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Volumn 78, Issue 14, 2004, Pages 7833-7838

Human coronavirus 229E nonstructural protein 13: Characterization of duplex-unwinding, nucleoside triphosphatase, and RNA 5′-triphosphatase activities

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; DEOXYADENOSINE TRIPHOSPHATE; GUANOSINE TRIPHOSPHATE; NONSTRUCTURAL PROTEIN 13; NUCLEOSIDE TRIPHOSPHATASE; RIBONUCLEOTIDE; UNCLASSIFIED DRUG; VIRUS PROTEIN; VIRUS RNA;

EID: 3142689813     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.78.14.7833-7838.2004     Document Type: Article
Times cited : (168)

References (54)
  • 1
    • 0031031958 scopus 로고    scopus 로고
    • Kinetic measurement of the step size of DNA unwinding by Escherichia coli UvrD helicase
    • Ali, J. A., and T. M. Lohman. 1997. Kinetic measurement of the step size of DNA unwinding by Escherichia coli UvrD helicase. Science 275:377-380.
    • (1997) Science , vol.275 , pp. 377-380
    • Ali, J.A.1    Lohman, T.M.2
  • 3
    • 0036374953 scopus 로고    scopus 로고
    • Functional properties of the predicted helicase of porcine reproductive and respiratory syndrome virus
    • Bautista, E. M., K. S. Faaberg, D. Mickelson, and E. D. McGruder. 2002. Functional properties of the predicted helicase of porcine reproductive and respiratory syndrome virus. Virology 298:258-270.
    • (2002) Virology , vol.298 , pp. 258-270
    • Bautista, E.M.1    Faaberg, K.S.2    Mickelson, D.3    McGruder, E.D.4
  • 4
    • 0030800967 scopus 로고    scopus 로고
    • Characterization of the nucleoside triphosphate phosphohydrolase and helicase activities of the reovirus lambda1 protein
    • Bisaillon, M., J. Bergeron, and G. Lemay. 1997. Characterization of the nucleoside triphosphate phosphohydrolase and helicase activities of the reovirus lambda1 protein. J. Biol. Chem. 272:18298-18303.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18298-18303
    • Bisaillon, M.1    Bergeron, J.2    Lemay, G.3
  • 5
    • 0035918981 scopus 로고    scopus 로고
    • Mouse hepatitis virus replicase protein complexes are translocated to sites of M protein accumulation in the ERGIC at late times of infection
    • Bost, A. G., E. Prentice, and M. R. Denison. 2001. Mouse hepatitis virus replicase protein complexes are translocated to sites of M protein accumulation in the ERGIC at late times of infection. Virology 285:21-29.
    • (2001) Virology , vol.285 , pp. 21-29
    • Bost, A.G.1    Prentice, E.2    Denison, M.R.3
  • 6
    • 0036880196 scopus 로고    scopus 로고
    • Helicase mechanisms and the coupling of helicases within macromolecular machines. Part I: Structures and properties of isolated helicases
    • Delagoutte, E., and P. H. von Hippel. 2002. Helicase mechanisms and the coupling of helicases within macromolecular machines. Part I: structures and properties of isolated helicases. Q. Rev. Biophys. 35:431-478.
    • (2002) Q. Rev. Biophys. , vol.35 , pp. 431-478
    • Delagoutte, E.1    Von Hippel, P.H.2
  • 7
    • 0034457382 scopus 로고    scopus 로고
    • Spectrum of clinical illness in hospitalized patients with "common cold" virus infections
    • El-Sahly, H. M., R. L. Atmar, W. P. Glezen, and S. B. Greenberg. 2000. Spectrum of clinical illness in hospitalized patients with "common cold" virus infections. Clin. Infect. Dis. 31:96-100.
    • (2000) Clin. Infect. Dis. , vol.31 , pp. 96-100
    • El-Sahly, H.M.1    Atmar, R.L.2    Glezen, W.P.3    Greenberg, S.B.4
  • 8
    • 0036569143 scopus 로고    scopus 로고
    • Rhinovirus and coronavirus infection-associated hospitalizations among older adults
    • Falsey, A. R., E. E. Walsb, and F. G. Hayden. 2002. Rhinovirus and coronavirus infection-associated hospitalizations among older adults. J. Infect. Dis. 185:1338-1341.
