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Volumn 13, Issue 8, 2015, Pages 488-506

An RNA Hybridization Assay for Screening Influenza A Virus Polymerase Inhibitors Using the Entire Ribonucleoprotein Complex

Author keywords

[No Author keywords available]

Indexed keywords

ANTIVIRUS AGENT; CAP BINDING INHIBITOR; CAP BINDING PROTEIN; EMBL R 05 1; EMBL R 05 2; EMBL R 05 3; ENDONUCLEASE; ENDONUCLEASE INHIBITOR; ENZYME INHIBITOR; FAVIPIRAVIR; FOLIC ACID; INFLUENZA A VIRUS POLYMERASE INHIBITOR; MONOSELECTIVE POLYMERASE INHIBITOR; NUCLEOZIN; RIBAVIRIN; RIBONUCLEOPROTEIN; RIBONUCLEOPROTEIN COMPLEX; RNA POLYMERASE; UNCLASSIFIED DRUG; VIRUS MESSENGER RNA; DNA DIRECTED RNA POLYMERASE;

EID: 84944452242     PISSN: 1540658X     EISSN: 15578127     Source Type: Journal    
DOI: 10.1089/adt.2015.668     Document Type: Article
Times cited : (7)

References (51)
  • 1
    • 60549110717 scopus 로고    scopus 로고
    • WHO Last accessed on March 9, 2015
    • WHO: Influenza fact sheet. 2014. www.who.int/mediaeentre/faetsheets/fs211/en/. (Last accessed on March 9, 2015).
    • (2014) Influenza Fact Sheet
  • 2
    • 84863754680 scopus 로고    scopus 로고
    • An overlapping protein-coding region in influenza A virus segment 3 modulates the host response
    • Jagger BW, Wise HM, Kash JC, et al.: An overlapping protein-coding region in influenza A virus segment 3 modulates the host response. Science 2012;337:199-204.
    • (2012) Science , vol.337 , pp. 199-204
    • Jagger, B.W.1    Wise, H.M.2    Kash, J.C.3
  • 3
    • 67749133883 scopus 로고    scopus 로고
    • A complicated message: Identification of a novel PB1-related protein translated from influenza A virus segment 2 mRNA
    • Wise HM, Foeglein A, Sun J, et al: A complicated message: identification of a novel PB1-related protein translated from influenza A virus segment 2 mRNA. J Virol 2009;83:8021-8031.
    • (2009) J Virol , vol.83 , pp. 8021-8031
    • Wise, H.M.1    Foeglein, A.2    Sun, J.3
  • 4
    • 84864228530 scopus 로고    scopus 로고
    • Antivirals targeting influenza A virus
    • Das K: Antivirals targeting influenza A virus. J Med Chem 2012;55:6263-6277.
    • (2012) J Med Chem , vol.55 , pp. 6263-6277
    • Das, K.1
  • 5
    • 77956536783 scopus 로고    scopus 로고
    • Influenza virus polymerase: Structural insights into replication and host adaptation mechanisms
    • Boivin S, Cusaek S, Ruigrok RW, Hart DJ: Influenza virus polymerase: structural insights into replication and host adaptation mechanisms. J Biol Chem 2010; 285:28411-28417.
    • (2010) J Biol Chem , vol.285 , pp. 28411-28417
    • Boivin, S.1    Cusaek, S.2    Ruigrok, R.W.3    Hart, D.J.4
  • 6
    • 84879569272 scopus 로고    scopus 로고
    • Influenza virus transcription and replication
    • Martin-Benito J, Ortin J: Influenza virus transcription and replication. Adv Virus Res 2013;87:113-137.
    • (2013) Adv Virus Res , vol.87 , pp. 113-137
    • Martin-Benito, J.1    Ortin, J.2
  • 7
    • 84880367286 scopus 로고    scopus 로고
    • The RNA polymerase of influenza a virus: Mechanisms of viral transcription and replication
    • Fodor E: The RNA polymerase of influenza a virus: mechanisms of viral transcription and replication. Acta Wro/2013;57:113-122.
    • (2013) Acta Wro , vol.57 , pp. 113-122
    • Fodor, E.1
  • 9
    • 0028171260 scopus 로고
    • Inhibition of cap (m7GpppXm)-dependent endonuelease of influenza virus by 4-substituted 2, 4-dioxobutanoie acid compounds
    • Tomassini J, Selniek H, Davies ME, et al: Inhibition of cap (m7GpppXm)-dependent endonuelease of influenza virus by 4-substituted 2, 4-dioxobutanoie acid compounds. Antimicrob Agents Chemother 1994;38:2827-2837.
