메뉴 건너뛰기




Volumn 19, Issue 3, 2013, Pages 333-344

Recognition of viral RNA stem-loops by the tandem double-stranded RNA binding domains of PKR

Author keywords

HIV 1 TAR; PKR; Protein RNA interactions; Small angle X ray scattering; VAI

Indexed keywords

DOUBLE STRANDED RNA; PROTEIN KINASE; VIRUS RNA;

EID: 84874337377     PISSN: 13558382     EISSN: 14699001     Source Type: Journal    
DOI: 10.1261/rna.035931.112     Document Type: Article
Times cited : (29)

References (59)
  • 1
    • 0029852357 scopus 로고    scopus 로고
    • Structure of HIV-1 TAR RNA in the absence of ligands reveals a novel conformation of the trinucleotide bulge
    • DOI 10.1093/nar/24.20.3974
    • Aboul-ela F, Karn J, Varani G. 1996. Structure of HIV-1 TAR RNA in the absence of ligands reveals a novel conformation of the trinucleotide bulge. Nucleic Acids Res 24: 3974-3981. (Pubitemid 26385329)
    • (1996) Nucleic Acids Research , vol.24 , Issue.20 , pp. 3974-3981
    • Aboul-ela, F.1    Karn, J.2    Varani, G.3
  • 2
    • 0036290269 scopus 로고    scopus 로고
    • Concerted motions in HIV-1 TAR RNA may allow access to bound state conformations: RNA dynamics from NMR residual dipolar couplings
    • DOI 10.1006/jmbi.2001.5235
    • Al-Hashimi HM, Gosser Y, Gorin A, Hu W, Majumdar A, Patel DJ. 2002. Concerted motions in HIV-1 TAR RNA may allow access to bound state conformations: RNA dynamics from NMR residual dipolar couplings. J Mol Biol 315: 95-102. (Pubitemid 34722113)
    • (2002) Journal of Molecular Biology , vol.315 , Issue.2 , pp. 95-102
    • Al-Hashimi, H.M.1    Gosser, Y.2    Gorin, A.3    Hu, W.4    Majumdar, A.5    Patel, D.J.6
  • 4
    • 0031014063 scopus 로고    scopus 로고
    • Oncogenic potential of TAR RNA binding protein TRBP and its regulatory interaction with RNA-dependent protein kinase PKR
    • DOI 10.1093/emboj/16.3.611
    • Benkirane M, Neuveut C, Chun RF, Smith SM, Samuel CE, Gatignol A, Jeang KT. 1997. Oncogenic potential of TAR RNA binding protein TRBP and its regulatory interaction with RNA-dependent protein kinase PKR. EMBO J 16: 611-624. (Pubitemid 27067790)
    • (1997) EMBO Journal , vol.16 , Issue.3 , pp. 611-624
    • Benkirane, M.1    Neuveut, C.2    Chun, R.F.3    Smith, S.M.4    Samuel, C.E.5    Gatignol, A.6    Jeang, K.-T.7
  • 5
    • 0024322804 scopus 로고
    • Tat trans-activates the human immunodeficiency virus through a nascent RNA target
    • DOI 10.1016/0092-8674(89)90289-4
    • Berkhout B, Silverman RH, Jeang KT. 1989. Tat trans-activates the human immunodeficiency virus through a nascent RNA target. Cell 59: 273-282. (Pubitemid 19264373)
    • (1989) Cell , vol.59 , Issue.2 , pp. 273-282
    • Berkhout, B.1    Silverman, R.H.2    Jeang, K.-T.3
  • 6
    • 0029782652 scopus 로고    scopus 로고
    • Minor-groove recognition of double-stranded RNA by the double-stranded RNA-binding domain from the RNA-activated protein kinase PKR
    • DOI 10.1021/bi9607259
    • Bevilacqua PC, Cech TR. 1996. Minor-groove recognition of doublestranded RNA by the double-stranded RNA-binding domain from the RNA-activated protein kinase PKR. Biochemistry 35: 9983-9994. (Pubitemid 26269913)
    • (1996) Biochemistry , vol.35 , Issue.31 , pp. 9983-9994
    • Bevilacqua, P.C.1    Cech, T.R.2
  • 7
    • 84861367008 scopus 로고    scopus 로고
    • The RNA helicase RHAU (DHX36) unwinds a G4-quadruplex in human telomerase RNA and promotes the formation of the P1 helix template boundary
    • Booy EP, Meier M, Okun N, Novakowski SK, Xiong S, Stetefeld J, McKenna SA. 2012. The RNA helicase RHAU (DHX36) unwinds a G4-quadruplex in human telomerase RNA and promotes the formation of the P1 helix template boundary. Nucleic Acids Res 40: 4110-4124.
