메뉴 건너뛰기




Volumn 169, Issue 1, 2012, Pages 80-90

RNA binding by the NS3 protease of the hepatitis C virus

Author keywords

ATPase activation; Hepatitis C virus; NS3 protease; Nucleic acid inhibitors; Positive strand RNA virus; RNA binding

Indexed keywords

ADENOSINE TRIPHOSPHATASE; HELICASE; NONSTRUCTURAL PROTEIN 3; PROTEINASE; SINGLE STRANDED RNA;

EID: 84867213168     PISSN: 01681702     EISSN: 18727492     Source Type: Journal    
DOI: 10.1016/j.virusres.2012.07.007     Document Type: Article
Times cited : (5)

References (67)
  • 1
    • 57649217269 scopus 로고    scopus 로고
    • Hepatitis C viral NS3-4A protease activity is enhanced by the NS3 helicase
    • Beran R.K., Pyle A.M. Hepatitis C viral NS3-4A protease activity is enhanced by the NS3 helicase. Journal of Biological Chemistry 2008, 283(44):29929-29937.
    • (2008) Journal of Biological Chemistry , vol.283 , Issue.44 , pp. 29929-29937
    • Beran, R.K.1    Pyle, A.M.2
  • 2
    • 36849075152 scopus 로고    scopus 로고
    • The serine protease domain of hepatitis C viral NS3 activates RNA helicase activity by promoting the binding of RNA substrate
    • Beran R.K., Serebrov V., Pyle A.M. The serine protease domain of hepatitis C viral NS3 activates RNA helicase activity by promoting the binding of RNA substrate. Journal of Biological Chemistry 2007, 282(48):34913-34920.
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.48 , pp. 34913-34920
    • Beran, R.K.1    Serebrov, V.2    Pyle, A.M.3
  • 3
    • 7644238616 scopus 로고    scopus 로고
    • The severe acute respiratory syndrome coronavirus Nsp15 protein is an endoribonuclease that prefers manganese as a cofactor
    • Bhardwaj K., Guarino L., Kao C.C. The severe acute respiratory syndrome coronavirus Nsp15 protein is an endoribonuclease that prefers manganese as a cofactor. Journal of Virology 2004, 78(22):12218-12224.
    • (2004) Journal of Virology , vol.78 , Issue.22 , pp. 12218-12224
    • Bhardwaj, K.1    Guarino, L.2    Kao, C.C.3
  • 7
    • 23944481107 scopus 로고    scopus 로고
    • Unscrambling hepatitis C virus-host interactions
    • Chisari F.V. Unscrambling hepatitis C virus-host interactions. Nature 2005, 436(7053):930-932.
    • (2005) Nature , vol.436 , Issue.7053 , pp. 930-932
    • Chisari, F.V.1
  • 8
    • 0024509701 scopus 로고
    • Isolation of a cDNA clone derived from a blood-borne non-A, non-B viral hepatitis genome
    • Choo Q.L., Kuo G., Weiner A.J., Overby L.R., Bradley D.W., Houghton M. Isolation of a cDNA clone derived from a blood-borne non-A, non-B viral hepatitis genome. Science 1989, 244(4902):359-362.
    • (1989) Science , vol.244 , Issue.4902 , pp. 359-362
    • Choo, Q.L.1    Kuo, G.2    Weiner, A.J.3    Overby, L.R.4    Bradley, D.W.5    Houghton, M.6
  • 10
    • 35748984642 scopus 로고    scopus 로고
    • Effects on protease inhibition by modifying of helicase residues in hepatitis C virus nonstructural protein 3
    • Dahl G., Sandstrom A., Akerblom E., Danielson U.H. Effects on protease inhibition by modifying of helicase residues in hepatitis C virus nonstructural protein 3. FEBS Journal 2007, 274(22):5979-5986.