    • (1994) Antimicrob Agents Chemother , vol.38 , pp. 2827-2837
    • Tomassini, J.1    Selniek, H.2    Davies, M.E.3
  • 10
    • 0029990093 scopus 로고    scopus 로고
    • A novel antiviral agent which inhibits the endonuelease of influenza viruses
    • Tomassini JE, Davies ME, Hastings JC, et al: A novel antiviral agent which inhibits the endonuelease of influenza viruses. Antimicrob Agents Chemother 1996;40:1189-1193.
    • (1996) Antimicrob Agents Chemother , vol.40 , pp. 1189-1193
    • Tomassini, J.E.1    Davies, M.E.2    Hastings, J.C.3
  • 11
    • 0344453794 scopus 로고    scopus 로고
    • Use of a pharmacophore model to discover a new class of influenza endonuelease inhibitors
    • Parkes KEB, Ermert P, Fuhssler J, et al: Use of a pharmacophore model to discover a new class of influenza endonuelease inhibitors. J Med Chem 2003;46:1153-1164.
    • (2003) J Med Chem , vol.46 , pp. 1153-1164
    • Parkes, K.E.B.1    Ermert, P.2    Fuhssler, J.3
  • 12
    • 0038182864 scopus 로고    scopus 로고
    • Quantitative analysis of influenza virus RNP interaction with RNA cap structures and comparison to human cap binding protein elF4E
    • Hooker L, Sully RR, Handa B, Ono N, Koyano H, Klumpp K: Quantitative analysis of influenza virus RNP interaction with RNA cap structures and comparison to human cap binding protein elF4E. Biochemistry 2003;42: 6234-6240.
    • (2003) Biochemistry , vol.42 , pp. 6234-6240
    • Hooker, L.1    Sully, R.R.2    Handa, B.3    Ono, N.4    Koyano, H.5    Klumpp, K.6
  • 13
    • 0037938782 scopus 로고    scopus 로고
    • Effectiveness of neuraminidase inhibitors in treatment and prevention of influenza A and B: Systematic review and meta-analyses of randomised controlled trials
    • Cooper NJ, Sutton AJ, Abrams KR, Wailoo A, Turner D, Nicholson KG: Effectiveness of neuraminidase inhibitors in treatment and prevention of influenza A and B: systematic review and meta-analyses of randomised controlled trials. BMJ 2003;326:1235.
    • (2003) BMJ , vol.326
    • Cooper, N.J.1    Sutton, A.J.2    Abrams, K.R.3    Wailoo, A.4    Turner, D.5    Nicholson, K.G.6
  • 14
    • 79851496686 scopus 로고    scopus 로고
    • Emerging influenza antiviral resistance threats
    • Hayden FG, de Jong MD: Emerging influenza antiviral resistance threats. J Infect Dis 2011;203:6-10.
    • (2011) J Infect Dis , vol.203 , pp. 6-10
    • Hayden, F.G.1    De Jong, M.D.2
  • 15
    • 57749187455 scopus 로고    scopus 로고
    • Developing new antiviral agents for influenza treatment: What does the future hold?
    • Hayden F: Developing new antiviral agents for influenza treatment: what does the future hold? Clin Infect Dis 2009;48:3-13.
    • (2009) Clin Infect Dis , vol.48 , pp. 3-13
    • Hayden, F.1
  • 16
    • 84871460710 scopus 로고    scopus 로고
    • The structure of native influenza virion ribonucleoproteins
    • Arranz R, Coloma R, Chichon FJ, et al: The structure of native influenza virion ribonucleoproteins. Science 2012;338:1634-1637.
    • (2012) Science , vol.338 , pp. 1634-1637
    • Arranz, R.1    Coloma, R.2    Chichon, F.J.3
  • 18
    • 67249130012 scopus 로고    scopus 로고
    • The cap-snatching endonuelease of influenza virus polymerase resides in the PA subunit
    • Dias A, Bouvier D, Crepin T, et al.: The cap-snatching endonuelease of influenza virus polymerase resides in the PA subunit. Nature 2009;458:914-918.
