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Volumn 25, Issue 5, 2014, Pages 507-512

Antiviral RNA recognition and assembly by RLR family innate immune sensors

Author keywords

Antiviral; Interferon; LGP2; MDA5; RIG I

Indexed keywords

BETA INTERFERON; CYTOPLASM PROTEIN; MEMBRANE PROTEIN; MESSENGER RNA; PROTEIN LGP2; PROTEIN MDA5; RECEPTOR; RIBONUCLEOPROTEIN; RIG I LIKE RECEPTOR; RNA; UNCLASSIFIED DRUG; DEAD BOX PROTEIN; SIGNAL RECOGNITION PARTICLE;

EID: 84908322828     PISSN: 13596101     EISSN: 18790305     Source Type: Journal    
DOI: 10.1016/j.cytogfr.2014.07.006     Document Type: Article
Times cited : (61)

References (82)
  • 1
    • 80052143412 scopus 로고    scopus 로고
    • RIG-I-like receptors: cytoplasmic sensors for non-self RNA
    • Kato H., Takahasi K., Fujita T. RIG-I-like receptors: cytoplasmic sensors for non-self RNA. Immunol Rev 2011, 243:91-98.
    • (2011) Immunol Rev , vol.243 , pp. 91-98
    • Kato, H.1    Takahasi, K.2    Fujita, T.3
  • 3
    • 84887990870 scopus 로고    scopus 로고
    • Mechanisms of MAVS regulation at the mitochondrial membrane
    • Jacobs J.L., Coyne C.B. Mechanisms of MAVS regulation at the mitochondrial membrane. J Mol Biol 2013, 425:5009-5019.
    • (2013) J Mol Biol , vol.425 , pp. 5009-5019
    • Jacobs, J.L.1    Coyne, C.B.2
  • 4
    • 82955178645 scopus 로고    scopus 로고
    • Cytosolic surveillance and antiviral immunity
    • Rathinam V.A., Fitzgerald K.A. Cytosolic surveillance and antiviral immunity. Curr Opin Virol 2011, 1:455-462.
    • (2011) Curr Opin Virol , vol.1 , pp. 455-462
    • Rathinam, V.A.1    Fitzgerald, K.A.2
  • 5
    • 23844438864 scopus 로고    scopus 로고
    • Shared and unique functions of the DExD/H-box helicases RIG-I, MDA5, and LGP2 in antiviral innate immunity
    • Yoneyama M., Kikuchi M., Matsumoto K., Imaizumi T., Miyagishi M., Taira K., et al. Shared and unique functions of the DExD/H-box helicases RIG-I, MDA5, and LGP2 in antiviral innate immunity. J Immunol 2005, 175:2851-2858.
    • (2005) J Immunol , vol.175 , pp. 2851-2858
    • Yoneyama, M.1    Kikuchi, M.2    Matsumoto, K.3    Imaizumi, T.4    Miyagishi, M.5    Taira, K.6
  • 6
    • 79959649316 scopus 로고    scopus 로고
    • RIG-I like receptors and their signaling crosstalk in the regulation of antiviral immunity
    • Ramos H.J., Gale M. RIG-I like receptors and their signaling crosstalk in the regulation of antiviral immunity. Curr Opin Virol 2011, 1:167-176.
    • (2011) Curr Opin Virol , vol.1 , pp. 167-176
    • Ramos, H.J.1    Gale, M.2
  • 7
    • 33344473656 scopus 로고    scopus 로고
    • The DEAD-box protein family of RNA helicases
    • Cordin O., Banroques J., Tanner N.K., Linder P. The DEAD-box protein family of RNA helicases. Gene 2006, 367:17-37.
    • (2006) Gene , vol.367 , pp. 17-37
    • Cordin, O.1    Banroques, J.2    Tanner, N.K.3    Linder, P.4
  • 8
    • 65649083024 scopus 로고    scopus 로고
    • Regulation of signal transduction by enzymatically inactive antiviral RNA helicase proteins MDA5, RIG-I, and LGP2
    • Bamming D., Horvath C.M. Regulation of signal transduction by enzymatically inactive antiviral RNA helicase proteins MDA5, RIG-I, and LGP2. J Biol Chem 2009, 284:9700-9712.
    • (2009) J Biol Chem , vol.284 , pp. 9700-9712
    • Bamming, D.1    Horvath, C.M.2
  • 9
    • 48249113056 scopus 로고    scopus 로고
    • Translocation and unwinding mechanisms of RNA and DNA helicases
    • Pyle A.M. Translocation and unwinding mechanisms of RNA and DNA helicases. Ann Rev Biophys 2008, 37:317-336.
