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Volumn 10, Issue 8, 2004, Pages 1277-1290

Isolation of specific and high-affinity RNA aptamers against NS3 helicase domain of hepatitis C virus

Author keywords

HCV; HCV replicon; Intracellular protein detection; NS3 helicase; RNA aptamer; SELEX

Indexed keywords

APTAMER; HELICASE; STRUCTURAL PROTEIN;

EID: 3342877385     PISSN: 13558382     EISSN: None     Source Type: Journal    
DOI: 10.1261/rna.7100904     Document Type: Article
Times cited : (59)

References (56)
  • 1
    • 0042353719 scopus 로고    scopus 로고
    • Abrogation of hepatitis C virus NS3 helicase enzymatic activity by recombinant human antibodies
    • Artsaenko, O., Tessmann, K., Sack, M., Haussinger, D., and Heintges, T. 2003. Abrogation of hepatitis C virus NS3 helicase enzymatic activity by recombinant human antibodies. J. Gen. Virol. 84: 2323-2332.
    • (2003) J. Gen. Virol. , vol.84 , pp. 2323-2332
    • Artsaenko, O.1    Tessmann, K.2    Sack, M.3    Haussinger, D.4    Heintges, T.5
  • 3
    • 0035138086 scopus 로고    scopus 로고
    • Specific interaction of hepatitis C virus protease/helicase NS3 with the 3′-terminal sequences of viral positive- and negative-strand RNA
    • Banerjee, R. and Dasgupta, A. 2001. Specific interaction of hepatitis C virus protease/helicase NS3 with the 3′-terminal sequences of viral positive- and negative-strand RNA. J. Virol. 75: 1708-1721.
    • (2001) J. Virol. , vol.75 , pp. 1708-1721
    • Banerjee, R.1    Dasgupta, A.2
  • 4
    • 0027287798 scopus 로고
    • Nonstructural protein 3 of the hepatitis C virus encodes a serine-type proteinase required for cleavage at the NS3/4 and NS4/5 junctions
    • Bartenschlager, R., Ahlborn-Laake, L., Mous, J., and Jacobsen, H. 1993. Nonstructural protein 3 of the hepatitis C virus encodes a serine-type proteinase required for cleavage at the NS3/4 and NS4/5 junctions. J. Virol. 67: 3835-3844.
    • (1993) J. Virol. , vol.67 , pp. 3835-3844
    • Bartenschlager, R.1    Ahlborn-Laake, L.2    Mous, J.3    Jacobsen, H.4
  • 5
    • 0036200412 scopus 로고    scopus 로고
    • Selection of RNA aptamers that are specific and high-affinity ligands of the hepatitis C virus RNA-dependent RNA polymerase
    • Biroccio, A., Hamm, J., Incitti, I., De Francesco, R., and Tomei, L. 2002. Selection of RNA aptamers that are specific and high-affinity ligands of the hepatitis C virus RNA-dependent RNA polymerase. J. Virol. 76: 3688-3696.
    • (2002) J. Virol. , vol.76 , pp. 3688-3696
    • Biroccio, A.1    Hamm, J.2    Incitti, I.3    De Francesco, R.4    Tomei, L.5
  • 6
    • 0038747996 scopus 로고    scopus 로고
    • Halogenated benzimidazoles and benzotriazoles as inhibitors of the NTPase/helicase activities of hepatitis C and related viruses
    • Borowski, P., Deinert, J., Schalinski, S., Bretner, M., Ginalski, K., Kulikowski, T., and Shugar, D. 2003. Halogenated benzimidazoles and benzotriazoles as inhibitors of the NTPase/helicase activities of hepatitis C and related viruses. Eur. J. Biochem. 270: 1645-1653.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 1645-1653
    • Borowski, P.1    Deinert, J.2    Schalinski, S.3    Bretner, M.4    Ginalski, K.5    Kulikowski, T.6    Shugar, D.7
  • 7
    • 0037114941 scopus 로고    scopus 로고
    • Aptamers as tools for target prioritization and lead identification
    • Burgstaller, P., Girod, A., and Blind, M. 2002. Aptamers as tools for target prioritization and lead identification. Drug Discov. Today 7: 1221-1228.