    • (2002) J. Infect. Dis. , vol.185 , pp. 1338-1341
    • Falsey, A.R.1    Walsb, E.E.2    Hayden, F.G.3
  • 9
    • 0036584349 scopus 로고    scopus 로고
    • Coronavirus-related nosocomial viral respiratory infections in a neonatal and paediatric intensive care unit: A prospective study
    • Gagneur, A., J. Sizun, S. Vallet, M. C. Legr, B. Picard, and P. J. Talbot. 2002. Coronavirus-related nosocomial viral respiratory infections in a neonatal and paediatric intensive care unit: a prospective study. J. Hosp. Infect. 51:59-64.
    • (2002) J. Hosp. Infect. , vol.51 , pp. 59-64
    • Gagneur, A.1    Sizun, J.2    Vallet, S.3    Legr, M.C.4    Picard, B.5    Talbot, P.J.6
  • 10
    • 0035701786 scopus 로고    scopus 로고
    • Big nidovirus genome. When count and order of domains matter
    • Gorbalenya, A. E. 2001. Big nidovirus genome. When count and order of domains matter. Adv. Exp. Med. Biol. 494:1-17.
    • (2001) Adv. Exp. Med. Biol. , vol.494 , pp. 1-17
    • Gorbalenya, A.E.1
  • 11
    • 0024398958 scopus 로고
    • Coronavirus genome: Prediction of putative functional domains in the non-structural polyprotein by comparative amino acid sequence analysis
    • Gorbalenya, A. E., E. V. Koonin, A. P. Donchenko, and V. M. Blinov. 1989. Coronavirus genome: prediction of putative functional domains in the non-structural polyprotein by comparative amino acid sequence analysis. Nucleic Acids Res. 17:4847-4861.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 4847-4861
    • Gorbalenya, A.E.1    Koonin, E.V.2    Donchenko, A.P.3    Blinov, V.M.4
  • 12
    • 0242673508 scopus 로고    scopus 로고
    • Characterization of a 105-kDa polypeptide encoded in gene 1 of the human coronavirus HCV 229E
    • Grötzinger, C., G. Heusipp, J. Ziebuhr, U. Harms, J. Süss, and S. G. Siddell. 1996. Characterization of a 105-kDa polypeptide encoded in gene 1 of the human coronavirus HCV 229E. Virology 222:227-235.
    • (1996) Virology , vol.222 , pp. 227-235
    • Grötzinger, C.1    Heusipp, G.2    Ziebuhr, J.3    Harms, U.4    Süss, J.5    Siddell, S.G.6
  • 13
    • 0036187709 scopus 로고    scopus 로고
    • Conservation of substrate specificities among coronavirus main proteases
    • Hegyi, A., and J. Ziebuhr. 2002. Conservation of substrate specificities among coronavirus main proteases. J. Gen. Virol. 83:595-599.
    • (2002) J. Gen. Virol. , vol.83 , pp. 595-599
    • Hegyi, A.1    Ziebuhr, J.2
  • 14
    • 0031907557 scopus 로고    scopus 로고
    • Proteolytic processing at the amino terminus of human coronavirus 229E gene 1-encoded polyproteins: Identification of a papain-like proteinase and its substrate
    • Herold, J., A. E. Gorbalenya, V. Thiel, B. Schelle, and S. G. Siddell. 1998. Proteolytic processing at the amino terminus of human coronavirus 229E gene 1-encoded polyproteins: identification of a papain-like proteinase and its substrate. J. Virol. 72:910-918.
    • (1998) J. Virol. , vol.72 , pp. 910-918
    • Herold, J.1    Gorbalenya, A.E.2    Thiel, V.3    Schelle, B.4    Siddell, S.G.5
  • 15
    • 0027313298 scopus 로고
    • Nucleotide sequence of the human coronavirus 229E RNA polymerase locus
    • Herold, J., T. Raabe, B. Schelle-Prinz, and S. G. Siddell. 1993. Nucleotide sequence of the human coronavirus 229E RNA polymerase locus. Virology 195:680-691.