    • (2008) Ann Rev Biophys , vol.37 , pp. 317-336
    • Pyle, A.M.1
  • 10
    • 67649413594 scopus 로고    scopus 로고
    • The RIG-I-like receptor LGP2 recognizes the termini of double-stranded RNA
    • Li X., Ranjith-Kumar C.T., Brooks M.T., Dharmaiah S., Herr A.B., Kao C., et al. The RIG-I-like receptor LGP2 recognizes the termini of double-stranded RNA. J Biol Chem 2009, 284:13881-13891.
    • (2009) J Biol Chem , vol.284 , pp. 13881-13891
    • Li, X.1    Ranjith-Kumar, C.T.2    Brooks, M.T.3    Dharmaiah, S.4    Herr, A.B.5    Kao, C.6
  • 11
    • 33846307026 scopus 로고    scopus 로고
    • Regulation of innate antiviral defenses through a shared repressor domain in RIG-I and LGP2
    • Saito T., Hirai R., Loo Y.M., Owen D., Johnson C.L., Sinha S.C., et al. Regulation of innate antiviral defenses through a shared repressor domain in RIG-I and LGP2. Proc Natl Acad Sci USA 2007, 104:582-587.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 582-587
    • Saito, T.1    Hirai, R.2    Loo, Y.M.3    Owen, D.4    Johnson, C.L.5    Sinha, S.C.6
  • 12
    • 81555204380 scopus 로고    scopus 로고
    • Structural basis of RNA recognition and activation by innate immune receptor RIG-I
    • Jiang F., Ramanathan A., Miller M.T., Tang G.Q., Gale M., Patel S.S., et al. Structural basis of RNA recognition and activation by innate immune receptor RIG-I. Nature 2011, 479:423-427.
    • (2011) Nature , vol.479 , pp. 423-427
    • Jiang, F.1    Ramanathan, A.2    Miller, M.T.3    Tang, G.Q.4    Gale, M.5    Patel, S.S.6
  • 13
    • 38649089789 scopus 로고    scopus 로고
    • The C-terminal regulatory domain is the RNA 5'-triphosphate sensor of RIG-I
    • Cui S., Eisenacher K., Kirchhofer A., Brzozka K., Lammens A., Lammens K., et al. The C-terminal regulatory domain is the RNA 5'-triphosphate sensor of RIG-I. Mol Cell 2008, 29:169-179.
    • (2008) Mol Cell , vol.29 , pp. 169-179
    • Cui, S.1    Eisenacher, K.2    Kirchhofer, A.3    Brzozka, K.4    Lammens, A.5    Lammens, K.6
  • 14
    • 67651232539 scopus 로고    scopus 로고
    • Structural basis of double-stranded RNA recognition by the RIG-I like receptor MDA5
    • Li X., Lu C., Stewart M., Xu H., Strong R.K., Igumenova T., et al. Structural basis of double-stranded RNA recognition by the RIG-I like receptor MDA5. Arch Biochem Biophys 2009, 488:23-33.
    • (2009) Arch Biochem Biophys , vol.488 , pp. 23-33
    • Li, X.1    Lu, C.2    Stewart, M.3    Xu, H.4    Strong, R.K.5    Igumenova, T.6
  • 15
    • 67650510680 scopus 로고    scopus 로고
    • Solution structures of cytosolic RNA sensor MDA5 and LGP2 C-terminal domains: identification of the RNA recognition loop in RIG-I-like receptors
    • Takahasi K., Kumeta H., Tsuduki N., Narita R., Shigemoto T., Hirai R., et al. Solution structures of cytosolic RNA sensor MDA5 and LGP2 C-terminal domains: identification of the RNA recognition loop in RIG-I-like receptors. J Biol Chem 2009, 284:17465-17474.
    • (2009) J Biol Chem , vol.284 , pp. 17465-17474
    • Takahasi, K.1    Kumeta, H.2    Tsuduki, N.3    Narita, R.4    Shigemoto, T.5    Hirai, R.6
  • 16
    • 39649092731 scopus 로고    scopus 로고
    • Nonself RNA-sensing mechanism of RIG-I helicase and activation of antiviral immune responses
    • Takahasi K., Yoneyama M., Nishihori T., Hirai R., Kumeta H., Narita R., et al. Nonself RNA-sensing mechanism of RIG-I helicase and activation of antiviral immune responses. Mol Cell 2008, 29:428-440.
    • (2008) Mol Cell , vol.29 , pp. 428-440
    • Takahasi, K.1    Yoneyama, M.2    Nishihori, T.3    Hirai, R.4    Kumeta, H.5    Narita, R.6
  • 18
    • 84898747432 scopus 로고    scopus 로고
    • Structural basis for the prion-like MAVS filaments in antiviral innate immunity
    • Xu H., He X., Zheng H., Huang L.J., Hou F., Yu Z., et al. Structural basis for the prion-like MAVS filaments in antiviral innate immunity. eLife 2014, 3:e01489.