    • (2012) Nucleic Acids Res , vol.40 , pp. 4110-4124
    • Booy, E.P.1    Meier, M.2    Okun, N.3    Novakowski, S.K.4    Xiong, S.5    Stetefeld, J.6    McKenna, S.A.7
  • 8
    • 0029041105 scopus 로고
    • NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5
    • Bycroft M, Grunert S, Murzin AG, Proctor M, St Johnston D. 1995. NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5. EMBO J 14: 3563-3571.
    • (1995) EMBO J , vol.14 , pp. 3563-3571
    • Bycroft, M.1    Grunert, S.2    Murzin, A.G.3    Proctor, M.4    St Johnston, D.5
  • 9
    • 0030989529 scopus 로고    scopus 로고
    • Characterization of the solution complex between the interferon-induced, double-stranded RNA-activated protein kinase and HIV-I trans-activating region RNA
    • DOI 10.1074/jbc.272.14.9510
    • Carpick BW, Graziano V, Schneider D, Maitra RK, Lee X, Williams BR. 1997. Characterization of the solution complex between the interferon-induced, double-stranded RNA-activated protein kinase and HIV-I trans-activating region RNA. J Biol Chem 272: 9510-9516. (Pubitemid 27154968)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.14 , pp. 9510-9516
    • Carpick, B.W.1    Graziano, V.2    Schneider, D.3    Maitra, R.K.4    Lee, X.5    Williams, B.R.G.6
  • 10
    • 25144502820 scopus 로고    scopus 로고
    • Higher-order substrate recognition of eIF2α by the RNA-dependent protein kinase PKR
    • DOI 10.1016/j.cell.2005.06.044, PII S0092867405007051
    • Dar AC, Dever TE, Sicheri F. 2005. Higher-order substrate recognition of eIF2α by the RNA-dependent protein kinase PKR. Cell 122: 887-900. (Pubitemid 41345206)
    • (2005) Cell , vol.122 , Issue.6 , pp. 887-900
    • Dar, A.C.1    Dever, T.E.2    Sicheri, F.3
  • 11
    • 0001229341 scopus 로고    scopus 로고
    • Calculation of hydrodynamic properties of globular proteins from their atomic-level structure
    • de la Torre JG, Huertas ML, Carrasco B. 2000. Calculation of hydrodynamic properties of globular proteins from their atomic-level structure. Biophys J 78: 719-730. (Pubitemid 30211830)
    • (2000) Biophysical Journal , vol.78 , Issue.2 , pp. 719-730
    • Garcia De La Torre, J.1    Huertas, M.L.2    Carrasco, B.3
  • 13
    • 62649139615 scopus 로고    scopus 로고
    • DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering
    • Franke D, Svergun DI. 2009. DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering. J Appl Crystallogr 42: 342-346.
    • (2009) J Appl Crystallogr , vol.42 , pp. 342-346
    • Franke, D.1    Svergun, D.I.2
  • 14
    • 77956013448 scopus 로고    scopus 로고
    • HIV-1 TAR RNA spontaneously undergoes relevant apo-to-holo conformational transitions in molecular dynamics and constrained geometrical simulations
    • Fulle S, Christ NA, Kestner E, Gohlke H. 2010. HIV-1 TAR RNA spontaneously undergoes relevant apo-to-holo conformational transitions in molecular dynamics and constrained geometrical simulations. J Chem Inf Model 50: 1489-1501.