    • (2007) FEBS Journal , vol.274 , Issue.22 , pp. 5979-5986
    • Dahl, G.1    Sandstrom, A.2    Akerblom, E.3    Danielson, U.H.4
  • 11
    • 0036100578 scopus 로고    scopus 로고
    • Expression of hepatitis C virus proteins induces distinct membrane alterations including a candidate viral replication complex
    • Egger D., Wolk B., Gosert R., Bianchi L., Blum H.E., Moradpour D., Bienz K. Expression of hepatitis C virus proteins induces distinct membrane alterations including a candidate viral replication complex. Journal of Virology 2002, 76(12):5974-5984.
    • (2002) Journal of Virology , vol.76 , Issue.12 , pp. 5974-5984
    • Egger, D.1    Wolk, B.2    Gosert, R.3    Bianchi, L.4    Blum, H.E.5    Moradpour, D.6    Bienz, K.7
  • 12
    • 4644281168 scopus 로고    scopus 로고
    • An N-terminal amphipathic helix in hepatitis C virus (HCV) NS4B mediates membrane association, correct localization of replication complex proteins, and HCV RNA replication
    • Elazar M., Liu P., Rice C.M., Glenn J.S. An N-terminal amphipathic helix in hepatitis C virus (HCV) NS4B mediates membrane association, correct localization of replication complex proteins, and HCV RNA replication. Journal of Virology 2004, 78(20):11393-11400.
    • (2004) Journal of Virology , vol.78 , Issue.20 , pp. 11393-11400
    • Elazar, M.1    Liu, P.2    Rice, C.M.3    Glenn, J.S.4
  • 13
    • 23944462641 scopus 로고    scopus 로고
    • Mechanism of action of interferon and ribavirin in treatment of hepatitis C
    • Feld J.J., Hoofnagle J.H. Mechanism of action of interferon and ribavirin in treatment of hepatitis C. Nature 2005, 436(7053):967-972.
    • (2005) Nature , vol.436 , Issue.7053 , pp. 967-972
    • Feld, J.J.1    Hoofnagle, J.H.2
  • 14
    • 33846456636 scopus 로고    scopus 로고
    • The hepatitis C virus NS3 protein: a model RNA helicase and potential drug target
    • Frick D.N. The hepatitis C virus NS3 protein: a model RNA helicase and potential drug target. Current Issues in Molecular Biology 2007, 9:1-20.
    • (2007) Current Issues in Molecular Biology , vol.9 , pp. 1-20
    • Frick, D.N.1
  • 15
    • 0346463036 scopus 로고    scopus 로고
    • The nonstructural protein 3 protease/helicase requires an intact protease domain to unwind duplex RNA efficiently
    • Frick D.N., Rypma R.S., Lam A.M., Gu B. The nonstructural protein 3 protease/helicase requires an intact protease domain to unwind duplex RNA efficiently. Journal of Biological Chemistry 2004, 279(2):1269-1280.
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.2 , pp. 1269-1280
    • Frick, D.N.1    Rypma, R.S.2    Lam, A.M.3    Gu, B.4
  • 18
    • 23944485662 scopus 로고    scopus 로고
    • Evasion of intracellular host defence by hepatitis C virus
    • Gale M., Foy E.M. Evasion of intracellular host defence by hepatitis C virus. Nature 2005, 436(7053):939-945.
    • (2005) Nature , vol.436 , Issue.7053 , pp. 939-945
    • Gale, M.1    Foy, E.M.2
  • 19
    • 1842457783 scopus 로고    scopus 로고
    • Interactions between viral nonstructural proteins and host protein hVAP-33 mediate the formation of hepatitis C virus RNA replication complex on lipid raft
    • Gao L., Aizaki H., He J.W., Lai M.M. Interactions between viral nonstructural proteins and host protein hVAP-33 mediate the formation of hepatitis C virus RNA replication complex on lipid raft. Journal of Virology 2004, 78(7):3480-3488.