    • (2009) Nature , vol.458 , pp. 914-918
    • Dias, A.1    Bouvier, D.2    Crepin, T.3
  • 19
    • 50649089174 scopus 로고    scopus 로고
    • Crystal structure of the polymerase PA-C-PB1-N complex from an avian influenza H5N1 virus
    • He X, Zhou J, Bartlam M, et al: Crystal structure of the polymerase PA-C-PB1-N complex from an avian influenza H5N1 virus. Nature 2008;454:1123-1126.
    • (2008) Nature , vol.454 , pp. 1123-1126
    • He, X.1    Zhou, J.2    Bartlam, M.3
  • 20
    • 67649552964 scopus 로고    scopus 로고
    • Structural insight into the essential PB1-PB2 subunit contact of the influenza virus RNA polymerase
    • Sugiyama K, Obayashi E, Kawaguchi A, et al: Structural insight into the essential PB1-PB2 subunit contact of the influenza virus RNA polymerase. EMBO Journal 2009;28:1803-1811.
    • (2009) EMBO Journal , vol.28 , pp. 1803-1811
    • Sugiyama, K.1    Obayashi, E.2    Kawaguchi, A.3
  • 21
    • 58149251913 scopus 로고    scopus 로고
    • The structural basis for cap binding by influenza virus polymerase subunit PB2
    • Guilligay D, Tarendeau F, Resa-lnfante P:The structural basis for cap binding by influenza virus polymerase subunit PB2. Chemtracts 2008;20:509-510.
    • (2008) Chemtracts , vol.20 , pp. 509-510
    • Guilligay, D.1    Tarendeau, F.2    Resa-Lnfante, P.3
  • 22
    • 50849137828 scopus 로고    scopus 로고
    • Host determinant residue lysine 627 lies on the surface of a discrete, folded domain of influenza virus polymerase PB2 subunit
    • Tarendeau F, Crepin T, Guilligay D, Ruigrok RWH, Cusaek S, Hart DJ: Host determinant residue lysine 627 lies on the surface of a discrete, folded domain of influenza virus polymerase PB2 subunit. PioS Pathog 2008;4; e1000136.
    • (2008) PioS Pathog , vol.4 , pp. e1000136
    • Tarendeau, F.1    Crepin, T.2    Guilligay, D.3    Ruigrok, R.W.H.4    Cusaek, S.5    Hart, D.J.6
  • 23
    • 84922257981 scopus 로고    scopus 로고
    • Structure of influenza A polymerase bound to the viral RNA promoter
    • Pflug A, Guilligay D, Reich S, Cusaek S: Structure of influenza A polymerase bound to the viral RNA promoter. Nature 2014;516:355-360.
    • (2014) Nature , vol.516 , pp. 355-360
    • Pflug, A.1    Guilligay, D.2    Reich, S.3    Cusaek, S.4
  • 24
    • 84922245983 scopus 로고    scopus 로고
    • Structural insight into cap-snatching and RNA synthesis by influenza polymerase
    • Reich S, Guilligay D, Pflug A, et al: Structural insight into cap-snatching and RNA synthesis by influenza polymerase. Nature 2014;516:361-366.
    • (2014) Nature , vol.516 , pp. 361-366
    • Reich, S.1    Guilligay, D.2    Pflug, A.3
  • 25
    • 84866146827 scopus 로고    scopus 로고
    • Structural and biochemical basis for development of influenza virus inhibitors targeting the PA endonuelease
    • Dubois RM, Slavish PJ, Baughman BM, et al: Structural and biochemical basis for development of influenza virus inhibitors targeting the PA endonuelease. PioS Pathog 2012;8:e1002830.
    • (2012) PioS Pathog , vol.8 , pp. e1002830
    • Dubois, R.M.1    Slavish, P.J.2    Baughman, B.M.3
  • 26
    • 84885187718 scopus 로고    scopus 로고
    • Phenyl substituted 3-hydroxypyridin-2(1H)-ones: Inhibitors of influenza A endonuelease
    • Parhi AK, Xiang A, Bauman JD, et al: Phenyl substituted 3-hydroxypyridin-2(1H)-ones: inhibitors of influenza A endonuelease. Bioorg Med Chem 2013;21: 6435-6446.