    • (1993) Virology , vol.195 , pp. 680-691
    • Herold, J.1    Raabe, T.2    Schelle-Prinz, B.3    Siddell, S.G.4
  • 16
    • 0027722243 scopus 로고
    • An 'elaborated' pseudoknot is required for high frequency frameshifting during translation of HCV 229E polymerase mRNA
    • Herold, J., and S. G. Siddell. 1993. An 'elaborated' pseudoknot is required for high frequency frameshifting during translation of HCV 229E polymerase mRNA. Nucleic Acids Res. 21:5838-5842.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 5838-5842
    • Herold, J.1    Siddell, S.G.2
  • 17
    • 0033591345 scopus 로고    scopus 로고
    • 2+-binding finger connecting the two domains of a papain-like fold
    • 2+-binding finger connecting the two domains of a papain-like fold. J. Biol. Chem. 274:14918-14925.
    • (1999) J. Biol. Chem. , vol.274 , pp. 14918-14925
    • Herold, J.1    Siddell, S.G.2    Gorbalenya, A.E.3
  • 18
    • 1842370236 scopus 로고    scopus 로고
    • Identification and subcellular localization of a 41 kDa, polyprotein 1ab processing product in human coronavirus 229E-infected cells
    • Heusipp, G., C. Grötzinger, J. Herold, S. G. Siddell, and J. Ziebuhr. 1997. Identification and subcellular localization of a 41 kDa, polyprotein 1ab processing product in human coronavirus 229E-infected cells. J. Gen. Virol. 78:2789-2794.
    • (1997) J. Gen. Virol. , vol.78 , pp. 2789-2794
    • Heusipp, G.1    Grötzinger, C.2    Herold, J.3    Siddell, S.G.4    Ziebuhr, J.5
  • 19
    • 0030922564 scopus 로고    scopus 로고
    • Identification of an ATPase activity associated with a 71-kilodalton polypeptide encoded in gene 1 of the human coronavirus 229E
    • Heusipp, G., U. Harms, S. G. Siddell, and J. Ziebuhr. 1997. Identification of an ATPase activity associated with a 71-kilodalton polypeptide encoded in gene 1 of the human coronavirus 229E. J. Virol. 71:5631-5634.
    • (1997) J. Virol. , vol.71 , pp. 5631-5634
    • Heusipp, G.1    Harms, U.2    Siddell, S.G.3    Ziebuhr, J.4
  • 20
    • 0001395234 scopus 로고
    • Non-inverted versus inverted plots in enzyme kinetics
    • Hofstee, B. H., M. Dixon, and E. C. Webb. 1959. Non-inverted versus inverted plots in enzyme kinetics. Nature 184:1296-1298.
    • (1959) Nature , vol.184 , pp. 1296-1298
    • Hofstee, B.H.1    Dixon, M.2    Webb, E.C.3
  • 21
    • 2442679084 scopus 로고    scopus 로고
    • Multiple enzymatic activities associated with severe acute respiratory syndrome coronavirus helicase
    • Ivanov, K. A., V. Thiel, J. C. Dobbe, Y. van der Meer, E. J. Snijder, and J Ziebuhr. 2004. Multiple enzymatic activities associated with severe acute respiratory syndrome coronavirus helicase. J. Virol. 78:5619-5632.
    • (2004) J. Virol. , vol.78 , pp. 5619-5632
    • Ivanov, K.A.1    Thiel, V.2    Dobbe, J.C.3    Van Der Meer, Y.4    Snijder, E.J.5    Ziebuhr, J.6
  • 22
    • 0034719392 scopus 로고    scopus 로고
    • The DExH protein NPH-II is a processive and directional motor for unwinding RNA
    • Jankowsky, E., C. H. Gross, S. Shuman, and A. M. Pyle. 2000. The DExH protein NPH-II is a processive and directional motor for unwinding RNA. Nature 403:447-451.
    • (2000) Nature , vol.403 , pp. 447-451
    • Jankowsky, E.1    Gross, C.H.2    Shuman, S.3    Pyle, A.M.4
  • 23
    • 0036290319 scopus 로고    scopus 로고
    • RNA helicase activity of the plant virus movement proteins encoded by the first gene of the triple gene block
    • Kalinina, N. O., D. V. Rakitina, A. G. Solovyev, J. Schiemann, and S. Y. Morozov. 2002. RNA helicase activity of the plant virus movement proteins encoded by the first gene of the triple gene block. Virology 296:321-329.