    • (2004) Journal of Virology , vol.78 , Issue.7 , pp. 3480-3488
    • Gao, L.1    Aizaki, H.2    He, J.W.3    Lai, M.M.4
  • 20
    • 19544394438 scopus 로고    scopus 로고
    • The RNA-unwinding activity of hepatitis C virus non-structural protein 3 (NS3) is positively modulated by its protease domain
    • Gu B., Pruss C.M., Gates A.T., Khandekar S.S. The RNA-unwinding activity of hepatitis C virus non-structural protein 3 (NS3) is positively modulated by its protease domain. Protein and Peptide Letters 2005, 12(4):315-321.
    • (2005) Protein and Peptide Letters , vol.12 , Issue.4 , pp. 315-321
    • Gu, B.1    Pruss, C.M.2    Gates, A.T.3    Khandekar, S.S.4
  • 24
    • 0242473186 scopus 로고    scopus 로고
    • Members of the NF90/NFAR protein group are involved in the life cycle of a positive-strand RNA virus
    • Isken O., Grassmann C.W., Sarisky R.T., Kann M., Zhang S., Grosse F., Kao P.N., Behrens S.E. Members of the NF90/NFAR protein group are involved in the life cycle of a positive-strand RNA virus. EMBO Journal 2003, 22(21):5655-5665.
    • (2003) EMBO Journal , vol.22 , Issue.21 , pp. 5655-5665
    • Isken, O.1    Grassmann, C.W.2    Sarisky, R.T.3    Kann, M.4    Zhang, S.5    Grosse, F.6    Kao, P.N.7    Behrens, S.E.8
  • 26
    • 27944463670 scopus 로고    scopus 로고
    • Probing protein tertiary structure with amidination
    • Janecki D.J., Beardsley R.L., Reilly J.P. Probing protein tertiary structure with amidination. Analytical Chemistry 2005, 77(22):7274-7281.
    • (2005) Analytical Chemistry , vol.77 , Issue.22 , pp. 7274-7281
    • Janecki, D.J.1    Beardsley, R.L.2    Reilly, J.P.3
  • 27
    • 31944452513 scopus 로고    scopus 로고
    • 2Apro is a multifunctional protein that regulates the stability, translation and replication of poliovirus RNA
    • Jurgens C.K., Barton D.J., Sharma N., Morasco B.J., Ogram S.A., Flanegan J.B. 2Apro is a multifunctional protein that regulates the stability, translation and replication of poliovirus RNA. Virology 2006, 345(2):346-357.
    • (2006) Virology , vol.345 , Issue.2 , pp. 346-357
    • Jurgens, C.K.1    Barton, D.J.2    Sharma, N.3    Morasco, B.J.4    Ogram, S.A.5    Flanegan, J.B.6
  • 29
    • 0033920304 scopus 로고    scopus 로고
    • Hepatitis C virus-encoded enzymatic activities and conserved RNA elements in the 3' nontranslated region are essential for virus replication in vivo
    • Kolykhalov A.A., Mihalik K., Feinstone S.M., Rice C.M. Hepatitis C virus-encoded enzymatic activities and conserved RNA elements in the 3' nontranslated region are essential for virus replication in vivo. Journal of Virology 2000, 74(4):2046-2051.
    • (2000) Journal of Virology , vol.74 , Issue.4 , pp. 2046-2051
    • Kolykhalov, A.A.1    Mihalik, K.2    Feinstone, S.M.3    Rice, C.M.4
  • 30
    • 80755159054 scopus 로고    scopus 로고
    • Discovery and development of telaprevir: an NS3-4A protease inhibitor for treating genotype 1 chronic hepatitis C virus
    • Kwong A.D., Kauffman R.S., Hurter P., Mueller P. Discovery and development of telaprevir: an NS3-4A protease inhibitor for treating genotype 1 chronic hepatitis C virus. Nature Biotechnology 2011, 29(11):993-1003.
