메뉴 건너뛰기




Volumn 9, Issue 9, 2014, Pages

RIG-I self-oligomerization is either dispensable or very transient for signal transduction

Author keywords

[No Author keywords available]

Indexed keywords

DOUBLE STRANDED RNA; INTERFERON; POLYINOSINIC POLYCYTIDYLIC ACID; RETINOIC ACID INDUCIBLE PROTEIN I; RNA; VIRUS RNA; BETA INTERFERON; DDX58 PROTEIN, HUMAN; DEAD BOX PROTEIN;

EID: 84907437841     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0108770     Document Type: Article
Times cited : (10)

References (65)
  • 2
    • 58049217490 scopus 로고    scopus 로고
    • RNA recognition and signal transduction by RIG-I-like receptors
    • Yoneyama M, Fujita T (2009) RNA recognition and signal transduction by RIG-I-like receptors. Immunological Reviews 227: 54-65.
    • (2009) Immunological Reviews , vol.227 , pp. 54-65
    • Yoneyama, M.1    Fujita, T.2
  • 4
    • 77249132637 scopus 로고    scopus 로고
    • Recognition of viruses by cytoplasmic sensors
    • Wilkins C, Gale M Jr (2010) Recognition of viruses by cytoplasmic sensors. Current opinion in Immunology 22: 41-47.
    • (2010) Current Opinion in Immunology , vol.22 , pp. 41-47
    • Wilkins, C.1    Gale, M.2
  • 5
    • 34548126512 scopus 로고    scopus 로고
    • RIG-I family RNA helicases: Cytoplasmic sensor for antiviral innate immunity
    • Yoneyama M, Fujita T (2007) RIG-I family RNA helicases: cytoplasmic sensor for antiviral innate immunity. Cytokine Growth Factor Reviews 18: 545-551.
    • (2007) Cytokine Growth Factor Reviews , vol.18 , pp. 545-551
    • Yoneyama, M.1    Fujita, T.2
  • 6
    • 75749089555 scopus 로고    scopus 로고
    • Recognition of viral nucleic acids in innate immunity
    • Yoneyama M, Fujita T (2010) Recognition of viral nucleic acids in innate immunity. Reviews in medical virology 20: 4-22.
    • (2010) Reviews in Medical Virology , vol.20 , pp. 4-22
    • Yoneyama, M.1    Fujita, T.2
  • 7
    • 79960990301 scopus 로고    scopus 로고
    • Molecular mechanism of signal perception and integration by the innate immune sensor retinoic acid-inducible gene-I (RIG-I)
    • Binder M, Eberle F, Seitz S, Mucke N, Huber CM, et al. (2011) Molecular mechanism of signal perception and integration by the innate immune sensor retinoic acid-inducible gene-I (RIG-I). The Journal of biological chemistry 286: 27278-27287.
    • (2011) The Journal of Biological Chemistry , vol.286 , pp. 27278-27287
    • Binder, M.1    Eberle, F.2    Seitz, S.3    Mucke, N.4    Huber, C.M.5
  • 8
    • 84883488816 scopus 로고    scopus 로고
    • Defining the functional determinants for RNA surveillance by RIG-I
    • Kohlway A, Luo D, Rawling DC, Ding SC, Pyle AM (2013) Defining the functional determinants for RNA surveillance by RIG-I. EMBO reports 14: 772-779.
    • (2013) EMBO Reports , vol.14 , pp. 772-779
    • Kohlway, A.1    Luo, D.2    Rawling, D.C.3    Ding, S.C.4    Pyle, A.M.5
  • 9
    • 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, et al. (2009) Recognition of 5′ triphosphate by RIG-I helicase requires short blunt double-stranded RNA as contained in panhandle of negative-strand virus. Immunity 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
  • 11
    • 84876698263 scopus 로고    scopus 로고
    • Intracellular pathogen detection by RIG-I-like receptors
    • Dixit E, Kagan JC (2013) Intracellular pathogen detection by RIG-I-like receptors. Advances in immunology 117: 99-125.