    • (2002) Drug Discov. Today , vol.7 , pp. 1221-1228
    • Burgstaller, P.1    Girod, A.2    Blind, M.3
  • 10
    • 0033992657 scopus 로고    scopus 로고
    • Structure and function of the hepatitis C virus NS3-NS4A serine protease
    • De Francesco, R. and Steinkühler, C. 2000. Structure and function of the hepatitis C virus NS3-NS4A serine protease. Curr. Top. Microbiol. Immunol. 242: 149-169.
    • (2000) Curr. Top. Microbiol. Immunol. , vol.242 , pp. 149-169
    • De Francesco, R.1    Steinkühler, C.2
  • 11
    • 0025074907 scopus 로고
    • In vitro selection of RNA molecules that bind specific ligands
    • Ellington, A.D. and Szostak, J.W. 1990. In vitro selection of RNA molecules that bind specific ligands. Nature 346: 818-822.
    • (1990) Nature , vol.346 , pp. 818-822
    • Ellington, A.D.1    Szostak, J.W.2
  • 12
    • 0020491096 scopus 로고
    • Co-existence of vinculin and a vinculin-like protein of higher molecular weight in smooth muscle
    • Feramisco, J.R., Smart, J.E., Burridge, K., Helfman, D.M., and Thomas, G.P. 1982. Co-existence of vinculin and a vinculin-like protein of higher molecular weight in smooth muscle. J. Biol. Chem. 257: 11024-11031.
    • (1982) J. Biol. Chem. , vol.257 , pp. 11024-11031
    • Feramisco, J.R.1    Smart, J.E.2    Burridge, K.3    Helfman, D.M.4    Thomas, G.P.5
  • 14
    • 0003103710 scopus 로고
    • RNA: The shape of things to come
    • (eds. R.F. Gestelend and J.F. Atkins). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Gold, L., Allen, P., Binkley, J., Brown, D., Schneider, D., Eddy, S.R., Tuerk, C., Green, L., Macdougal, S., and Tasset, D. 1993. RNA: the shape of things to come. In The RNA World (eds. R.F. Gestelend and J.F. Atkins), pp. 497-510, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1993) The RNA World , pp. 497-510
    • Gold, L.1    Allen, P.2    Binkley, J.3    Brown, D.4    Schneider, D.5    Eddy, S.R.6    Tuerk, C.7    Green, L.8    Macdougal, S.9    Tasset, D.10
  • 15
    • 0027414062 scopus 로고
    • Characterization of the hepatitis C virus-encoded serine proteinase: Determination of proteinase-dependent polyprotein cleavage sites
    • Grakoui, A., McCourt, D.W., Wychowski, C., Feinstone, S.M., and Rice, C.M. 1993. Characterization of the hepatitis C virus-encoded serine proteinase: determination of proteinase-dependent polyprotein cleavage sites. J. Virol. 67: 2832-2843.
    • (1993) J. Virol. , vol.67 , pp. 2832-2843
    • Grakoui, A.1    McCourt, D.W.2    Wychowski, C.3    Feinstone, S.M.4    Rice, C.M.5
  • 16
    • 0030583249 scopus 로고    scopus 로고
    • Characterization of RNA binding activity and RNA helicase activity of the hepatitis C virus NS3 protein
    • Gwack, Y., Kim, D.W., Han, J.H., and Choe, J. 1996. Characterization of RNA binding activity and RNA helicase activity of the hepatitis C virus NS3 protein. Biochem. Biophys. Res. Comm. 225: 654-659.