    • (2011) Nature Biotechnology , vol.29 , Issue.11 , pp. 993-1003
    • Kwong, A.D.1    Kauffman, R.S.2    Hurter, P.3    Mueller, P.4
  • 31
    • 84862816908 scopus 로고    scopus 로고
    • Recent progress in the development of selected hepatitis C virus NS3-4A protease and NS5B polymerase inhibitors
    • Kwong A.D., McNair L., Jacobson I., George S. Recent progress in the development of selected hepatitis C virus NS3-4A protease and NS5B polymerase inhibitors. Current Opinion in Pharmacology 2008, 8(5):522-531.
    • (2008) Current Opinion in Pharmacology , vol.8 , Issue.5 , pp. 522-531
    • Kwong, A.D.1    McNair, L.2    Jacobson, I.3    George, S.4
  • 32
    • 33645967464 scopus 로고    scopus 로고
    • Hepatitis C virus subgenomic replicon requires an active NS3 RNA helicase
    • Lam A.M., Frick D.N. Hepatitis C virus subgenomic replicon requires an active NS3 RNA helicase. Journal of Virology 2006, 80(1):404-411.
    • (2006) Journal of Virology , vol.80 , Issue.1 , pp. 404-411
    • Lam, A.M.1    Frick, D.N.2
  • 33
    • 70349923633 scopus 로고    scopus 로고
    • B. subtilis ribosomal proteins: structural homology and post-translational modifications
    • Lauber M.A., Running W.E., Reilly J.P. B. subtilis ribosomal proteins: structural homology and post-translational modifications. Journal of Proteome Research 2009, 8(9):4193-4206.
    • (2009) Journal of Proteome Research , vol.8 , Issue.9 , pp. 4193-4206
    • Lauber, M.A.1    Running, W.E.2    Reilly, J.P.3
  • 37
    • 33744913266 scopus 로고    scopus 로고
    • Dissociation of a MAVS/IPS-1/VISA/Cardif-IKKepsilon molecular complex from the mitochondrial outer membrane by hepatitis C virus NS3-4A proteolytic cleavage
    • Lin R., Lacoste J., Nakhaei P., Sun Q., Yang L., Paz S., Wilkinson P., Julkunen I., Vitour D., Meurs E., Hiscott J. Dissociation of a MAVS/IPS-1/VISA/Cardif-IKKepsilon molecular complex from the mitochondrial outer membrane by hepatitis C virus NS3-4A proteolytic cleavage. Journal of Virology 2006, 80(12):6072-6083.
    • (2006) Journal of Virology , vol.80 , Issue.12 , pp. 6072-6083
    • Lin, R.1    Lacoste, J.2    Nakhaei, P.3    Sun, Q.4    Yang, L.5    Paz, S.6    Wilkinson, P.7    Julkunen, I.8    Vitour, D.9    Meurs, E.10    Hiscott, J.11
  • 38
    • 70349970275 scopus 로고    scopus 로고
    • Correlating the chemical modification of Escherichia coli ribosomal proteins with crystal structure data
    • Liu X., Reilly J.P. Correlating the chemical modification of Escherichia coli ribosomal proteins with crystal structure data. Journal of Proteome Research 2009, 8(10):4466-4478.
    • (2009) Journal of Proteome Research , vol.8 , Issue.10 , pp. 4466-4478
    • Liu, X.1    Reilly, J.P.2
  • 39
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method
    • Livak K.J., Schmittgen T.D. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method. Methods 2001, 25:402-408.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 41
    • 0030592514 scopus 로고    scopus 로고
    • The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site
    • Love R.A., Parge H.E., Wickersham J.A., Hostomsky Z., Habuka N., Moomaw E.W., Adachi T., Hostomska Z. The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site. Cell 1996, 87(2):331-342.
    • (1996) Cell , vol.87 , Issue.2 , pp. 331-342
    • Love, R.A.1    Parge, H.E.2    Wickersham, J.A.3    Hostomsky, Z.4    Habuka, N.5    Moomaw, E.W.6    Adachi, T.7    Hostomska, Z.8
  • 44
    • 62249141788 scopus 로고    scopus 로고
    • Boceprevir, an NS3 serine protease inhibitor of hepatitis C virus, for the treatment of HCV infection
    • Mederacke I., Wedemeyer H., Manns M.P. Boceprevir, an NS3 serine protease inhibitor of hepatitis C virus, for the treatment of HCV infection. Current Opinion in Investigational Drugs 2009, 10(2):181-189.