    • (2013) Advances in Immunology , vol.117 , pp. 99-125
    • Dixit, E.1    Kagan, J.C.2
  • 12
    • 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, et al. (2007) TRIM25 RING-finger E3 ubiquitin ligase is essential for RIG-I-mediated antiviral activity. Nature 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
  • 13
    • 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, et al. (2010) Reconstitution of the RIG-I pathway reveals a signaling role of unanchored polyubiquitin chains in innate immunity. Cell 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
  • 14
    • 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, et al. (2008) The C-terminal regulatory domain is the RNA 5′-triphosphate sensor of RIG-I. Molecular Cell 29: 169-179.
    • (2008) Molecular Cell , vol.29 , pp. 169-179
    • Cui, S.1    Eisenacher, K.2    Kirchhofer, A.3    Brzozka, K.4    Lammens, A.5
  • 15
    • 84862994793 scopus 로고    scopus 로고
    • Ubiquitin-induced oligomerization of the RNA sensors RIG-I and MDA5 activates antiviral innate immune response
    • Jiang X, Kinch LN, Brautigam CA, Chen X, Du F, et al. (2012) Ubiquitin-induced oligomerization of the RNA sensors RIG-I and MDA5 activates antiviral innate immune response. Immunity 36: 959-973.
    • (2012) Immunity , vol.36 , pp. 959-973
    • Jiang, X.1    Kinch, L.N.2    Brautigam, C.A.3    Chen, X.4    Du, F.5
  • 16
  • 17
    • 77955481642 scopus 로고    scopus 로고
    • The structural basis of 5′ triphosphate double-stranded RNA recognition by RIG-I C-terminal domain
    • Lu C, Xu H, Ranjith-Kumar CT, Brooks MT, Hou TY, et al. (2010) The structural basis of 5′ triphosphate double-stranded RNA recognition by RIG-I C-terminal domain. Structure 18: 1032-1043.
    • (2010) Structure , vol.18 , pp. 1032-1043
    • Lu, C.1    Xu, H.2    Ranjith-Kumar, C.T.3    Brooks, M.T.4    Hou, T.Y.5
  • 21
    • 77954386541 scopus 로고    scopus 로고
    • Structural and functional insights into 5′-ppp RNA pattern recognition by the innate immune receptor RIG-I
    • Wang Y, Ludwig J, Schuberth C, Goldeck M, Schlee M, et al. (2010) Structural and functional insights into 5′-ppp RNA pattern recognition by the innate immune receptor RIG-I. Nature structural & molecular biology 17: 781-787.
    • (2010) Nature Structural & Molecular Biology , vol.17 , pp. 781-787
    • Wang, Y.1    Ludwig, J.2    Schuberth, C.3    Goldeck, M.4    Schlee, M.5
  • 22
    • 0036893332 scopus 로고    scopus 로고
    • Highly permissive cell lines for subgenomic and genomic hepatitis C virus RNA replication
    • Blight KJ, McKeating JA, Rice CM (2002) Highly permissive cell lines for subgenomic and genomic hepatitis C virus RNA replication. Journal of virology 76: 13001-13014.
    • (2002) Journal of Virology , vol.76 , pp. 13001-13014
    • Blight, K.J.1    McKeating, J.A.2    Rice, C.M.3
  • 23
    • 0000841684 scopus 로고
    • The research for the SV40 by means of tissue culture technique
    • Yasumura Y, Kawakita M (1963) The research for the SV40 by means of tissue culture technique. Nippon Rinsho 21: 1201-1219.
    • (1963) Nippon Rinsho , vol.21 , pp. 1201-1219
    • Yasumura, Y.1    Kawakita, M.2
  • 24
    • 0017710978 scopus 로고
    • Characteristics of a human cell line transformed by DNA from human adenovirus type 5
    • Graham FL, Smiley J, Russell WC, Nairn R (1977) Characteristics of a human cell line transformed by DNA from human adenovirus type 5. The Journal of general virology 36: 59-74.
    • (1977) The Journal of General Virology , vol.36 , pp. 59-74
    • Graham, F.L.1    Smiley, J.2    Russell, W.C.3    Nairn, R.4
  • 26
    • 0026331267 scopus 로고
    • X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil
    • O'Shea EK, Klemm JD, Kim PS, Alber T (1991) X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil. Science 254: 539-544.