    • (1996) Biochem. Biophys. Res. Comm. , vol.225 , pp. 654-659
    • Gwack, Y.1    Kim, D.W.2    Han, J.H.3    Choe, J.4
  • 17
    • 0027163740 scopus 로고
    • Two distinct proteinase activities required for the processing of a putative nonstructural precursor protein of hepatitis C virus
    • Hijikata, M., Mizushima, H., Akagi, T., Mori, S., Kakiuchi, N., Kato, N., Tanaka, T., Kimura, K., and Shimotohno, K. 1993. Two distinct proteinase activities required for the processing of a putative nonstructural precursor protein of hepatitis C virus. J. Virol. 67: 4665-4675.
    • (1993) J. Virol. , vol.67 , pp. 4665-4675
    • Hijikata, M.1    Mizushima, H.2    Akagi, T.3    Mori, S.4    Kakiuchi, N.5    Kato, N.6    Tanaka, T.7    Kimura, K.8    Shimotohno, K.9
  • 18
    • 0042737486 scopus 로고    scopus 로고
    • Prevention of passively transferred experimental autoimmune myasthenia gravis by an in vitro selected RNA aptamer
    • Hwang, B., Han, K., and Lee, S.-W. 2003. Prevention of passively transferred experimental autoimmune myasthenia gravis by an in vitro selected RNA aptamer. FEBS Lett. 548: 85-89.
    • (2003) FEBS Lett. , vol.548 , pp. 85-89
    • Hwang, B.1    Han, K.2    Lee, S.-W.3
  • 19
    • 0345005029 scopus 로고
    • Improved predictions of secondary structures for RNA
    • Jaeger, J., Turner, D., and Zuker, M. 1989. Improved predictions of secondary structures for RNA. Proc. Natl. Acad. Sci. 86: 7706-7710.
    • (1989) Proc. Natl. Acad. Sci. , vol.86 , pp. 7706-7710
    • Jaeger, J.1    Turner, D.2    Zuker, M.3
  • 20
    • 0028800155 scopus 로고
    • Poly(U) binding activity of hepatitis C virus NS3 protein, a putative RNA helicase
    • Kanai, A., Tanabe, K., and Kohara, M. 1995. Poly(U) binding activity of hepatitis C virus NS3 protein, a putative RNA helicase. FEBS Lett. 376: 221-224.
    • (1995) FEBS Lett. , vol.376 , pp. 221-224
    • Kanai, A.1    Tanabe, K.2    Kohara, M.3
  • 21
    • 0034749457 scopus 로고    scopus 로고
    • Mutations that affect dimer formation and helicase activity of the hepatitis C virus helicase
    • Khu, Y.-L., Koh, E., Lim, S.P., Tan, Y.H., Brenner, S., Lim, S.G., Hong, W.J., and Goh, P.-Y. 2001. Mutations that affect dimer formation and helicase activity of the hepatitis C virus helicase. J. Virol. 75: 205-214.
    • (2001) J. Virol. , vol.75 , pp. 205-214
    • Khu, Y.-L.1    Koh, E.2    Lim, S.P.3    Tan, Y.H.4    Brenner, S.5    Lim, S.G.6    Hong, W.J.7    Goh, P.-Y.8
  • 22
    • 0028817781 scopus 로고
    • C-terminal domain of the hepatitis C virus NS3 protein contains an RNA helicase activity
    • Kim, D.W., Gwak, Y., Han, J.H., and Choe, J. 1995. C-terminal domain of the hepatitis C virus NS3 protein contains an RNA helicase activity. Biochem. Biophys. Res. Comm. 215: 160-166.
    • (1995) Biochem. Biophys. Res. Comm. , vol.215 , pp. 160-166
    • Kim, D.W.1    Gwak, Y.2    Han, J.H.3    Choe, J.4
  • 23
    • 0013627747 scopus 로고    scopus 로고
    • Mutational analysis of the hepatitis C virus RNA helicase
    • Kim, D.W., Kim, J., Gwack, Y., Han, J.H., and Choe, J. 1997. Mutational analysis of the hepatitis C virus RNA helicase. J. Virol. 71: 9400-9409.