    • (2009) Current Opinion in Investigational Drugs , vol.10 , Issue.2 , pp. 181-189
    • Mederacke, I.1    Wedemeyer, H.2    Manns, M.P.3
  • 45
    • 27144440476 scopus 로고    scopus 로고
    • Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus
    • Meylan E., Curran J., Hofmann K., Moradpour D., Binder M., Bartenschlager R., Tschopp J. Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus. Nature 2005, 437(7062):1167-1172.
    • (2005) Nature , vol.437 , Issue.7062 , pp. 1167-1172
    • Meylan, E.1    Curran, J.2    Hofmann, K.3    Moradpour, D.4    Binder, M.5    Bartenschlager, R.6    Tschopp, J.7
  • 47
    • 0036354884 scopus 로고    scopus 로고
    • Reversible cross-linking combined with immunoprecipitation to study RNA-protein interactions in vivo
    • Niranjanakumari S., Lasda E., Brazas R., Garcia-Blanco M.A. Reversible cross-linking combined with immunoprecipitation to study RNA-protein interactions in vivo. Methods 2002, 26(2):182-190.
    • (2002) Methods , vol.26 , Issue.2 , pp. 182-190
    • Niranjanakumari, S.1    Lasda, E.2    Brazas, R.3    Garcia-Blanco, M.A.4
  • 48
    • 0036500976 scopus 로고    scopus 로고
    • The hepatitis C viral NS3 protein is a processive DNA helicase with cofactor enhanced RNA unwinding
    • Pang P.S., Jankowsky E., Planet P.J., Pyle A.M. The hepatitis C viral NS3 protein is a processive DNA helicase with cofactor enhanced RNA unwinding. EMBO Journal 2002, 21(5):1168-1176.
    • (2002) EMBO Journal , vol.21 , Issue.5 , pp. 1168-1176
    • Pang, P.S.1    Jankowsky, E.2    Planet, P.J.3    Pyle, A.M.4
  • 49
    • 65249106020 scopus 로고    scopus 로고
    • Ribosomal proteins of Deinococcus radiodurans: their solvent accessibility and reactivity
    • Running W.E., Reilly J.P. Ribosomal proteins of Deinococcus radiodurans: their solvent accessibility and reactivity. Journal of Proteome Research 2009, 8(3):1228-1246.
    • (2009) Journal of Proteome Research , vol.8 , Issue.3 , pp. 1228-1246
    • Running, W.E.1    Reilly, J.P.2
  • 50
    • 36049045180 scopus 로고    scopus 로고
    • Human rhinovirus type 14 gain-of-function mutants for oriI utilization define residues of 3C(D) and 3Dpol that contribute to assembly and stability of the picornavirus VPg uridylylation complex
    • Shen M., Wang Q., Yang Y., Pathak H.B., Arnold J.J., Castro C., Lemon S.M., Cameron C.E. Human rhinovirus type 14 gain-of-function mutants for oriI utilization define residues of 3C(D) and 3Dpol that contribute to assembly and stability of the picornavirus VPg uridylylation complex. Journal of Virology 2007, 81(22):12485-12495.
    • (2007) Journal of Virology , vol.81 , Issue.22 , pp. 12485-12495
    • Shen, M.1    Wang, Q.2    Yang, Y.3    Pathak, H.B.4    Arnold, J.J.5    Castro, C.6    Lemon, S.M.7    Cameron, C.E.8
  • 53
    • 0036835590 scopus 로고    scopus 로고
    • Hepatitis C therapeutics: current status and emerging strategies
    • Tan S.L., Pause A., Shi Y., Sonenberg N. Hepatitis C therapeutics: current status and emerging strategies. Nature Reviews Drug Discovery 2002, 1(11):867-881.