    • (2013) Bioorg Med Chem , vol.21 , pp. 6435-6446
    • Parhi, A.K.1    Xiang, A.2    Bauman, J.D.3
  • 27
    • 84866177810 scopus 로고    scopus 로고
    • Structural analysis of specific metal chelating inhibitor binding totheendonuclease domain of influenza pHINI (2009) polymerase
    • Kowalinski E, Zubieta C, Wolkerstorfer A, Szolar OH, Ruigrok RW, Cusack S: Structural analysis of specific metal chelating inhibitor binding totheendonuclease domain of influenza pHINI (2009) polymerase. P/-oSPoftog2012;8:e1002831.
    • (2012) PoS Poftog , vol.8 , pp. e1002831
    • Kowalinski, E.1    Zubieta, C.2    Wolkerstorfer, A.3    Szolar, O.H.4    Ruigrok, R.W.5    Cusack, S.6
  • 28
    • 79960587884 scopus 로고    scopus 로고
    • Free energy calculations and binding analysis of two potential anti-influenza drugs with Polymerase basic protein-2 (PB2)
    • Lv HM, Guo XL, Gu RX, Wei DQ: Free energy calculations and binding analysis of two potential anti-influenza drugs with Polymerase basic protein-2 (PB2). Protein Pept Lett 2011 ;18:1002-1009.
    • (2011) Protein Pept Lett , vol.18 , pp. 1002-1009
    • Lv, H.M.1    Guo, X.L.2    Gu, R.X.3    Wei, D.Q.4
  • 29
    • 84887926053 scopus 로고    scopus 로고
    • New 7-methylguanine derivatives targeting the influenza polymerase PB2 cap-binding domain
    • Pautus S, Sehr P, Lewis J, ef at New 7-methylguanine derivatives targeting the influenza polymerase PB2 cap-binding domain. J Med Chem 2013;56:8915-8930.
    • (2013) J Med Chem , vol.56 , pp. 8915-8930
    • Pautus, S.1    Sehr, P.2    Lewis, J.3
  • 30
    • 84944466538 scopus 로고    scopus 로고
    • Panomics Affymetrix/Panomics Brochure Last accessed on March 9, 2015
    • Panomics: QuantiGene 2.0 Gene Expression without the Limitations. Affymetrix/Panomics Brochure. 2007. www.panomics.com/products/gene-expression/single-plex-assay/literature-support (Last accessed on March 9, 2015).
    • (2007) QuantiGene 2.0 Gene Expression Without the Limitations
  • 31
    • 43249128376 scopus 로고    scopus 로고
    • The structural basis for cap binding by influenza virus polymerase subunit PB2
    • Guilligay D, Tarendeau F, Resa-lnfante P, et al: The structural basis for cap binding by influenza virus polymerase subunit PB2. Nat Struct Mol Biol 2008; 15:500-506.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 500-506
    • Guilligay, D.1    Tarendeau, F.2    Resa-Lnfante, P.3
  • 32
    • 7444262377 scopus 로고    scopus 로고
    • Development and optimization of a binding assay for the XIAP BIR3 domain using fluorescence polarization
    • Nikolovska-Coleska Z, Wang R, Fang X, et al Development and optimization of a binding assay for the XIAP BIR3 domain using fluorescence polarization. Anal Biochem 2004;332:261-273.
    • (2004) Anal Biochem , vol.332 , pp. 261-273
    • Nikolovska-Coleska, Z.1    Wang, R.2    Fang, X.3
  • 33
    • 84858635392 scopus 로고    scopus 로고
    • Identification of influenza endonuclease inhibitors using a novel fluorescence polarization assay
    • Baughman BM, Jake SP, Dubois RM, Boyd VA, White SW, Webb TR: Identification of influenza endonuclease inhibitors using a novel fluorescence polarization assay. ACS Chem Biol 2012;7:526-534.
    • (2012) ACS Chem Biol , vol.7 , pp. 526-534
    • Baughman, B.M.1    Jake, S.P.2    Dubois, R.M.3    Boyd, V.A.4    White, S.W.5    Webb, T.R.6
  • 35
    • 84922770299 scopus 로고    scopus 로고
    • Panomics Last accessed on March 9, 2015
    • Panomics: QuantiGene 2.0 Reagent System. User Manual. 2007. www.panomics.com/downloads/UM13074-QG2Manual-RevB-080102.pdf. (Last accessed on March 9, 2015).