    • (1997) J. Virol. , vol.71 , pp. 9400-9409
    • Kim, D.W.1    Kim, J.2    Gwack, Y.3    Han, J.H.4    Choe, J.5
  • 24
    • 0032518490 scopus 로고    scopus 로고
    • Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: The crystal structure provides insights into the mode of unwinding
    • Kim, J.L., Morgenstern, K.A., Griffith, J.P., Dwyer, M.D., Thomson, J.A., Murcko, M.A., Lin, C., and Caron, P.R. 1998. Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding. Structure 6: 89-100.
    • (1998) Structure , vol.6 , pp. 89-100
    • Kim, J.L.1    Morgenstern, K.A.2    Griffith, J.P.3    Dwyer, M.D.4    Thomson, J.A.5    Murcko, M.A.6    Lin, C.7    Caron, P.R.8
  • 25
    • 0037213894 scopus 로고    scopus 로고
    • Structurally conserved amino acid W5011 is required for RNA helicase activity but is not essential for DNA helicase activity of hepatitis C virus NS3 protein
    • Kim, J.W., Seo, M.Y., Shelat, A., Kim, C.S., Kwon, T.W., Lu, H.-h., Moustakas, D.T., Sun, J., and Han, J.H. 2003. Structurally conserved amino acid W5011 is required for RNA helicase activity but is not essential for DNA helicase activity of hepatitis C virus NS3 protein. J. Virol. 77: 571-582.
    • (2003) J. Virol. , vol.77 , pp. 571-582
    • Kim, J.W.1    Seo, M.Y.2    Shelat, A.3    Kim, C.S.4    Kwon, T.W.5    Lu, H.-H.6    Moustakas, D.T.7    Sun, J.8    Han, J.H.9
  • 26
    • 0035032237 scopus 로고    scopus 로고
    • Enhancement of hepatitis C virus RNA replication by cell culture-adative mutations
    • Krieger, N., Lohmann, V., and Bartenschlager, R. 2001. Enhancement of hepatitis C virus RNA replication by cell culture-adative mutations. J. Virol. 75: 4614-4624.
    • (2001) J. Virol. , vol.75 , pp. 4614-4624
    • Krieger, N.1    Lohmann, V.2    Bartenschlager, R.3
  • 27
  • 28
    • 0033992576 scopus 로고    scopus 로고
    • Structure and function of hepatitis C virus NS3 helicase
    • Kwong, A.D., Kim, J.L., and Lin, C. 2000. Structure and function of hepatitis C virus NS3 helicase. Curr. Top. Microbiol. Immunol. 242: 171-196.
    • (2000) Curr. Top. Microbiol. Immunol. , vol.242 , pp. 171-196
    • Kwong, A.D.1    Kim, J.L.2    Lin, C.3
  • 29
  • 30
    • 0029788208 scopus 로고    scopus 로고
    • Isolation of a nuclease resistant decoy RNA that selectively blocks autoantibody binding to insulin receptors on human lymphocytes
    • Lee, S.-W. and Sullenger, B. 1996. Isolation of a nuclease resistant decoy RNA that selectively blocks autoantibody binding to insulin receptors on human lymphocytes. J. Exp. Med. 194: 315-324.
    • (1996) J. Exp. Med. , vol.194 , pp. 315-324
    • Lee, S.-W.1    Sullenger, B.2
  • 31
    • 0031031521 scopus 로고    scopus 로고
    • Isolation of a nuclease-resistant decoy RNA that can protect human acetylcholine receptors from myasthenic antibodies
    • -. 1997. Isolation of a nuclease-resistant decoy RNA that can protect human acetylcholine receptors from myasthenic antibodies. Nature Biotechnol. 15: 41-45.
    • (1997) Nature Biotechnol , vol.15 , pp. 41-45
  • 32
    • 0028290389 scopus 로고
    • Processing in the hepatitis C virus E2-NS2 region: Identification of p7 and two distinct E2-specific products with different C termini
    • Lin, C., Lindenbach, B.D., Pragai, B.M., McCourt, D.W., and Rice, C.M. 1994. Processing in the hepatitis C virus E2-NS2 region: Identification of p7 and two distinct E2-specific products with different C termini. J. Virol. 68: 5063-5073.