    • (2010) J Chem Inf Model , vol.50 , pp. 1489-1501
    • Fulle, S.1    Christ, N.A.2    Kestner, E.3    Gohlke, H.4
  • 16
    • 0345164384 scopus 로고    scopus 로고
    • Molecular mechanisms of interferon resistance mediated by viral-directed inhibition of PKR, the interferon-induced protein kinase
    • DOI 10.1016/S0163-7258(97)00165-4, PII S0163725897001654
    • Gale M Jr, Katze MG. 1998. Molecular mechanisms of interferon resistance mediated by viral-directed inhibition of PKR, the interferoninduced protein kinase. Pharmacol Ther 78: 29-46. (Pubitemid 28178928)
    • (1998) Pharmacology and Therapeutics , vol.78 , Issue.1 , pp. 29-46
    • Gale Jr., M.1    Katze, M.G.2
  • 17
    • 31044448524 scopus 로고    scopus 로고
    • Structural insight into the mechanism of double-stranded RNA processing by ribonuclease III
    • DOI 10.1016/j.cell.2005.11.034, PII S0092867405013292
    • Gan J, Tropea JE, Austin BP, Court DL, Waugh DS, Ji X. 2006. Structural insight into the mechanism of double-stranded RNA processing by ribonuclease III. Cell 124: 355-366. (Pubitemid 43121983)
    • (2006) Cell , vol.124 , Issue.2 , pp. 355-366
    • Gan, J.1    Tropea, J.E.2    Austin, B.P.3    Court, D.L.4    Waugh, D.S.5    Ji, X.6
  • 18
    • 0026490072 scopus 로고
    • Tat-responsive region RNA of human immunodeficiency virus type 1 stimulates protein synthesis in vivo and in vitro: Relationship between structure and function
    • Gunnery S, Green SR, Mathews MB. 1992. Tat-responsive region RNA of human immunodeficiency virus type 1 stimulates protein synthesis in vivo and in vitro: Relationship between structure and function. Proc Natl Acad Sci 89: 11557-11561.
    • (1992) Proc Natl Acad Sci , vol.89 , pp. 11557-11561
    • Gunnery, S.1    Green, S.R.2    Mathews, M.B.3
  • 20
    • 34548137353 scopus 로고    scopus 로고
    • On the discovery of interferon-inducible, double-stranded RNA activated enzymes: The 2'-5'oligoadenylate synthetases and the protein kinase PKR
    • DOI 10.1016/j.cytogfr.2007.06.003, PII S1359610107000718
    • Hovanessian AG. 2007. On the discovery of interferon-inducible, double-stranded RNA activated enzymes: The 2'-5'oligoadenylate synthetases and the protein kinase PKR. Cytokine Growth Factor Rev 18: 351-361. (Pubitemid 47302823)
    • (2007) Cytokine and Growth Factor Reviews , vol.18 , Issue.5-6 , pp. 351-361
    • Hovanessian, A.G.1
  • 21
    • 0027444622 scopus 로고
    • An NMR study of the HIV-1 TAR element hairpin
    • DOI 10.1021/bi00097a032
    • Jaeger JA, Tinoco I Jr. 1993. An NMR study of the HIV-1 TAR element hairpin. Biochemistry 32: 12522-12530. (Pubitemid 23357975)
    • (1993) Biochemistry , vol.32 , Issue.46 , pp. 12522-12530
    • Jaeger, J.A.1    Tinoco Jr., I.2
  • 22
  • 23
    • 33646096014 scopus 로고    scopus 로고
    • Specific recognition of HIV TAR RNA by the dsRNA binding domains (dsRBD1-dsRBD2) of PKR
    • Kim I, Liu CW, Puglisi JD. 2006. Specific recognition of HIV TAR RNA by the dsRNA binding domains (dsRBD1-dsRBD2) of PKR. J Mol Biol 358: 430-442.