    • (1991) Science , vol.254 , pp. 539-544
    • O'Shea, E.K.1    Klemm, J.D.2    Kim, P.S.3    Alber, T.4
  • 27
    • 0023896289 scopus 로고
    • Antigenic analysis of African measles virus field isolates: Identification and localisation of one conserved and two variable epitope sites on the NP protein
    • Giraudon P, Jacquier MF, Wild TF (1988) Antigenic analysis of African measles virus field isolates: identification and localisation of one conserved and two variable epitope sites on the NP protein. Virus Research 10: 137-152.
    • (1988) Virus Research , vol.10 , pp. 137-152
    • Giraudon, P.1    Jacquier, M.F.2    Wild, T.F.3
  • 28
    • 24644433742 scopus 로고    scopus 로고
    • Inhibition of ubiquitination and stabilization of human ubiquitin E3 ligase PIRH2 by measles virus phosphoprotein
    • Chen M, Cortay JC, Logan IR, Sapountzi V, Robson CN, et al. (2005) Inhibition of ubiquitination and stabilization of human ubiquitin E3 ligase PIRH2 by measles virus phosphoprotein. Journal of virology 79: 11824-11836.
    • (2005) Journal of Virology , vol.79 , pp. 11824-11836
    • Chen, M.1    Cortay, J.C.2    Logan, I.R.3    Sapountzi, V.4    Robson, C.N.5
  • 30
    • 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 AA, Louber J, Brunel J, et al. (2011) Structural basis for the activation of innate immune pattern-recognition receptor RIG-I by viral RNA. Cell 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
  • 31
    • 79953166075 scopus 로고    scopus 로고
    • Short double-stranded RNAs with an overhanging 5′ ppp-nucleotide, as found in arenavirus genomes, act as RIG-I decoys
    • Marq JB, Hausmann S, Veillard N, Kolakofsky D, Garcin D (2011) Short double-stranded RNAs with an overhanging 5′ ppp-nucleotide, as found in arenavirus genomes, act as RIG-I decoys. The Journal of biological chemistry 286: 6108-6116.
    • (2011) The Journal of Biological Chemistry , vol.286 , pp. 6108-6116
    • Marq, J.B.1    Hausmann, S.2    Veillard, N.3    Kolakofsky, D.4    Garcin, D.5
  • 32
    • 0006876621 scopus 로고
    • The dependence of the scattering of light on angle and concentration in linear polymer solutions
    • Zimm BH (1948) The dependence of the scattering of light on angle and concentration in linear polymer solutions. The Journal of physical and colloid chemistry 52: 260-267.
    • (1948) The Journal of Physical and Colloid Chemistry , vol.52 , pp. 260-267
    • Zimm, B.H.1
  • 33
    • 82355163586 scopus 로고    scopus 로고
    • Benchmarking a luciferase complementation assay for detecting protein complexes
    • Cassonnet P, Rolloy C, Neveu G, Vidalain PO, Chantier T, et al. (2011) Benchmarking a luciferase complementation assay for detecting protein complexes. Nature methods 8: 990-992.
    • (2011) Nature Methods , vol.8 , pp. 990-992
    • Cassonnet, P.1    Rolloy, C.2    Neveu, G.3    Vidalain, P.O.4    Chantier, T.5
  • 37
    • 20444442721 scopus 로고    scopus 로고
    • Distinct poly(I-C) and virus-activated signaling pathways leading to interferon-beta production in hepatocytes
    • Li K, Chen Z, Kato N, Gale M Jr, Lemon SM (2005) Distinct poly(I-C) and virus-activated signaling pathways leading to interferon-beta production in hepatocytes. The Journal of biological chemistry 280: 16739-16747.