    • (2007) QuantiGene 2.0 Reagent System. User Manual
  • 36
    • 84884961327 scopus 로고    scopus 로고
    • Characterization of PA-N terminal domain of influenza A polymerase reveals sequence specific RNA cleavage
    • Datta K, Wolkerstorfer A, Szolar OH, Cusack S, Klumpp K: Characterization of PA-N terminal domain of influenza A polymerase reveals sequence specific RNA cleavage. Nucleic Acids Res 2013;41:8289-8299.
    • (2013) Nucleic Acids Res , vol.41 , pp. 8289-8299
    • Datta, K.1    Wolkerstorfer, A.2    Szolar, O.H.3    Cusack, S.4    Klumpp, K.5
  • 37
    • 33745158157 scopus 로고
    • A simple method of estimating fifty per cent end points
    • Reed U, Muench H: A simple method of estimating fifty per cent end points. Am J Epidemiol 1938;27:493-497.
    • (1938) Am J Epidemiol , vol.27 , pp. 493-497
    • Reed, U.1    Muench, H.2
  • 38
    • 33144488409 scopus 로고    scopus 로고
    • Different de novo initiation strategies are used by influenza virus RNA polymerase on its cRNA and viral RNA promoters during viral RNA replication
    • Deng T, Vreede FT, Brownlee GG. Different de novo initiation strategies are used by influenza virus RNA polymerase on its cRNA and viral RNA promoters during viral RNA replication. J Virol 2006;80:2337-2348.
    • (2006) J Virol , vol.80 , pp. 2337-2348
    • Deng, T.1    Vreede, F.T.2    Brownlee, G.G.3
  • 39
    • 0022021473 scopus 로고
    • Activation of influenza virus-associated RNA polymerase by cap-1 structure (m7GpppNm)
    • Kawakami K, Mizumoto K, Ishihama A, Shinozaki-Yamaguchi K, Miura K: Activation of influenza virus-associated RNA polymerase by cap-1 structure (m7GpppNm). J Biochem 1985;97:655-661.
    • (1985) J Biochem , vol.97 , pp. 655-661
    • Kawakami, K.1    Mizumoto, K.2    Ishihama, A.3    Shinozaki-Yamaguchi, K.4    Miura, K.5
  • 40
    • 0033608967 scopus 로고    scopus 로고
    • Metal ion catalysis of RNA cleavage by the influenza virus endonuclease
    • Doan L, Handa B, Roberts NA, Klumpp K: Metal ion catalysis of RNA cleavage by the influenza virus endonuclease. Biochemistry 1999;38:5612-5619.
    • (1999) Biochemistry , vol.38 , pp. 5612-5619
    • Doan, L.1    Handa, B.2    Roberts, N.A.3    Klumpp, K.4
  • 41
    • 77956030336 scopus 로고    scopus 로고
    • Mutational and metal binding analysis of the endonuclease domain of the influenza virus polymerase PA subunit
    • Crepin T, Dias A, Palencia A, Swale C, Cusack S, Ruigrok RW: Mutational and metal binding analysis of the endonuclease domain of the influenza virus polymerase PA subunit. J Virol 2010;84:9096-9104.
    • (2010) J Virol , vol.84 , pp. 9096-9104
    • Crepin, T.1    Dias, A.2    Palencia, A.3    Swale, C.4    Cusack, S.5    Ruigrok, R.W.6
  • 42
    • 77953259427 scopus 로고    scopus 로고
    • Identification of influenza A nucleoprotein as an antiviral target
    • Kao RY, Yang D, Lau LS, et al:. Identification of influenza A nucleoprotein as an antiviral target. Nat Biotechnol 2010;28:600-605.
    • (2010) Nat Biotechnol , vol.28 , pp. 600-605
    • Kao, R.Y.1    Yang, D.2    Lau, L.S.3
  • 43
    • 0015523596 scopus 로고
    • Broad-spectrum antiviral activity of Virazole: 1-beta-D-ribofuranosyl-1,2,4-triazole-3-carboxamide
    • Sidwell RW, Huffman JH, Khare GP, Allen LB, Witkowski JT, Robins RK. Broad-spectrum antiviral activity of Virazole: 1-beta-D-ribofuranosyl-1, 2, 4-triazole-3-carboxamide. Science 1972;177:705-706.