    • (2006) J Mol Biol , vol.358 , pp. 430-442
    • Kim, I.1    Liu, C.W.2    Puglisi, J.D.3
  • 25
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- and low-resolution structural models
    • DOI 10.1107/S0021889800014126
    • Kozin MB, Svergun DI. 2001. Automated matching of high-and lowresolution structural models. J Appl Crystallogr 34: 33-41. (Pubitemid 32151714)
    • (2001) Journal of Applied Crystallography , vol.34 , Issue.1 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2
  • 27
    • 9644266744 scopus 로고    scopus 로고
    • Mechanism of PKR activation: Dimerization and kinase activation in the absence of double-stranded RNA
    • DOI 10.1016/j.jmb.2004.10.031, PII S0022283604013233
    • Lemaire PA, Lary J, Cole JL. 2005. Mechanism of PKR activation: Dimerization and kinase activation in the absence of double-stranded RNA. J Mol Biol 345: 81-90. (Pubitemid 39572826)
    • (2005) Journal of Molecular Biology , vol.345 , Issue.1 , pp. 81-90
    • Lemaire, P.A.1    Lary, J.2    Cole, J.L.3
  • 28
    • 33746650460 scopus 로고    scopus 로고
    • Unactivated PKR exists in an open conformation capable of binding nucleotides
    • DOI 10.1021/bi060567d
    • Lemaire PA, Tessmer I, Craig R, Erie DA, Cole JL. 2006. Unactivated PKR exists in an open conformation capable of binding nucleotides. Biochemistry 45: 9074-9084. (Pubitemid 44156370)
    • (2006) Biochemistry , vol.45 , Issue.30 , pp. 9074-9084
    • Lemaire, P.A.1    Tessmer, I.2    Craig, R.3    Erie, D.A.4    Cole, J.L.5
  • 30
    • 4344658402 scopus 로고    scopus 로고
    • Induction and regulation of IFNs during viral infections
    • DOI 10.1089/1079990041689665
    • Malmgaard L. 2004. Induction and regulation of IFNs during viral infections. J Interferon Cytokine Res 24: 439-454. (Pubitemid 39120592)
    • (2004) Journal of Interferon and Cytokine Research , vol.24 , Issue.8 , pp. 439-454
    • Malmgaard, L.1
  • 31
    • 33646116314 scopus 로고    scopus 로고
    • Uncoupling of RNA binding and PKR kinase activation by viral inhibitor RNAs
    • McKenna SA, Kim I, Liu CW, Puglisi JD. 2006. Uncoupling of RNA binding and PKR kinase activation by viral inhibitor RNAs. J Mol Biol 358: 1270-1285.
    • (2006) J Mol Biol , vol.358 , pp. 1270-1285
    • McKenna, S.A.1    Kim, I.2    Liu, C.W.3    Puglisi, J.D.4
  • 34
    • 44149112583 scopus 로고    scopus 로고
    • Nucleoside modifications modulate activation of the protein kinase PKR in an RNA structure-specific manner
    • DOI 10.1261/rna.1007408
    • Nallagatla SR, Bevilacqua PC. 2008. Nucleoside modifications modulate activation of the protein kinase PKR in an RNA structure-specific manner. RNA 14: 1201-1213. (Pubitemid 351717499)
    • (2008) RNA , vol.14 , Issue.6 , pp. 1201-1213
    • Nallagatla, S.R.1    Bevilacqua, P.C.2
  • 35
    • 36749086446 scopus 로고    scopus 로고
    • 5'-triphosphate-dependent activation of PKR by RNAs with short stem-loops
    • DOI 10.1126/science.1147347
    • Nallagatla SR, Hwang J, Toroney R, Zheng X, Cameron CE, Bevilacqua PC. 2007. 5'-triphosphate-dependent activation of PKR by RNAs with short stem-loops. Science 318: 1455-1458. (Pubitemid 350208957)
    • (2007) Science , vol.318 , Issue.5855 , pp. 1455-1458
    • Nallagatla, S.R.1    Hwang, J.2    Toroney, R.3    Zheng, X.4    Cameron, C.E.5    Bevilacqua, P.C.6
  • 36
    • 0032530310 scopus 로고    scopus 로고
    • Structure of the double-stranded RNA-binding domain of the protein kinase PKR reveals the molecular basis of its dsRNA-mediated activation
    • DOI 10.1093/emboj/17.18.5458
    • Nanduri S, Carpick BW, Yang Y, Williams BR, Qin J. 1998. Structure of the double-stranded RNA-binding domain of the protein kinase PKR reveals the molecular basis of its dsRNA-mediated activation. EMBO J 17: 5458-5465. (Pubitemid 28427059)
    • (1998) EMBO Journal , vol.17 , Issue.18 , pp. 5458-5465
    • Nanduri, S.1    Carpick, B.W.2    Yang, Y.3    Williams, B.R.G.4    Qin, J.5
  • 39
    • 84857029766 scopus 로고    scopus 로고
    • Determination of a molecular shape for netrin-4 from hydrodynamic and small angle X-ray scattering measurements
    • Patel TR, Reuten R, Xiong S, Meier M, Winzor DJ, Koch M, Stetefeld J. 2012. Determination of a molecular shape for netrin-4 from hydrodynamic and small angle X-ray scattering measurements. Matrix Biol 31: 135-140.
