regulates antiviral responses by mediating degradation of the adaptor protein MITA. Immunity 30: 397–407. doi: 10.1016/j.immuni.2009.01.008 19285439
    • (2009) Immunity , vol.30 , pp. 397-407
    • Zhong, B.1    Zhang, L.2    Lei, C.3    Li, Y.4    Mao, A.P.5
  • 22
    • 73949083594 scopus 로고    scopus 로고
    • Atg9a controls dsDNA-driven dynamic translocation of STING and the innate immune response
    • Saitoh T, Fujita N, Hayashi T, Takahara K, Satoh T, et al. (2009) Atg9a controls dsDNA-driven dynamic translocation of STING and the innate immune response. Proc Natl Acad Sci U S A 106: 20842–20846. doi: 10.1073/pnas.0911267106 19926846
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 20842-20846
    • Saitoh, T.1    Fujita, N.2    Hayashi, T.3    Takahara, K.4    Satoh, T.5
  • 23
    • 84886789626 scopus 로고    scopus 로고
    • Cyclic dinucleotides trigger ULK1 (ATG1) phosphorylation of STING to prevent sustained innate immune signaling
    • Konno H, Konno K, Barber GN, (2013) Cyclic dinucleotides trigger ULK1 (ATG1) phosphorylation of STING to prevent sustained innate immune signaling. Cell 155: 688–698. doi: 10.1016/j.cell.2013.09.049 24119841
    • (2013) Cell , vol.155 , pp. 688-698
    • Konno, H.1    Konno, K.2    Barber, G.N.3
  • 24
    • 84896344782 scopus 로고    scopus 로고
    • NLRC3, a member of the NLR family of proteins, is a negative regulator of innate immune signaling induced by the DNA sensor STING
    • Zhang L, Mo J, Swanson KV, Wen H, Petrucelli A, et al. (2014) NLRC3, a member of the NLR family of proteins, is a negative regulator of innate immune signaling induced by the DNA sensor STING. Immunity 40: 329–341. doi: 10.1016/j.immuni.2014.01.010 24560620
    • (2014) Immunity , vol.40 , pp. 329-341
    • Zhang, L.1    Mo, J.2    Swanson, K.V.3    Wen, H.4    Petrucelli, A.5
  • 25
    • 84857937262 scopus 로고    scopus 로고
    • STING specifies IRF3 phosphorylation by TBK1 in the cytosolic DNA signaling pathway
    • Tanaka Y, Chen ZJ, (2012) STING specifies IRF3 phosphorylation by TBK1 in the cytosolic DNA signaling pathway. Sci Signal 5: ra20. doi: 10.1126/scisignal.2002521 22394562
    • (2012) Sci Signal , vol.5 , pp. 20
    • Tanaka, Y.1    Chen, Z.J.2
  • 26
    • 84924778328 scopus 로고    scopus 로고
    • Phosphorylation of innate immune adaptor proteins MAVS, STING, and TRIF induces IRF3 activation
    • Liu S, Cai X, Wu J, Cong Q, Chen X, et al. (2015) Phosphorylation of innate immune adaptor proteins MAVS, STING, and TRIF induces IRF3 activation. Science.
    • (2015) Science
    • Liu, S.1    Cai, X.2    Wu, J.3    Cong, Q.4    Chen, X.5
  • 27
    • 0032541227 scopus 로고    scopus 로고
    • Protein phosphatase 2Calpha inhibits the human stress-responsive p38 and JNK MAPK pathways
    • Takekawa M, Maeda T, Saito H, (1998) Protein phosphatase 2Calpha inhibits the human stress-responsive p38 and JNK MAPK pathways. EMBO J 17: 4744–4752. 9707433
    • (1998) EMBO J , vol.17 , pp. 4744-4752
    • Takekawa, M.1    Maeda, T.2    Saito, H.3
  • 28
    • 0032751695 scopus 로고    scopus 로고
    • Dephosphorylation of cyclin-dependent kinases by type 2C protein phosphatases
    • Cheng A, Ross KE, Kaldis P, Solomon MJ, (1999) Dephosphorylation of cyclin-dependent kinases by type 2C protein phosphatases. Genes Dev 13: 2946–2957. 10580002
    • (1999) Genes Dev , vol.13 , pp. 2946-2957
    • Cheng, A.1    Ross, K.E.2    Kaldis, P.3    Solomon, M.J.4
  • 29
    • 56949087707 scopus 로고    scopus 로고
    • PPM1A and PPM1B act as IKKbeta phosphatases to terminate TNFalpha-induced IKKbeta-NF-kappaB activation
    • Sun W, Yu Y, Dotti G, Shen T, Tan X, et al. (2009) PPM1A and PPM1B act as IKKbeta phosphatases to terminate TNFalpha-induced IKKbeta-NF-kappaB activation. Cell Signal 21: 95–102. doi: 10.1016/j.cellsig.2008.09.012 18930133