    • (2014) eLife , vol.3 , pp. e01489
    • Xu, H.1    He, X.2    Zheng, H.3    Huang, L.J.4    Hou, F.5    Yu, Z.6
  • 19
    • 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 Q.X., Chen Z.J. 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
  • 20
    • 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., 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
  • 22
    • 80054703126 scopus 로고    scopus 로고
    • Structural basis for the activation of innate immune pattern-recognition receptor RIG-I by viral RNA
    • Kowalinski E., Lunardi T., McCarthy A.A., Louber J., Brunel J., Grigorov B., et al. Structural basis for the activation of innate immune pattern-recognition receptor RIG-I by viral RNA. Cell 2011, 147:423-435.
    • (2011) Cell , vol.147 , pp. 423-435
    • Kowalinski, E.1    Lunardi, T.2    McCarthy, A.A.3    Louber, J.4    Brunel, J.5    Grigorov, B.6
  • 23
    • 77954754505 scopus 로고    scopus 로고
    • Induction of type I interferon by RNA viruses: cellular receptors and their substrates
    • Baum A., Garcia-Sastre A. Induction of type I interferon by RNA viruses: cellular receptors and their substrates. Amino Acids 2010, 38:1283-1299.
    • (2010) Amino Acids , vol.38 , pp. 1283-1299
    • Baum, A.1    Garcia-Sastre, A.2
  • 24
    • 33646342149 scopus 로고    scopus 로고
    • Differential roles of MDA5 and RIG-I helicases in the recognition of RNA viruses
    • Kato H., Takeuchi O., Sato S., Yoneyama M., Yamamoto M., Matsui K., et al. Differential roles of MDA5 and RIG-I helicases in the recognition of RNA viruses. Nature 2006, 441:101-105.
    • (2006) Nature , vol.441 , pp. 101-105
    • Kato, H.1    Takeuchi, O.2    Sato, S.3    Yoneyama, M.4    Yamamoto, M.5    Matsui, K.6
  • 25
    • 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 P.V., Kirchhofer A., Gack M.U., Jung J.U., 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
  • 26
    • 84555178934 scopus 로고    scopus 로고
    • Structural insights into the activation of RIG-I, a nanosensor for viral RNAs
    • Jiang Q.X., Chen Z.J. Structural insights into the activation of RIG-I, a nanosensor for viral RNAs. EMBO Rep 2012, 13:7-8.
    • (2012) EMBO Rep , vol.13 , pp. 7-8
    • Jiang, Q.X.1    Chen, Z.J.2
  • 27
    • 84883488816 scopus 로고    scopus 로고
    • Defining the functional determinants for RNA surveillance by RIG-I
    • Kohlway A., Luo D., Rawling D.C., Ding S.C., Pyle A.M. Defining the functional determinants for RNA surveillance by RIG-I. EMBO Rep 2013, 14:772-779.
    • (2013) EMBO Rep , vol.14 , pp. 772-779
    • Kohlway, A.1    Luo, D.2    Rawling, D.C.3    Ding, S.C.4    Pyle, A.M.5
  • 28
    • 84883487585 scopus 로고    scopus 로고
    • ATPase-driven oligomerization of RIG-I on RNA allows optimal activation of type-I interferon
    • Patel J.R., Jain A., Chou Y.Y., Baum A., Ha T., Garcia-Sastre A. ATPase-driven oligomerization of RIG-I on RNA allows optimal activation of type-I interferon. EMBO Rep 2013, 14:780-787.
    • (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    Garcia-Sastre, A.6
  • 29
    • 84883759334 scopus 로고    scopus 로고
    • RIG-I forms signaling-competent filaments in an ATP-dependent, ubiquitin-independent manner
    • Peisley A., Wu B., Yao H., Walz T., Hur S. RIG-I forms signaling-competent filaments in an ATP-dependent, ubiquitin-independent manner. Mol Cell 2013, 51:573-583.
    • (2013) Mol Cell , vol.51 , pp. 573-583
    • Peisley, A.1    Wu, B.2    Yao, H.3    Walz, T.4    Hur, S.5
  • 30
    • 84855218318 scopus 로고    scopus 로고
    • Ubiquitin-mediated modulation of the cytoplasmic viral RNA sensor RIG-I
    • Oshiumi H., Matsumoto M., Seya T. Ubiquitin-mediated modulation of the cytoplasmic viral RNA sensor RIG-I. J Biochem 2012, 151:5-11.
    • (2012) J Biochem , vol.151 , pp. 5-11
    • Oshiumi, H.1    Matsumoto, M.2    Seya, T.3
  • 31
    • 84860499060 scopus 로고    scopus 로고
    • Emerging role of ubiquitination in antiviral RIG-I signaling
    • Maelfait J., Beyaert R. Emerging role of ubiquitination in antiviral RIG-I signaling. Microbiol Mol Biol Rev: MMBR 2012, 76:33-45.