    • (2005) The Journal of Biological Chemistry , vol.280 , pp. 16739-16747
    • Li, K.1    Chen, Z.2    Kato, N.3    Gale, M.4    Lemon, S.M.5
  • 38
    • 13944253573 scopus 로고    scopus 로고
    • Regulating intracellular antiviral defense and permissiveness to hepatitis C virus RNA replication through a cellular RNA helicase, RIG-I
    • Sumpter R Jr, Loo YM, Foy E, Li K, Yoneyama M, et al. (2005) Regulating intracellular antiviral defense and permissiveness to hepatitis C virus RNA replication through a cellular RNA helicase, RIG-I. Journal of virology 79: 2689-2699.
    • (2005) Journal of Virology , vol.79 , pp. 2689-2699
    • Sumpter, R.1    Loo, Y.M.2    Foy, E.3    Li, K.4    Yoneyama, M.5
  • 39
    • 77953308262 scopus 로고    scopus 로고
    • Unpaired 5′ ppp-nucleotides, as found in arenavirus double-stranded RNA panhandles, are not recognized by RIG-I
    • Marq JB, Kolakofsky D, Garcin D (2010) Unpaired 5′ ppp-nucleotides, as found in arenavirus double-stranded RNA panhandles, are not recognized by RIG-I. The Journal of biological chemistry 285: 18208-18216.
    • (2010) The Journal of Biological Chemistry , vol.285 , pp. 18208-18216
    • Marq, J.B.1    Kolakofsky, D.2    Garcin, D.3
  • 40
    • 84901376043 scopus 로고    scopus 로고
    • In Vivo Ligands of MDA5 and RIG-I in Measles Virus-Infected Cells
    • Runge S, Sparrer KM, Lassig C, Hembach K, Baum A, et al. (2014) In Vivo Ligands of MDA5 and RIG-I in Measles Virus-Infected Cells. PLoS Pathogens 10: e1004081.
    • (2014) PLoS Pathogens , vol.10 , pp. e1004081
    • Runge, S.1    Sparrer, K.M.2    Lassig, C.3    Hembach, K.4    Baum, A.5
  • 41
    • 65649083024 scopus 로고    scopus 로고
    • Regulation of signal transduction by enzymatically inactive antiviral RNA helicase proteins MDA5, RIG-I, and LGP2
    • Bamming D, Horvath CM (2009) Regulation of signal transduction by enzymatically inactive antiviral RNA helicase proteins MDA5, RIG-I, and LGP2. The Journal of biological chemistry 284: 9700-9712.
    • (2009) The Journal of Biological Chemistry , vol.284 , pp. 9700-9712
    • Bamming, D.1    Horvath, C.M.2
  • 42
    • 34547157869 scopus 로고    scopus 로고
    • Cytosolic 5′-triphosphate ended viral leader transcript of measles virus as activator of the RIG I-mediated interferon response
    • Plumet S, Herschke F, Bourhis JM, Valentin H, Longhi S, et al. (2007) Cytosolic 5′-triphosphate ended viral leader transcript of measles virus as activator of the RIG I-mediated interferon response. PLoS One 2: e279.
    • (2007) PLoS One , vol.2 , pp. e279
    • Plumet, S.1    Herschke, F.2    Bourhis, J.M.3    Valentin, H.4    Longhi, S.5
  • 43
    • 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, et al. (2009) Solution structures of cytosolic RNA sensor MDA5 and LGP2 C-terminal domains: identification of the RNA recognition loop in RIG-I-like receptors. The Journal of biological chemistry 284: 17465-17474.
    • (2009) The Journal of Biological Chemistry , vol.284 , pp. 17465-17474
    • Takahasi, K.1    Kumeta, H.2    Tsuduki, N.3    Narita, R.4    Shigemoto, T.5
  • 44
    • 84866614430 scopus 로고    scopus 로고
    • Interaction between the C-terminal domains of measles virus nucleoprotein and phosphoprotein: A tight complex implying one binding site
    • Blocquel D, Habchi J, Costanzo S, Doizy A, Oglesbee M, et al. (2012) Interaction between the C-terminal domains of measles virus nucleoprotein and phosphoprotein: a tight complex implying one binding site. Protein science: a - publication of the Protein Society 21: 1577-1585.