    • (2009) Cell Signal , vol.21 , pp. 95-102
    • Sun, W.1    Yu, Y.2    Dotti, G.3    Shen, T.4    Tan, X.5
  • 30
    • 84901834334 scopus 로고    scopus 로고
    • PPM1A is a RelA phosphatase with tumor suppressor-like activity
    • Lu X, An H, Jin R, Zou M, Guo Y, et al. (2014) PPM1A is a RelA phosphatase with tumor suppressor-like activity. Oncogene 33: 2918–2927. doi: 10.1038/onc.2013.246 23812431
    • (2014) Oncogene , vol.33 , pp. 2918-2927
    • Lu, X.1    An, H.2    Jin, R.3    Zou, M.4    Guo, Y.5
  • 31
    • 84865311481 scopus 로고    scopus 로고
    • PPM1B negatively regulates antiviral response via dephosphorylating TBK1
    • Zhao Y, Liang L, Fan Y, Sun S, An L, et al. (2012) PPM1B negatively regulates antiviral response via dephosphorylating TBK1. Cell Signal 24: 2197–2204. doi: 10.1016/j.cellsig.2012.06.017 22750291
    • (2012) Cell Signal , vol.24 , pp. 2197-2204
    • Zhao, Y.1    Liang, L.2    Fan, Y.3    Sun, S.4    An, L.5
  • 32
    • 0037779029 scopus 로고    scopus 로고
    • Probing the function of conserved residues in the serine/threonine phosphatase PP2Calpha
    • Jackson MD, Fjeld CC, Denu JM, (2003) Probing the function of conserved residues in the serine/threonine phosphatase PP2Calpha. Biochemistry 42: 8513–8521. 12859198
    • (2003) Biochemistry , vol.42 , pp. 8513-8521
    • Jackson, M.D.1    Fjeld, C.C.2    Denu, J.M.3
  • 33
    • 33646950265 scopus 로고    scopus 로고
    • PPM1A functions as a Smad phosphatase to terminate TGFbeta signaling
    • Lin X, Duan X, Liang YY, Su Y, Wrighton KH, et al. (2006) PPM1A functions as a Smad phosphatase to terminate TGFbeta signaling. Cell 125: 915–928. 16751101
    • (2006) Cell , vol.125 , pp. 915-928
    • Lin, X.1    Duan, X.2    Liang, Y.Y.3    Su, Y.4    Wrighton, K.H.5
  • 34
    • 84896381627 scopus 로고    scopus 로고
    • Prion-like polymerization underlies signal transduction in antiviral immune defense and inflammasome activation
    • Cai X, Chen J, Xu H, Liu S, Jiang QX, et al. (2014) Prion-like polymerization underlies signal transduction in antiviral immune defense and inflammasome activation. Cell 156: 1207–1222. doi: 10.1016/j.cell.2014.01.063 24630723
    • (2014) Cell , vol.156 , pp. 1207-1222
    • Cai, X.1    Chen, J.2    Xu, H.3    Liu, S.4    Jiang, Q.X.5
  • 35
    • 84896332642 scopus 로고    scopus 로고
    • Unified polymerization mechanism for the assembly of ASC-dependent inflammasomes
    • Lu A, Magupalli VG, Ruan J, Yin Q, Atianand MK, et al. (2014) Unified polymerization mechanism for the assembly of ASC-dependent inflammasomes. Cell 156: 1193–1206. doi: 10.1016/j.cell.2014.02.008 24630722
    • (2014) Cell , vol.156 , pp. 1193-1206
    • Lu, A.1    Magupalli, V.G.2    Ruan, J.3    Yin, Q.4    Atianand, M.K.5
  • 36
    • 63049091236 scopus 로고    scopus 로고
    • A systematic survey identifies prions and illuminates sequence features of prionogenic proteins
    • Alberti S, Halfmann R, King O, Kapila A, Lindquist S, (2009) A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell 137: 146–158. doi: 10.1016/j.cell.2009.02.044 19345193
    • (2009) Cell , vol.137 , pp. 146-158
    • Alberti, S.1    Halfmann, R.2    King, O.3    Kapila, A.4    Lindquist, S.5
  • 37
    • 78649941711 scopus 로고    scopus 로고
    • The Fused/Smurf complex controls the fate of Drosophila germline stem cells by generating a gradient BMP response
    • Xia L, Jia S, Huang S, Wang H, Zhu Y, et al. (2010) The Fused/Smurf complex controls the fate of Drosophila germline stem cells by generating a gradient BMP response. Cell 143: 978–990. doi: 10.1016/j.cell.2010.11.022 21145463
    • (2010) Cell , vol.143 , pp. 978-990
    • Xia, L.1    Jia, S.2    Huang, S.3    Wang, H.4    Zhu, Y.5
  • 38
    • 69249133298 scopus 로고    scopus 로고