    • (1994) J. Virol. , vol.68 , pp. 5063-5073
    • Lin, C.1    Lindenbach, B.D.2    Pragai, B.M.3    McCourt, D.W.4    Rice, C.M.5
  • 33
    • 0035976707 scopus 로고    scopus 로고
    • Solution structure and backbone dynamics of an engineered arginine-rich subdomain 2 of the hepatitis C virus NS3 RNA helicase
    • Liu, D., Wang, Y.S., Gesell, J.J., and Wyss, D.F. 2001. Solution structure and backbone dynamics of an engineered arginine-rich subdomain 2 of the hepatitis C virus NS3 RNA helicase. J. Mol. Biol. 314: 543-561.
    • (2001) J. Mol. Biol. , vol.314 , pp. 543-561
    • Liu, D.1    Wang, Y.S.2    Gesell, J.J.3    Wyss, D.F.4
  • 34
  • 36
    • 0028265186 scopus 로고
    • Analysis of N-terminal processing of hepatitis C virus nonstructural protein 2
    • Mizushima, H., Hijikata, M., Tanji, Y., Kimura, K., and Shimotohno, K. 1994. Analysis of N-terminal processing of hepatitis C virus nonstructural protein 2. J. Virol. 68: 2731-2734.
    • (1994) J. Virol. , vol.68 , pp. 2731-2734
    • Mizushima, H.1    Hijikata, M.2    Tanji, Y.3    Kimura, K.4    Shimotohno, K.5
  • 41
    • 0029784485 scopus 로고    scopus 로고
    • A steady-state and pre-steady-state kinetic analysis of the NTPase activity associated with the hepatitis C virus NS3 helicase domain
    • Preugschat, F., Averett, D.R., Clark, B.E., and Porter, D.J.T. 1996. A steady-state and pre-steady-state kinetic analysis of the NTPase activity associated with the hepatitis C virus NS3 helicase domain. J. Biol. Chem. 271: 24449-24457.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24449-24457
    • Preugschat, F.1    Averett, D.R.2    Clark, B.E.3    Porter, D.J.T.4
  • 42
    • 0028817281 scopus 로고
    • Nonradioactive 3′-end-labeling of RNA molecules of different lengths by terminal deoxynucleotidyltransferase
    • Rosemeyer, V., Laubrock, A., and Seibl, R. 1995. Nonradioactive 3′-end-labeling of RNA molecules of different lengths by terminal deoxynucleotidyltransferase. Anal. Biochem. 224: 446-449.
    • (1995) Anal. Biochem. , vol.224 , pp. 446-449
    • Rosemeyer, V.1    Laubrock, A.2    Seibl, R.3
  • 44
    • 0029076837 scopus 로고
    • The N-terminal region of hepatitis C virus nonstructural protein 3 (NS3) is essential for stable complex formation with NS4A
    • Satoh, S., Tanji, Y., Hijikata, M., Kimura, K., and Shimotohno, K. 1995. The N-terminal region of hepatitis C virus nonstructural protein 3 (NS3) is essential for stable complex formation with NS4A. J. Virol. 69: 4255-4260.
    • (1995) J. Virol. , vol.69 , pp. 4255-4260
    • Satoh, S.1    Tanji, Y.2    Hijikata, M.3    Kimura, K.4    Shimotohno, K.5
  • 46
    • 0037062920 scopus 로고    scopus 로고
    • Emerging clinical applications of RNA
    • Sullenger, B.A. and Gilboa, E. 2002. Emerging clinical applications of RNA. Nature 418: 252-258.