    • (1972) Science , vol.177 , pp. 705-706
    • Sidwell, R.W.1    Huffman, J.H.2    Khare, G.P.3    Allen, L.B.4    Witkowski, J.T.5    Robins, R.K.6
  • 44
    • 0034864547 scopus 로고    scopus 로고
    • Ribavirin-current status of a broad spectrum antiviral agent
    • Snell NJ.: Ribavirin-current status of a broad spectrum antiviral agent. Expert Opin Pharmacother 2001;2:1317-1324.
    • (2001) Expert Opin Pharmacother , vol.2 , pp. 1317-1324
    • Snell, N.J.1
  • 45
    • 0036211719 scopus 로고    scopus 로고
    • In vitro and in vivo activities of anti-influenza virus compound T-705
    • Furuta Y. Takahashi K, Fukuda Y, et al:. In vitro and in vivo activities of anti-influenza virus compound T-705. Antimicrob Agents Chemother 2002;46:977-981.
    • (2002) Antimicrob Agents Chemother , vol.46 , pp. 977-981
    • Furuta, Y.1    Takahashi, K.2    Fukuda, Y.3
  • 46
    • 64749093901 scopus 로고    scopus 로고
    • T-705 (favipiravir) and related compounds: Novel broad-spectrum inhibitors of RNA viral infections
    • Furuta Y, Takahashi K, Shiraki K, et al: T-705 (favipiravir) and related compounds: novel broad-spectrum inhibitors of RNA viral infections. Antiviral Res 2009;82:95-102.
    • (2009) Antiviral Res , vol.82 , pp. 95-102
    • Furuta, Y.1    Takahashi, K.2    Shiraki, K.3
  • 47
    • 0036182633 scopus 로고    scopus 로고
    • Ribavirin's antiviral mechanism of action: Lethal mutagenesis?
    • Crotty S, Cameron C, Andino R.: Ribavirin's antiviral mechanism of action: lethal mutagenesis? J Mol Med (Berlj 2002;80:86-95.
    • (2002) J Mol Med (Berl) , vol.80 , pp. 86-95
    • Crotty, S.1    Cameron, C.2    Andino, R.3
  • 48
    • 0035208293 scopus 로고    scopus 로고
    • The mechanism of action of ribavirin: Lethal mutagenesis of RNA virus genomes mediated by the viral RNA-dependent RNA polymerase
    • Cameron CE, Castro C: The mechanism of action of ribavirin: lethal mutagenesis of RNA virus genomes mediated by the viral RNA-dependent RNA polymerase. Curr Opin Infect Dis 2001;14:757-764.
    • (2001) Curr Opin Infect Dis , vol.14 , pp. 757-764
    • Cameron, C.E.1    Castro, C.2
  • 49
    • 11144220618 scopus 로고    scopus 로고
    • Ribavirin suppresses elF4E-mediated oncogenic transformation by physical mimicry of the 7-methyl guanosine mRNA cap
    • Kentsis A, Topisirovic I, Culjkovic B, Shao L, Borden KLB.: Ribavirin suppresses elF4E-mediated oncogenic transformation by physical mimicry of the 7-methyl guanosine mRNA cap. Proc Natl Acad Sei USA 2004;101:18105-18110.
    • (2004) Proc Natl Acad Sei USA , vol.101 , pp. 18105-18110
    • Kentsis, A.1    Topisirovic, I.2    Culjkovic, B.3    Shao, L.4    Borden, K.L.B.5
  • 50
    • 0030826444 scopus 로고    scopus 로고
    • Structure of translation factor elF4E bound to m7GDP and interaction with 4E-binding protein
    • Matsuo H, Li H, McGuire AM, et al. Structure of translation factor elF4E bound to m7GDP and interaction with 4E-binding protein. Nat Struct Biol 1997;4:717-724.
    • (1997) Nat Struct Biol , vol.4 , pp. 717-724
    • Matsuo, H.1    Li, H.2    McGuire, A.M.3
  • 51
    • 23644440980 scopus 로고    scopus 로고
    • Ribavirin is not a functional mimic of the 7-methyl guanosine mRNA cap
    • Yan Y, Svitkin Y, Lee JM, Bisaillon M, Pelletier J.: Ribavirin is not a functional mimic of the 7-methyl guanosine mRNA cap. RNA 2005;11:1238-1244.
    • (2005) RNA , vol.11 , pp. 1238-1244
    • Yan, Y.1    Svitkin, Y.2    Lee, J.M.3    Bisaillon, M.4    Pelletier, J.5


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