    • (2012) Microbiol Mol Biol Rev: MMBR , vol.76 , pp. 33-45
    • Maelfait, J.1    Beyaert, R.2
  • 32
    • 34247341367 scopus 로고    scopus 로고
    • TRIM25 RING-finger E3 ubiquitin ligase is essential for RIG-I-mediated antiviral activity
    • Gack M.U., Shin Y.C., Joo C.H., Urano T., Liang C., Sun L., 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
  • 33
    • 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., 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
    • Zeng, W.1    Sun, L.2    Jiang, X.3    Chen, X.4    Hou, F.5    Adhikari, A.6
  • 34
    • 84899957213 scopus 로고    scopus 로고
    • Structural basis for ubiquitin-mediated antiviral signal activation by RIG-I
    • Peisley A., Wu B., Xu H., Chen Z.J., Hur S. Structural basis for ubiquitin-mediated antiviral signal activation by RIG-I. Nature 2014, 509:110-114.
    • (2014) Nature , vol.509 , pp. 110-114
    • Peisley, A.1    Wu, B.2    Xu, H.3    Chen, Z.J.4    Hur, S.5
  • 35
    • 84872348735 scopus 로고    scopus 로고
    • ATP hydrolysis enhances RNA recognition and antiviral signal transduction by the innate immune sensor, Laboratory of Genetics and Physiology 2 (LGP2)
    • Bruns A.M., Pollpeter D., Hadizadeh N., Myong S., Marko J.F., Horvath C.M. ATP hydrolysis enhances RNA recognition and antiviral signal transduction by the innate immune sensor, Laboratory of Genetics and Physiology 2 (LGP2). J Biol Chem 2013, 288:938-946.
    • (2013) J Biol Chem , vol.288 , pp. 938-946
    • Bruns, A.M.1    Pollpeter, D.2    Hadizadeh, N.3    Myong, S.4    Marko, J.F.5    Horvath, C.M.6
  • 36
    • 84875542059 scopus 로고    scopus 로고
    • Dephosphorylation of the RNA sensors RIG-I and MDA5 by the phosphatase PP1 is essential for innate immune signaling
    • Wies E., Wang M.K., Maharaj N.P., Chen K., Zhou S., Finberg R.W., et al. Dephosphorylation of the RNA sensors RIG-I and MDA5 by the phosphatase PP1 is essential for innate immune signaling. Immunity 2013, 38:437-449.
    • (2013) Immunity , vol.38 , pp. 437-449
    • Wies, E.1    Wang, M.K.2    Maharaj, N.P.3    Chen, K.4    Zhou, S.5    Finberg, R.W.6
  • 38
    • 80053590435 scopus 로고    scopus 로고
    • Orchestrating the interferon antiviral response through the mitochondrial antiviral signaling (MAVS) adapter
    • Belgnaoui S.M., Paz S., Hiscott J. Orchestrating the interferon antiviral response through the mitochondrial antiviral signaling (MAVS) adapter. Curr Opin Immunol 2011, 23:564-572.
    • (2011) Curr Opin Immunol , vol.23 , pp. 564-572
    • Belgnaoui, S.M.1    Paz, S.2    Hiscott, J.3
  • 39
    • 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., Vilasco M., Werden S.J., Arguello M., Joseph-Pillai D., Zhao T., et al. A functional C-terminal TRAF3-binding site in MAVS participates in positive and negative regulation of the IFN antiviral response. Cell Res 2011, 21:895-910.
    • (2011) Cell Res , vol.21 , pp. 895-910
    • Paz, S.1    Vilasco, M.2    Werden, S.J.3    Arguello, M.4    Joseph-Pillai, D.5    Zhao, T.6
  • 40
    • 33744791510 scopus 로고    scopus 로고
    • Essential role of mda-5 in type I IFN responses to polyriboinosinic:polyribocytidylic acid and encephalomyocarditis picornavirus
    • Gitlin L., Barchet W., Gilfillan S., Cella M., Beutler B., Flavell R.A., et al. Essential role of mda-5 in type I IFN responses to polyriboinosinic:polyribocytidylic acid and encephalomyocarditis picornavirus. Proc Natl Acad Sci USA 2006, 103:8459-8464.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 8459-8464
    • Gitlin, L.1    Barchet, W.2    Gilfillan, S.3    Cella, M.4    Beutler, B.5    Flavell, R.A.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., 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
  • 43
    • 70349728538 scopus 로고    scopus 로고
    • Activation of MDA5 requires higher-order RNA structures generated during virus infection
    • Pichlmair A., Schulz O., Tan C.P., Rehwinkel J., Kato H., Takeuchi O., et al. Activation of MDA5 requires higher-order RNA structures generated during virus infection. J Virol 2009, 83:10761-10769.
    • (2009) J Virol , vol.83 , pp. 10761-10769
    • Pichlmair, A.1    Schulz, O.2    Tan, C.P.3    Rehwinkel, J.4    Kato, H.5    Takeuchi, O.6
  • 44
    • 78751637122 scopus 로고    scopus 로고
    • Ribose 2'-O-methylation provides a molecular signature for the distinction of self and non-self mRNA dependent on the RNA sensor Mda5
    • Zust R., Cervantes-Barragan L., Habjan M., Maier R., Neuman B.W., Ziebuhr J., et al. Ribose 2'-O-methylation provides a molecular signature for the distinction of self and non-self mRNA dependent on the RNA sensor Mda5. Nat Immunol 2011, 12:137-143.