    • (2012) Protein Science: A - Publication of the Protein Society , vol.21 , pp. 1577-1585
    • Blocquel, D.1    Habchi, J.2    Costanzo, S.3    Doizy, A.4    Oglesbee, M.5
  • 45
    • 84906351352 scopus 로고    scopus 로고
    • Sequence of events in measles virus replication: Role of phosphoprotein-nucleocapsid interactions
    • Brunel J, Chopy D, Dosnon M, Bloyet LM, Devaux P, et al. (2014) Sequence of events in measles virus replication: role of phosphoprotein-nucleocapsid interactions. Journal of virology 88: 10851-10863.
    • (2014) Journal of Virology , vol.88 , pp. 10851-10863
    • Brunel, J.1    Chopy, D.2    Dosnon, M.3    Bloyet, L.M.4    Devaux, P.5
  • 46
    • 77955378293 scopus 로고    scopus 로고
    • Solution structure of the C-terminal X domain of the measles virus phosphoprotein and interaction with the intrinsically disordered C-terminal domain of the nucleoprotein
    • Gely S, Lowry DF, Bernard C, Jensen MR, Blackledge M, et al. (2010) Solution structure of the C-terminal X domain of the measles virus phosphoprotein and interaction with the intrinsically disordered C-terminal domain of the nucleoprotein. Journal of molecular recognition: JMR 23: 435-447.
    • (2010) Journal of Molecular Recognition: JMR , vol.23 , pp. 435-447
    • Gely, S.1    Lowry, D.F.2    Bernard, C.3    Jensen, M.R.4    Blackledge, M.5
  • 48
    • 84859498913 scopus 로고    scopus 로고
    • Plasticity in structural and functional interactions between the phosphoprotein and nucleoprotein of measles virus
    • Shu Y, Habchi J, Costanzo S, Padilla A, Brunel J, et al. (2012) Plasticity in structural and functional interactions between the phosphoprotein and nucleoprotein of measles virus. The Journal of biological chemistry 287: 11951-11967.
    • (2012) The Journal of Biological Chemistry , vol.287 , pp. 11951-11967
    • Shu, Y.1    Habchi, J.2    Costanzo, S.3    Padilla, A.4    Brunel, J.5
  • 49
    • 84875167118 scopus 로고    scopus 로고
    • Incoming RNA virus nucleocapsids containing a 5′-triphosphorylated genome activate RIG-I and antiviral signaling
    • Weber M, Gawanbacht A, Habjan M, Rang A, Borner C, et al. (2013) Incoming RNA virus nucleocapsids containing a 5′-triphosphorylated genome activate RIG-I and antiviral signaling. Cell host & microbe 13: 336-346.
    • (2013) Cell Host & Microbe , vol.13 , pp. 336-346
    • Weber, M.1    Gawanbacht, A.2    Habjan, M.3    Rang, A.4    Borner, C.5
  • 50
    • 80052705992 scopus 로고    scopus 로고
    • Interplay between innate immunity and negative-strand RNA viruses: Towards a rational model. Microbiology and molecular biology reviews
    • Gerlier D, Lyles DS (2011) Interplay between innate immunity and negative-strand RNA viruses: towards a rational model. Microbiology and molecular biology reviews: MMBR 75: 468-490.
    • (2011) MMBR , vol.75 , pp. 468-490
    • Gerlier, D.1    Lyles, D.S.2
  • 51
    • 33751208345 scopus 로고    scopus 로고
    • A highly sensitive protein-protein interaction assay based on Gaussia luciferase
    • Remy I, Michnick SW (2006) A highly sensitive protein-protein interaction assay based on Gaussia luciferase. Nature methods 3: 977-979.
    • (2006) Nature Methods , vol.3 , pp. 977-979
    • Remy, I.1    Michnick, S.W.2
  • 52
    • 84876396981 scopus 로고    scopus 로고
    • Conformational rearrangements of RIG-I receptor on formation of a multiprotein: DsRNA assembly
    • Beckham SA, Brouwer J, Roth A, Wang D, Sadler AJ, et al. (2013) Conformational rearrangements of RIG-I receptor on formation of a multiprotein: dsRNA assembly. Nucleic acids research 41: 3436-3445.