    • (2012) Matrix Biol , vol.31 , pp. 135-140
    • Patel, T.R.1    Reuten, R.2    Xiong, S.3    Meier, M.4    Winzor, D.J.5    Koch, M.6    Stetefeld, J.7
  • 40
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • DOI 10.1529/biophysj.105.064154
    • Petoukhov MV, Svergun DI. 2005. Global rigid body modeling of macromolecular complexes against small-angle scattering data. Biophys J 89: 1237-1250. (Pubitemid 41099005)
    • (2005) Biophysical Journal , vol.89 , Issue.2 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 42
    • 33750201146 scopus 로고    scopus 로고
    • Controlling activation of the RNA-dependent protein kinase by siRNAs using site-specific chemical modification
    • DOI 10.1093/nar/gkl464
    • Puthenveetil S, Whitby L, Ren J, Kelnar K, Krebs JF, Beal PA. 2006. Controlling activation of the RNA-dependent protein kinase by siRNAs using site-specific chemical modification. Nucleic Acids Res 34: 4900-4911. (Pubitemid 44605633)
    • (2006) Nucleic Acids Research , vol.34 , Issue.17 , pp. 4900-4911
    • Puthenveetil, S.1    Whitby, L.2    Ren, J.3    Kelnar, K.4    Krebs, J.F.5    Beal, P.A.6
  • 45
    • 0032535613 scopus 로고    scopus 로고
    • Molecular basis of double-stranded RNA-protein interactions: Structure of a dsRNA-binding domain complexed with dsRNA
    • DOI 10.1093/emboj/17.24.7505
    • Ryter JM, Schultz SC. 1998. Molecular basis of double-stranded RNAprotein interactions: Structure of a dsRNA-binding domain complexed with dsRNA. EMBO J 17: 7505-7513. (Pubitemid 29002717)
    • (1998) EMBO Journal , vol.17 , Issue.24 , pp. 7505-7513
    • Ryter, J.M.1    Schultz, S.C.2
  • 46
    • 46249115827 scopus 로고    scopus 로고
    • Interferon-inducible antiviral effectors
    • DOI 10.1038/nri2314, PII NRI2314
    • Sadler AJ, Williams BR. 2008. Interferon-inducible antiviral effectors. Nat Rev Immunol 8: 559-568. (Pubitemid 351913674)
    • (2008) Nature Reviews Immunology , vol.8 , Issue.7 , pp. 559-568
    • Sadler, A.J.1    Williams, B.R.G.2
  • 47
    • 0037711199 scopus 로고    scopus 로고
    • The dsRNA binding protein family: Critical roles, diverse cellular functions
    • DOI 10.1096/fj.02-0958rev
    • Saunders LR, Barber GN. 2003. The dsRNA binding protein family: Critical roles, diverse cellular functions. FASEB J 17: 961-983. (Pubitemid 36676385)
    • (2003) FASEB Journal , vol.17 , Issue.9 , pp. 961-983
    • Saunders, L.R.1    Barber, G.N.2
  • 48
    • 0024600978 scopus 로고
    • Activation of interferon-regulated, dsRNA-dependent enzymes by human immunodeficiency virus-1 leader RNA
    • SenGupta DN, Silverman RH. 1989. Activation of interferon-regulated, dsRNA-dependent enzymes by human immunodeficiency virus-1 leader RNA. Nucleic Acids Res 17: 969-978. (Pubitemid 19062884)
    • (1989) Nucleic Acids Research , vol.17 , Issue.3 , pp. 969-978
    • SenGupta, D.N.1    Silverman, R.H.2
  • 49
    • 60149091189 scopus 로고    scopus 로고
    • Regulation of translation initiation in eukaryotes: Mechanisms and biological targets
    • Sonenberg N, Hinnebusch AG. 2009. Regulation of translation initiation in eukaryotes: Mechanisms and biological targets. Cell 136: 731-745.