    • (2011) Nat Immunol , vol.12 , pp. 137-143
    • Zust, R.1    Cervantes-Barragan, L.2    Habjan, M.3    Maier, R.4    Neuman, B.W.5    Ziebuhr, J.6
  • 45
    • 79952125382 scopus 로고    scopus 로고
    • Activation of IFN expression by a viral mRNA through RNase L and MDA5
    • Luthra P., Sun D., Silverman R.H., He B. Activation of IFN expression by a viral mRNA through RNase L and MDA5. Proc Natl Acad Sci USA 2011, 108:2118-2123.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 2118-2123
    • Luthra, P.1    Sun, D.2    Silverman, R.H.3    He, B.4
  • 46
    • 84898722385 scopus 로고    scopus 로고
    • Identification of an LGP2-associated MDA5 agonist in picornavirus-infected cells
    • Deddouche S., Goubau D., Rehwinkel J., Chakravarty P., Begum S., Maillard P.V., et al. Identification of an LGP2-associated MDA5 agonist in picornavirus-infected cells. eLife 2014, 3:e01535.
    • (2014) eLife , vol.3 , pp. e01535
    • Deddouche, S.1    Goubau, D.2    Rehwinkel, J.3    Chakravarty, P.4    Begum, S.5    Maillard, P.V.6
  • 47
    • 84903880722 scopus 로고    scopus 로고
    • MDA5 and LGP2: accomplices and antagonists of antiviral signal transduction
    • Rodriguez K.R., Bruns A.M., Horvath C.M. MDA5 and LGP2: accomplices and antagonists of antiviral signal transduction. J Virol 2014.
    • (2014) J Virol
    • Rodriguez, K.R.1    Bruns, A.M.2    Horvath, C.M.3
  • 48
    • 84874269512 scopus 로고    scopus 로고
    • Structural basis of innate immune recognition of viral RNA
    • Berke I.C., Li Y., Modis Y. Structural basis of innate immune recognition of viral RNA. Cell Microbiol 2012.
    • (2012) Cell Microbiol
    • Berke, I.C.1    Li, Y.2    Modis, Y.3
  • 49
    • 84859427527 scopus 로고    scopus 로고
    • MDA5 cooperatively forms dimers and ATP-sensitive filaments upon binding double-stranded RNA
    • Berke I.C., Modis Y. MDA5 cooperatively forms dimers and ATP-sensitive filaments upon binding double-stranded RNA. EMBO J 2012, 31:1714-1726.
    • (2012) EMBO J , vol.31 , pp. 1714-1726
    • Berke, I.C.1    Modis, Y.2
  • 50
    • 84868538362 scopus 로고    scopus 로고
    • MDA5 assembles into a polar helical filament on dsRNA
    • Berke I.C., Yu X., Modis Y., Egelman E.H. MDA5 assembles into a polar helical filament on dsRNA. Proc Natl Acad Sci USA 2012, 109:18437-18441.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 18437-18441
    • Berke, I.C.1    Yu, X.2    Modis, Y.3    Egelman, E.H.4
  • 51
    • 84870614532 scopus 로고    scopus 로고
    • Kinetic mechanism for viral dsRNA length discrimination by MDA5 filaments
    • Peisley A., Jo M.H., Lin C., Wu B., Orme-Johnson M., Walz T., et al. Kinetic mechanism for viral dsRNA length discrimination by MDA5 filaments. Proc Natl Acad Sci USA 2012, 109:E3340-E3349.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. E3340-E3349
    • Peisley, A.1    Jo, M.H.2    Lin, C.3    Wu, B.4    Orme-Johnson, M.5    Walz, T.6
  • 52
    • 84873523444 scopus 로고    scopus 로고
    • Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling
    • Motz C., Schuhmann K.M., Kirchhofer A., Moldt M., Witte G., Conzelmann K.K., et al. Paramyxovirus V proteins disrupt the fold of the RNA sensor MDA5 to inhibit antiviral signaling. Science 2013, 339:690-693.
    • (2013) Science , vol.339 , pp. 690-693
    • Motz, C.1    Schuhmann, K.M.2    Kirchhofer, A.3    Moldt, M.4    Witte, G.5    Conzelmann, K.K.6
  • 53
    • 84872604349 scopus 로고    scopus 로고
    • Structural basis for dsRNA recognition, filament formation, and antiviral signal activation by MDA5
    • Wu B., Peisley A., Richards C., Yao H., Zeng X., Lin C., et al. Structural basis for dsRNA recognition, filament formation, and antiviral signal activation by MDA5. Cell 2013, 152:276-289.