    • (2002) Nature Reviews Drug Discovery , vol.1 , Issue.11 , pp. 867-881
    • Tan, S.L.1    Pause, A.2    Shi, Y.3    Sonenberg, N.4
  • 54
    • 0031789165 scopus 로고    scopus 로고
    • Construction, expression, and characterization of a novel fully activated recombinant single-chain hepatitis C virus protease
    • Taremi S.S., Beyer B., Maher M., Yao N., Prosise W., Weber P.C., Malcolm B.A. Construction, expression, and characterization of a novel fully activated recombinant single-chain hepatitis C virus protease. Protein Science 1998, 7(10):2143-2149.
    • (1998) Protein Science , vol.7 , Issue.10 , pp. 2143-2149
    • Taremi, S.S.1    Beyer, B.2    Maher, M.3    Yao, N.4    Prosise, W.5    Weber, P.C.6    Malcolm, B.A.7
  • 55
    • 18244375011 scopus 로고    scopus 로고
    • Rational design of dual-functional aptamers that inhibit the protease and helicase activities of HCV NS3
    • Umehara T., Fukuda K., Nishikawa F., Kohara M., Hasegawa T., Nishikawa S. Rational design of dual-functional aptamers that inhibit the protease and helicase activities of HCV NS3. Journal of Biochemistry 2005, 137(3):339-347.
    • (2005) Journal of Biochemistry , vol.137 , Issue.3 , pp. 339-347
    • Umehara, T.1    Fukuda, K.2    Nishikawa, F.3    Kohara, M.4    Hasegawa, T.5    Nishikawa, S.6
  • 58
    • 43549119526 scopus 로고    scopus 로고
    • A simple and inexpensive on-column frit fabrication method for fused-silica capillaries for increased capacity and versatility in LC-MS/MS applications
    • Wang L.C., Okitsu C.Y., Kochounian H., Rodriguez A., Hsieh C.L., Zandi E. A simple and inexpensive on-column frit fabrication method for fused-silica capillaries for increased capacity and versatility in LC-MS/MS applications. Proteomics 2008, 8(9):1758-1761.
    • (2008) Proteomics , vol.8 , Issue.9 , pp. 1758-1761
    • Wang, L.C.1    Okitsu, C.Y.2    Kochounian, H.3    Rodriguez, A.4    Hsieh, C.L.5    Zandi, E.6
  • 60
    • 0033571623 scopus 로고    scopus 로고
    • Molecular views of viral polyprotein processing revealed by the crystal structure of the hepatitis C virus bifunctional protease-helicase
    • Yao N., Reichert P., Taremi S.S., Prosise W.W., Weber P.C. Molecular views of viral polyprotein processing revealed by the crystal structure of the hepatitis C virus bifunctional protease-helicase. Structure 1999, 7(11):1353-1363.
    • (1999) Structure , vol.7 , Issue.11 , pp. 1353-1363
    • Yao, N.1    Reichert, P.2    Taremi, S.S.3    Prosise, W.W.4    Weber, P.C.5
  • 61
    • 79960401766 scopus 로고    scopus 로고
    • Hepatitis C virus co-opts Ras-GTPase-activating protein-binding protein 1 for its genome replication
    • Yi Z., Pan T., Wu X., Song W., Wang S., Xu Y., Rice C.M., Macdonald M.R., Yuan Z. Hepatitis C virus co-opts Ras-GTPase-activating protein-binding protein 1 for its genome replication. Journal of Virology 2011, 85:6996-7004.