    • Polo-like kinase 1 (PLK1) regulates interferon (IFN) induction by MAVS
    • Vitour D, Dabo S, Ahmadi Pour M, Vilasco M, Vidalain PO, et al. (2009) Polo-like kinase 1 (PLK1) regulates interferon (IFN) induction by MAVS. J Biol Chem 284: 21797–21809. doi: 10.1074/jbc.M109.018275 19546225
    • (2009) J Biol Chem , vol.284 , pp. 21797-21809
    • Vitour, D.1    Dabo, S.2    Ahmadi, P.M.3    Vilasco, M.4    Vidalain, P.O.5
  • 39
    • 0038393016 scopus 로고    scopus 로고
    • IKKepsilon and TBK1 are essential components of the IRF3 signaling pathway
    • Fitzgerald KA, McWhirter SM, Faia KL, Rowe DC, Latz E, et al. (2003) IKKepsilon and TBK1 are essential components of the IRF3 signaling pathway. Nat Immunol 4: 491–496. 12692549
    • (2003) Nat Immunol , vol.4 , pp. 491-496
    • Fitzgerald, K.A.1    McWhirter, S.M.2    Faia, K.L.3    Rowe, D.C.4    Latz, E.5
  • 40
    • 66949172391 scopus 로고    scopus 로고
    • Role of nuclear-encoded subunit Vb in the assembly and stability of cytochrome c oxidase complex: implications in mitochondrial dysfunction and ROS production
    • Galati D, Srinivasan S, Raza H, Prabu SK, Hardy M, et al. (2009) Role of nuclear-encoded subunit Vb in the assembly and stability of cytochrome c oxidase complex: implications in mitochondrial dysfunction and ROS production. Biochem J 420: 439–449. doi: 10.1042/BJ20090214 19338496
    • (2009) Biochem J , vol.420 , pp. 439-449
    • Galati, D.1    Srinivasan, S.2    Raza, H.3    Prabu, S.K.4    Hardy, M.5
  • 41
    • 70349943834 scopus 로고    scopus 로고
    • STING regulates intracellular DNA-mediated, type I interferon-dependent innate immunity
    • Ishikawa H, Ma Z, Barber GN, (2009) STING regulates intracellular DNA-mediated, type I interferon-dependent innate immunity. Nature 461: 788–792. doi: 10.1038/nature08476 19776740
    • (2009) Nature , vol.461 , pp. 788-792
    • Ishikawa, H.1    Ma, Z.2    Barber, G.N.3
  • 42
    • 82755176160 scopus 로고    scopus 로고
    • Delayed re-epithelialization in Ppm1a gene-deficient mice is mediated by enhanced activation of Smad2
    • Yang X, Teng Y, Hou N, Fan X, Cheng X, et al. (2011) Delayed re-epithelialization in Ppm1a gene-deficient mice is mediated by enhanced activation of Smad2. J Biol Chem 286: 42267–42273. doi: 10.1074/jbc.M111.292284 21990361
    • (2011) J Biol Chem , vol.286 , pp. 42267-42273
    • Yang, X.1    Teng, Y.2    Hou, N.3    Fan, X.4    Cheng, X.5
  • 43
    • 33646592188 scopus 로고    scopus 로고
    • The specific and essential role of MAVS in antiviral innate immune responses
    • Sun Q, Sun L, Liu HH, Chen X, Seth RB, et al. (2006) The specific and essential role of MAVS in antiviral innate immune responses. Immunity 24: 633–642. 16713980
    • (2006) Immunity , vol.24 , pp. 633-642
    • Sun, Q.1    Sun, L.2    Liu, H.H.3    Chen, X.4    Seth, R.B.5
  • 44
    • 80054694130 scopus 로고    scopus 로고
    • Activation of STAT6 by STING is critical for antiviral innate immunity
    • Chen H, Sun H, You F, Sun W, Zhou X, et al. (2011) Activation of STAT6 by STING is critical for antiviral innate immunity. Cell 147: 436–446. doi: 10.1016/j.cell.2011.09.022 22000020
    • (2011) Cell , vol.147 , pp. 436-446
    • Chen, H.1    Sun, H.2    You, F.3    Sun, W.4    Zhou, X.5
  • 45
    • 84872040983 scopus 로고    scopus 로고
    • COX5B regulates MAVS-mediated antiviral signaling through interaction with ATG5 and repressing ROS production
    • Zhao Y, Sun X, Nie X, Sun L, Tang TS, et al. (2012) COX5B regulates MAVS-mediated antiviral signaling through interaction with ATG5 and repressing ROS production. PLoS Pathog 8: e1003086. doi: 10.1371/journal.ppat.1003086 23308066
    • (2012) PLoS Pathog , vol.8 , pp. 1003086
    • Zhao, Y.1    Sun, X.2    Nie, X.3    Sun, L.4    Tang, T.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.