    • (2013) Cell , vol.152 , pp. 276-289
    • Wu, B.1    Peisley, A.2    Richards, C.3    Yao, H.4    Zeng, X.5    Lin, C.6
  • 54
    • 84870476784 scopus 로고    scopus 로고
    • MDA5 detects the double-stranded RNA replicative form in picornavirus-infected cells
    • Feng Q., Hato S.V., Langereis M.A., Zoll J., Virgen-Slane R., Peisley A., et al. MDA5 detects the double-stranded RNA replicative form in picornavirus-infected cells. Cell Rep 2012, 2:1187-1196.
    • (2012) Cell Rep , vol.2 , pp. 1187-1196
    • Feng, Q.1    Hato, S.V.2    Langereis, M.A.3    Zoll, J.4    Virgen-Slane, R.5    Peisley, A.6
  • 55
    • 84862909216 scopus 로고    scopus 로고
    • Cooperative assembly and dynamic disassembly of MDA5 filaments for viral dsRNA recognition
    • Peisley A., Lin C., Wu B., Orme-Johnson M., Liu M., Walz T., et al. Cooperative assembly and dynamic disassembly of MDA5 filaments for viral dsRNA recognition. Proc Natl Acad Sci USA 2011, 108:21010-21015.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 21010-21015
    • Peisley, A.1    Lin, C.2    Wu, B.3    Orme-Johnson, M.4    Liu, M.5    Walz, T.6
  • 56
    • 0037154176 scopus 로고    scopus 로고
    • Mda-5: an interferon-inducible putative RNA helicase with double-stranded RNA-dependent ATPase activity and melanoma growth-suppressive properties
    • Kang D.C., Gopalkrishnan R.V., Wu Q., Jankowsky E., Pyle A.M., Fisher P.B. mda-5: an interferon-inducible putative RNA helicase with double-stranded RNA-dependent ATPase activity and melanoma growth-suppressive properties. Proc Natl Acad Sci USA 2002, 99:637-642.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 637-642
    • Kang, D.C.1    Gopalkrishnan, R.V.2    Wu, Q.3    Jankowsky, E.4    Pyle, A.M.5    Fisher, P.B.6
  • 57
    • 1642348822 scopus 로고    scopus 로고
    • Expression analysis and genomic characterization of human melanoma differentiation associated gene-5, mda-5: a novel type I interferon-responsive apoptosis-inducing gene
    • Kang D.C., Gopalkrishnan R.V., Lin L., Randolph A., Valerie K., Pestka S., et al. Expression analysis and genomic characterization of human melanoma differentiation associated gene-5, mda-5: a novel type I interferon-responsive apoptosis-inducing gene. Oncogene 2004, 23:1789-1800.
    • (2004) Oncogene , vol.23 , pp. 1789-1800
    • Kang, D.C.1    Gopalkrishnan, R.V.2    Lin, L.3    Randolph, A.4    Valerie, K.5    Pestka, S.6
  • 58
    • 0037076217 scopus 로고    scopus 로고
    • Overexpression of Helicard, a CARD-containing helicase cleaved during apoptosis, accelerates DNA degradation
    • Kovacsovics M., Martinon F., Micheau O., Bodmer J.L., Hofmann K., Tschopp J. Overexpression of Helicard, a CARD-containing helicase cleaved during apoptosis, accelerates DNA degradation. Curr Biol: CB 2002, 12:838-843.
    • (2002) Curr Biol: CB , vol.12 , pp. 838-843
    • Kovacsovics, M.1    Martinon, F.2    Micheau, O.3    Bodmer, J.L.4    Hofmann, K.5    Tschopp, J.6
  • 59
    • 33745240931 scopus 로고    scopus 로고
    • A genome-wide association study of nonsynonymous SNPs identifies a type 1 diabetes locus in the interferon-induced helicase (IFIH1) region
    • Smyth D.J., Cooper J.D., Bailey R., Field S., Burren O., Smink L.J., et al. A genome-wide association study of nonsynonymous SNPs identifies a type 1 diabetes locus in the interferon-induced helicase (IFIH1) region. Nat Genet 2006, 38:617-619.
    • (2006) Nat Genet , vol.38 , pp. 617-619
    • Smyth, D.J.1    Cooper, J.D.2    Bailey, R.3    Field, S.4    Burren, O.5    Smink, L.J.6
  • 60
    • 80051619284 scopus 로고    scopus 로고
    • Autoimmune disease risk variant of IFIH1 is associated with increased sensitivity to IFN-alpha and serologic autoimmunity in lupus patients
    • Robinson T., Kariuki S.N., Franek B.S., Kumabe M., Kumar A.A., Badaracco M., et al. Autoimmune disease risk variant of IFIH1 is associated with increased sensitivity to IFN-alpha and serologic autoimmunity in lupus patients. J Immunol 2011, 187:1298-1303.