    • (2011) Journal of Virology , vol.85 , pp. 6996-7004
    • Yi, Z.1    Pan, T.2    Wu, X.3    Song, W.4    Wang, S.5    Xu, Y.6    Rice, C.M.7    Macdonald, M.R.8    Yuan, Z.9
  • 62
    • 62549135687 scopus 로고    scopus 로고
    • Brome mosaic virus capsid protein regulates accumulation of viral replication proteins by binding to the replicase assembly RNA element
    • Yi G., Letteney E., Kim C.H., Kao C.C. Brome mosaic virus capsid protein regulates accumulation of viral replication proteins by binding to the replicase assembly RNA element. RNA-A Publication of the RNA Society 2009, 15(4):615-626.
    • (2009) RNA-A Publication of the RNA Society , vol.15 , Issue.4 , pp. 615-626
    • Yi, G.1    Letteney, E.2    Kim, C.H.3    Kao, C.C.4
  • 63
    • 67650700208 scopus 로고    scopus 로고
    • RNA binding by the Brome mosaic virus capsid protein and the regulation of viral RNA accumulation
    • Yi G., Vaughan R.C., Yarbrough I., Dharmaiah S., Kao C.C. RNA binding by the Brome mosaic virus capsid protein and the regulation of viral RNA accumulation. Journal of Molecular Biology 2009, 391(2):314-326.
    • (2009) Journal of Molecular Biology , vol.391 , Issue.2 , pp. 314-326
    • Yi, G.1    Vaughan, R.C.2    Yarbrough, I.3    Dharmaiah, S.4    Kao, C.C.5
  • 64
    • 33846111662 scopus 로고    scopus 로고
    • Compensatory mutations in E1, p7, NS2, and NS3 enhance yields of cell culture-infectious intergenotypic chimeric hepatitis C virus
    • Yi M., Ma Y., Yates J., Lemon S.M. Compensatory mutations in E1, p7, NS2, and NS3 enhance yields of cell culture-infectious intergenotypic chimeric hepatitis C virus. Journal of Virology 2007, 81(2):629-638.
    • (2007) Journal of Virology , vol.81 , Issue.2 , pp. 629-638
    • Yi, M.1    Ma, Y.2    Yates, J.3    Lemon, S.M.4
  • 65
    • 0037405787 scopus 로고    scopus 로고
    • Functional dissection of a poliovirus cis-acting replication element [PV-cre(2C)]: analysis of single- and dual-cre viral genomes and proteins that bind specifically to PV-cre RNA
    • Yin J., Paul A.V., Wimmer E., Rieder E. Functional dissection of a poliovirus cis-acting replication element [PV-cre(2C)]: analysis of single- and dual-cre viral genomes and proteins that bind specifically to PV-cre RNA. Journal of Virology 2003, 77(9):5152-5166.
    • (2003) Journal of Virology , vol.77 , Issue.9 , pp. 5152-5166
    • Yin, J.1    Paul, A.V.2    Wimmer, E.3    Rieder, E.4
  • 66
    • 21644463166 scopus 로고    scopus 로고
    • Stimulation of hepatitis C virus (HCV) nonstructural protein 3 (NS3) helicase activity by the NS3 protease domain and by HCV RNA-dependent RNA polymerase
    • Zhang C., Cai Z., Kim Y.C., Kumar R., Yuan F., Shi P.Y., Kao C., Luo G. Stimulation of hepatitis C virus (HCV) nonstructural protein 3 (NS3) helicase activity by the NS3 protease domain and by HCV RNA-dependent RNA polymerase. Journal of Virology 2005, 79(14):8687-8697.
    • (2005) Journal of Virology , vol.79 , Issue.14 , pp. 8687-8697
    • Zhang, C.1    Cai, Z.2    Kim, Y.C.3    Kumar, R.4    Yuan, F.5    Shi, P.Y.6    Kao, C.7    Luo, G.8
  • 67
    • 0042121256 scopus 로고    scopus 로고
    • Mfold web server for nucleic acid folding and hybridization prediction
    • Zuker M. Mfold web server for nucleic acid folding and hybridization prediction. Nucleic Acids Research 2003, 31(13):3406-3415.
    • (2003) Nucleic Acids Research , vol.31 , Issue.13 , pp. 3406-3415
    • Zuker, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.