    • (2002) Nature , vol.418 , pp. 252-258
    • Sullenger, B.A.1    Gilboa, E.2
  • 47
    • 0027199917 scopus 로고
    • Hepatitis C virus NS3 protein polynucleotide-stimulated nucleoside triphosphatase and comparison with the related pestivirus and flavivirus enzymes
    • Suzich, J.A., Tamura, J.K., Palmer-Hill, F., Warrener, P., Grakoui, A., Rice, C.M., Feinstone, S.M., and Collett, M.S. 1993. Hepatitis C virus NS3 protein polynucleotide-stimulated nucleoside triphosphatase and comparison with the related pestivirus and flavivirus enzymes. J. Virol. 67: 6152-6158.
    • (1993) J. Virol. , vol.67 , pp. 6152-6158
    • Suzich, J.A.1    Tamura, J.K.2    Palmer-Hill, F.3    Warrener, P.4    Grakoui, A.5    Rice, C.M.6    Feinstone, S.M.7    Collett, M.S.8
  • 48
    • 0029970903 scopus 로고    scopus 로고
    • The helicase activity associated with hepatitis C virus nonstructural protein 3 (NS3)
    • Tai, C.-L., Chi, W.-K., Chen, D.-S., and Hwang, L.-H. 1996. The helicase activity associated with hepatitis C virus nonstructural protein 3 (NS3). J. Virol. 70: 8477-8484.
    • (1996) J. Virol. , vol.70 , pp. 8477-8484
    • Tai, C.-L.1    Chi, W.-K.2    Chen, D.-S.3    Hwang, L.-H.4
  • 50
    • 0027176287 scopus 로고
    • NS3 is a serine protease required for processing of hepatitis C virus polyprotein
    • Tomei, L., Failla, C., Santolini, E., DeFrancesco, R., and LaMonica, N. 1993. NS3 is a serine protease required for processing of hepatitis C virus polyprotein. J. Virol. 67: 4017-4026.
    • (1993) J. Virol. , vol.67 , pp. 4017-4026
    • Tomei, L.1    Failla, C.2    Santolini, E.3    DeFrancesco, R.4    LaMonica, N.5
  • 51
    • 0025194307 scopus 로고
    • Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase
    • Tuerk, C. and Gold, L. 1990. Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase. Science 249: 505-510.
    • (1990) Science , vol.249 , pp. 505-510
    • Tuerk, C.1    Gold, L.2
  • 53
    • 0037444390 scopus 로고    scopus 로고
    • Identification of RNA ligands that bind hepatitis C virus polymerase selectively and inhibit its RNA synthesis from the natural viral RNA templates
    • Vo, N.V., Oh, J.W., and Lai, M.M. 2003. Identification of RNA ligands that bind hepatitis C virus polymerase selectively and inhibit its RNA synthesis from the natural viral RNA templates. Virology 307: 301-316.
    • (2003) Virology , vol.307 , pp. 301-316
    • Vo, N.V.1    Oh, J.W.2    Lai, M.M.3
  • 54
    • 0033030027 scopus 로고    scopus 로고
    • Characterization and mutational analysis of the helicase and NTPase activities of hepatitis C virus full-length NS3 protein
    • Wardell, A.D., Errington, W., Ciaramella, G., Merson, J., and McGarvey, M.J. 1999. Characterization and mutational analysis of the helicase and NTPase activities of hepatitis C virus full-length NS3 protein. J. Gen. Virol. 80: 701-709.
    • (1999) J. Gen. Virol. , vol.80 , pp. 701-709
    • Wardell, A.D.1    Errington, W.2    Ciaramella, G.3    Merson, J.4    McGarvey, M.J.5
  • 55
    • 0343384412 scopus 로고    scopus 로고
    • Internal cleavage of hepatitis C virus NS3 protein is dependent on the activity of NS34A protease
    • Yang, S.H., Lee, C.G., Song, M.K., and Sung, Y.C. 2000. Internal cleavage of hepatitis C virus NS3 protein is dependent on the activity of NS34A protease. Virology 268: 132-140.
    • (2000) Virology , vol.268 , pp. 132-140
    • Yang, S.H.1    Lee, C.G.2    Song, M.K.3    Sung, Y.C.4


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