    • (2011) J Immunol , vol.187 , pp. 1298-1303
    • Robinson, T.1    Kariuki, S.N.2    Franek, B.S.3    Kumabe, M.4    Kumar, A.A.5    Badaracco, M.6
  • 61
    • 84893075305 scopus 로고    scopus 로고
    • Regulation of type I interferon responses
    • Ivashkiv L.B., Donlin L.T. Regulation of type I interferon responses. Nat Rev Immunol 2014, 14:36-49.
    • (2014) Nat Rev Immunol , vol.14 , pp. 36-49
    • Ivashkiv, L.B.1    Donlin, L.T.2
  • 62
    • 84894028950 scopus 로고    scopus 로고
    • Autoimmune disorders associated with gain of function of the intracellular sensor MDA5
    • Funabiki M., Kato H., Miyachi Y., Toki H., Motegi H., Inoue M., et al. Autoimmune disorders associated with gain of function of the intracellular sensor MDA5. Immunity 2014, 40:199-212.
    • (2014) Immunity , vol.40 , pp. 199-212
    • Funabiki, M.1    Kato, H.2    Miyachi, Y.3    Toki, H.4    Motegi, H.5    Inoue, M.6
  • 63
    • 84899534322 scopus 로고    scopus 로고
    • MDA5 and autoimmune disease
    • Miner J.J., Diamond M.S. MDA5 and autoimmune disease. Nat Genet 2014, 46:418-419.
    • (2014) Nat Genet , vol.46 , pp. 418-419
    • Miner, J.J.1    Diamond, M.S.2
  • 64
    • 18544373226 scopus 로고    scopus 로고
    • Errata: overexpression of Helicard, a CARD-containing helicase cleaved during apoptosis, accelerates DNA degradation
    • Kovacsovics M., Martinon F., Micheau O., Bodmer J.L., Hofmann K., Tschopp J. Errata: overexpression of Helicard, a CARD-containing helicase cleaved during apoptosis, accelerates DNA degradation. Curr Biol: CB 2002, 12:1633.
    • (2002) Curr Biol: CB , vol.12 , pp. 1633
    • Kovacsovics, M.1    Martinon, F.2    Micheau, O.3    Bodmer, J.L.4    Hofmann, K.5    Tschopp, J.6
  • 65
    • 84893811728 scopus 로고    scopus 로고
    • The laboratory of genetics and physiology 2: emerging insights into the controversial functions of this RIG-I-like receptor
    • Zhu Z., Zhang X., Wang G., Zheng H. The laboratory of genetics and physiology 2: emerging insights into the controversial functions of this RIG-I-like receptor. BioMed Res Int 2014, 2014:960190.
    • (2014) BioMed Res Int , vol.2014 , pp. 960190
    • Zhu, Z.1    Zhang, X.2    Wang, G.3    Zheng, H.4
  • 66
    • 33845431988 scopus 로고    scopus 로고
    • RNA- and virus-independent inhibition of antiviral signaling by RNA helicase LGP2
    • Komuro A., Horvath C.M. RNA- and virus-independent inhibition of antiviral signaling by RNA helicase LGP2. J Virol 2006, 80:12332-12342.
    • (2006) J Virol , vol.80 , pp. 12332-12342
    • Komuro, A.1    Horvath, C.M.2
  • 67
    • 26844503987 scopus 로고    scopus 로고
    • The RNA helicase Lgp2 inhibits TLR-independent sensing of viral replication by retinoic acid-inducible gene-I
    • Rothenfusser S., Goutagny N., DiPerna G., Gong M., Monks B.G., Schoenemeyer A., et al. The RNA helicase Lgp2 inhibits TLR-independent sensing of viral replication by retinoic acid-inducible gene-I. J Immunol 2005, 175:5260-5268.
    • (2005) J Immunol , vol.175 , pp. 5260-5268
    • Rothenfusser, S.1    Goutagny, N.2    DiPerna, G.3    Gong, M.4    Monks, B.G.5    Schoenemeyer, A.6
  • 70
    • 34248168157 scopus 로고    scopus 로고
    • Loss of DExD/H box RNA helicase LGP2 manifests disparate antiviral responses
    • Venkataraman T., Valdes M., Elsby R., Kakuta S., Caceres G., Saijo S., et al. Loss of DExD/H box RNA helicase LGP2 manifests disparate antiviral responses. J Immunol 2007, 178:6444-6455.
    • (2007) J Immunol , vol.178 , pp. 6444-6455
    • Venkataraman, T.1    Valdes, M.2    Elsby, R.3    Kakuta, S.4    Caceres, G.5    Saijo, S.6
  • 71
    • 79954989343 scopus 로고    scopus 로고
    • Impaired cellular responses to cytosolic DNA or infection with Listeria monocytogenes and vaccinia virus in the absence of the murine LGP2 protein
    • Pollpeter D., Komuro A., Barber G.N., Horvath C.M. Impaired cellular responses to cytosolic DNA or infection with Listeria monocytogenes and vaccinia virus in the absence of the murine LGP2 protein. PLoS ONE 2011, 6:e18842.