    • (2009) Cell , vol.136 , pp. 731-745
    • Sonenberg, N.1    Hinnebusch, A.G.2
  • 51
    • 0034711012 scopus 로고    scopus 로고
    • Phosphorylation of serine 51 in initiation factor 2α (eIF2α) promotes complex formation between eIF2α(P) and eIF2B and causes inhibition in the guanine nucleotide exchange activity of eIF2B
    • Sudhakar A, Ramachandran A, Ghosh S, Hasnain SE, Kaufman RJ, Ramaiah KV. 2000. Phosphorylation of serine 51 in initiation factor 2α (eIF2α) promotes complex formation between eIF2α(P) and eIF2B and causes inhibition in the guanine nucleotide exchange activity of eIF2B. Biochemistry 39: 12929-12938.
    • (2000) Biochemistry , vol.39 , pp. 12929-12938
    • Sudhakar, A.1    Ramachandran, A.2    Ghosh, S.3    Hasnain, S.E.4    Kaufman, R.J.5    Ramaiah, K.V.6
  • 52
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • DOI 10.1107/S0021889892001663
    • Svergun DI. 1992. Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J Appl Crystallogr 25: 495-503. (Pubitemid 23564996)
    • (1992) Journal of Applied Crystallography , vol.25 , Issue.PART 4 , pp. 495-503
    • Svergun, D.I.1
  • 53
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun DI. 1999. Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys J 76: 2879-2886. (Pubitemid 29269438)
    • (1999) Biophysical Journal , vol.76 , Issue.6 , pp. 2879-2886
    • Svergun, D.I.1
  • 54
    • 0027420488 scopus 로고
    • Mechanism of interferon action: Evidence for intermolecular autophosphorylation and autoactivation of the interferon-induced, RNA- dependent protein kinase PKR
    • Thomis DC, Samuel CE. 1993. Mechanism of interferon action: Evidence for intermolecular autophosphorylation and autoactivation of the interferon-induced, RNA-dependent protein kinase PKR. J Virol 67: 7695-7700. (Pubitemid 23343908)
    • (1993) Journal of Virology , vol.67 , Issue.12 , pp. 7695-7700
    • Thomis, D.C.1    Samuel, C.E.2
  • 56
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov VV, Svergun DI. 2003. Uniqueness of ab initio shape determination in small-angle scattering. J Appl Crystallogr 36: 860-864.
    • (2003) J Appl Crystallogr , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 57
    • 12544256134 scopus 로고    scopus 로고
    • Calculation of standard atomic volumes for RNA and comparison with proteins: RNA is packed more tightly
    • Voss NR, Gerstein M. 2005. Calculation of standard atomic volumes for RNA and comparison with proteins: RNA is packed more tightly. J Mol Biol 346: 477-492.
    • (2005) J Mol Biol , vol.346 , pp. 477-492
    • Voss, N.R.1    Gerstein, M.2
  • 58
    • 33646453915 scopus 로고    scopus 로고
    • Double-stranded RNA is produced by positive-strand RNA viruses and DNA viruses but not in detectable amounts by negative-strand RNA viruses
    • Weber F, Wagner V, Rasmussen SB, Hartmann R, Paludan SR. 2006. Double-stranded RNA is produced by positive-strand RNA viruses and DNA viruses but not in detectable amounts by negative-strand RNA viruses. J Virol 80: 5059-5064.
    • (2006) J Virol , vol.80 , pp. 5059-5064
    • Weber, F.1    Wagner, V.2    Rasmussen, S.B.3    Hartmann, R.4    Paludan, S.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.