    • (2013) Nucleic Acids Research , vol.41 , pp. 3436-3445
    • Beckham, S.A.1    Brouwer, J.2    Roth, A.3    Wang, D.4    Sadler, A.J.5
  • 53
    • 81555204380 scopus 로고    scopus 로고
    • Structural basis of RNA recognition and activation by innate immune receptor RIG-I
    • Jiang F, Ramanathan A, Miller MT, Tang GQ, Gale M, et al. (2011) Structural basis of RNA recognition and activation by innate immune receptor RIG-I. Nature 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
  • 54
    • 84883487585 scopus 로고    scopus 로고
    • ATPase-driven oligomerization of RIG-I on RNA allows optimal activation of type-I interferon
    • Patel JR, Jain A, Chou YY, Baum A, Ha T, et al. (2013) ATPase-driven oligomerization of RIG-I on RNA allows optimal activation of type-I interferon. EMBO reports 14: 780-787.
    • (2013) EMBO Reports , vol.14 , pp. 780-787
    • Patel, J.R.1    Jain, A.2    Chou, Y.Y.3    Baum, A.4    Ha, T.5
  • 55
    • 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 (2013) RIG-I forms signaling-competent filaments in an ATP-dependent, ubiquitin-independent manner. Molecular cell 51: 573-583.
    • (2013) Molecular Cell , vol.51 , pp. 573-583
    • Peisley, A.1    Wu, B.2    Yao, H.3    Walz, T.4    Hur, S.5
  • 56
    • 80054685883 scopus 로고    scopus 로고
    • Structural Insights into RNA Recognition by RIG-I
    • Luo D, Ding SC, Vela A, Kohlway A, Lindenbach BD, et al. (2011) Structural Insights into RNA Recognition by RIG-I. Cell 147: 409-422.
    • (2011) Cell , vol.147 , pp. 409-422
    • Luo, D.1    Ding, S.C.2    Vela, A.3    Kohlway, A.4    Lindenbach, B.D.5
  • 58
    • 84869765600 scopus 로고    scopus 로고
    • The thermodynamic basis for viral RNA detection by the RIG-I innate immune sensor
    • Vela A, Fedorova O, Ding SC, Pyle AM (2012) The thermodynamic basis for viral RNA detection by the RIG-I innate immune sensor. The Journal of biological chemistry 287: 42564-42573.
    • (2012) The Journal of Biological Chemistry , vol.287 , pp. 42564-42573
    • Vela, A.1    Fedorova, O.2    Ding, S.C.3    Pyle, A.M.4
  • 59
    • 84899957213 scopus 로고    scopus 로고
    • Structural basis for ubiquitin-mediated antiviral signal activation by RIG-I
    • Peisley A, Wu B, Xu H, Chen ZJ, Hur S (2014) Structural basis for ubiquitin-mediated antiviral signal activation by RIG-I. Nature 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
  • 60
    • 84869845792 scopus 로고    scopus 로고
    • A structure-based model of RIG-I activation
    • Kolakofsky D, Kowalinski E, Cusack S (2012) A structure-based model of RIG-I activation. RNA 18: 2118-2127.
    • (2012) RNA , vol.18 , pp. 2118-2127
    • Kolakofsky, D.1    Kowalinski, E.2    Cusack, S.3
  • 61
    • 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.
    • (2011) Cell , vol.146 , pp. 448-461
    • Hou, F.1    Sun, L.2    Zheng, H.3    Skaug, B.4    Jiang, Q.X.5
  • 65
    • 84906342978 scopus 로고    scopus 로고
    • Molecular Imprinting as a Signal-Activation Mechanism of the Viral RNA Sensor RIG-I
    • Wu B, Peisley A, Tetrault D, Li Z, Egelman EH, et al. (2014) Molecular Imprinting as a Signal-Activation Mechanism of the Viral RNA Sensor RIG-I. Molecular cell 55: 511-523.
    • (2014) Molecular Cell , vol.55 , pp. 511-523
    • Wu, B.1    Peisley, A.2    Tetrault, D.3    Li, Z.4    Egelman, E.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.