    • (2011) PLoS ONE , vol.6 , pp. e18842
    • Pollpeter, D.1    Komuro, A.2    Barber, G.N.3    Horvath, C.M.4
  • 73
    • 84856850841 scopus 로고    scopus 로고
    • Chicken cells sense influenza A virus infection through MDA5 and CARDIF signaling involving LGP2
    • Liniger M., Summerfield A., Zimmer G., McCullough K.C., Ruggli N. Chicken cells sense influenza A virus infection through MDA5 and CARDIF signaling involving LGP2. J Virol 2012, 86:705-717.
    • (2012) J Virol , vol.86 , pp. 705-717
    • Liniger, M.1    Summerfield, A.2    Zimmer, G.3    McCullough, K.C.4    Ruggli, N.5
  • 74
    • 84869017282 scopus 로고    scopus 로고
    • LGP2 downregulates interferon production during infection with seasonal human influenza A viruses that activate interferon regulatory factor 3
    • Malur M., Gale M., Krug R.M. LGP2 downregulates interferon production during infection with seasonal human influenza A viruses that activate interferon regulatory factor 3. J Virol 2012, 86:10733-10738.
    • (2012) J Virol , vol.86 , pp. 10733-10738
    • Malur, M.1    Gale, M.2    Krug, R.M.3
  • 77
    • 84877326407 scopus 로고    scopus 로고
    • LGP2 plays a critical role in sensitizing mda-5 to activation by double-stranded RNA
    • Childs K.S., Randall R.E., Goodbourn S. LGP2 plays a critical role in sensitizing mda-5 to activation by double-stranded RNA. PLoS ONE 2013, 8:e64202.
    • (2013) PLoS ONE , vol.8 , pp. e64202
    • Childs, K.S.1    Randall, R.E.2    Goodbourn, S.3
  • 78
    • 67650439286 scopus 로고    scopus 로고
    • A shared interface mediates paramyxovirus interference with antiviral RNA helicases MDA5 and LGP2
    • Parisien J.P., Bamming D., Komuro A., Ramachandran A., Rodriguez J.J., Barber G., et al. A shared interface mediates paramyxovirus interference with antiviral RNA helicases MDA5 and LGP2. J Virol 2009, 83:7252-7260.
    • (2009) J Virol , vol.83 , pp. 7252-7260
    • Parisien, J.P.1    Bamming, D.2    Komuro, A.3    Ramachandran, A.4    Rodriguez, J.J.5    Barber, G.6
  • 79
    • 84903906555 scopus 로고    scopus 로고
    • Paramyxovirus V protein interaction with the antiviral sensor LGP2 disrupts MDA5 signaling enhancement but is not relevant to LGP2-mediated RLR signaling inhibition
    • Rodriguez K.R., Horvath C.M. Paramyxovirus V protein interaction with the antiviral sensor LGP2 disrupts MDA5 signaling enhancement but is not relevant to LGP2-mediated RLR signaling inhibition. J Virol 2014.
    • (2014) J Virol
    • Rodriguez, K.R.1    Horvath, C.M.2
  • 80
    • 77649221014 scopus 로고    scopus 로고
    • Melanoma differentiation-associated gene 5 (MDA5) is involved in the innate immune response to Paramyxoviridae infection in vivo
    • Gitlin L., Benoit L., Song C., Cella M., Gilfillan S., Holtzman M.J., et al. Melanoma differentiation-associated gene 5 (MDA5) is involved in the innate immune response to Paramyxoviridae infection in vivo. PLoS Pathog 2010, 6:e1000734.
    • (2010) PLoS Pathog , vol.6 , pp. e1000734
    • Gitlin, L.1    Benoit, L.2    Song, C.3    Cella, M.4    Gilfillan, S.5    Holtzman, M.J.6
  • 81
    • 84857393830 scopus 로고    scopus 로고
    • Activation of RIG-I-like receptor signal transduction
    • Bruns A.M., Horvath C.M. Activation of RIG-I-like receptor signal transduction. Crit Rev Biochem Mol Biol 2012, 47:194-206.
    • (2012) Crit Rev Biochem Mol Biol , vol.47 , pp. 194-206
    • Bruns, A.M.1    Horvath, C.M.2
  • 82
    • 84926104091 scopus 로고    scopus 로고
    • The innate immune sensor LGP2 activates antiviral signal transduction by regulating MDA5-RNA interactions and filament assembly
    • Bruns A.M., Leser G.P., Lamb R.A., Horvath C.M. The innate immune sensor LGP2 activates antiviral signal transduction by regulating MDA5-RNA interactions and filament assembly. Mol Cell 2014.
    • (2014) Mol Cell
    • Bruns, A.M.1    Leser, G.P.2    Lamb, R.A.3    Horvath, C.M.4


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