    • (2002) Virology , vol.296 , pp. 321-329
    • Kalinina, N.O.1    Rakitina, D.V.2    Solovyev, A.G.3    Schiemann, J.4    Morozov, S.Y.5
  • 24
    • 0027504136 scopus 로고
    • Evolution and taxonomy of positive-strand RNA viruses: Implications of comparative analysis of amino acid sequences
    • Koonin, E. V., and V. V. Dolja. 1993. Evolution and taxonomy of positive-strand RNA viruses: implications of comparative analysis of amino acid sequences. Crit. Rev. Biochem. Mol. Biol. 28:375-430.
    • (1993) Crit. Rev. Biochem. Mol. Biol. , vol.28 , pp. 375-430
    • Koonin, E.V.1    Dolja, V.V.2
  • 25
    • 0030633479 scopus 로고    scopus 로고
    • The molecular biology of coronaviruses
    • Lai, M. M., and D. Cavanagh. 1997. The molecular biology of coronaviruses. Adv. Virus Res. 48:1-100.
    • (1997) Adv. Virus Res. , vol.48 , pp. 1-100
    • Lai, M.M.1    Cavanagh, D.2
  • 26
    • 0020024485 scopus 로고
    • Further characterization of mRNA's of mouse hepatitis virus: Presence of common 5′-end nucleotides
    • Lai, M. M., C. D. Patton, and S. A. Stohlman. 1982. Further characterization of mRNA's of mouse hepatitis virus: presence of common 5′-end nucleotides. J. Virol. 41:557-565.
    • (1982) J. Virol , vol.41 , pp. 557-565
    • Lai, M.M.1    Patton, C.D.2    Stohlman, S.A.3
  • 27
    • 0003208239 scopus 로고    scopus 로고
    • Coronaviridae: The viruses and their replication
    • D. M. Knipe and P. M. Howley (ed.). Lippincott Williams & Wilkins, Philadelphia, Pa
    • Lai, M. M. C., and K. V. Holmes. 2001. Coronaviridae: the viruses and their replication, p, 1163-1185. In D. M. Knipe and P. M. Howley (ed.), Fields virology, 4th ed., vol. 1. Lippincott Williams & Wilkins, Philadelphia, Pa.
    • (2001) Fields Virology, 4th Ed. , vol.1 , pp. 1163-1185
    • Lai, M.M.C.1    Holmes, K.V.2
  • 28
    • 0035198148 scopus 로고    scopus 로고
    • The helicase-like domain of plant potexvirus replicase participates in formation of RNA 5′ cap structure by exhibiting RNA 5′- triphosphatase activity
    • Li, Y. I., T. W. Shih, Y. H. Hsu, Y. T. Han, Y. L. Huang, and M. Meng. 2001. The helicase-like domain of plant potexvirus replicase participates in formation of RNA 5′ cap structure by exhibiting RNA 5′- triphosphatase activity. J. Virol. 75:12114-12120.
    • (2001) J. Virol. , vol.75 , pp. 12114-12120
    • Li, Y.I.1    Shih, T.W.2    Hsu, Y.H.3    Han, Y.T.4    Huang, Y.L.5    Meng, M.6
  • 29
    • 0029893874 scopus 로고    scopus 로고
    • Mechanisms of helicase-catalyzed DNA unwinding
    • Lohman, T. M., and K. P. Bjornson. 1996. Mechanisms of helicase-catalyzed DNA unwinding. Annu. Rev. Biochem. 65:169-214.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 169-214
    • Lohman, T.M.1    Bjornson, K.P.2
  • 30
    • 0002572397 scopus 로고
    • Human coronavirus infections
    • S. G. Siddell (ed.). Plenum Press, New York, N.Y.
    • Myint, S. H. 1995. Human coronavirus infections, p. 389-401. In S. G. Siddell (ed.), The Coronaviridae. Plenum Press, New York, N.Y.
    • (1995) The Coronaviridae , pp. 389-401
    • Myint, S.H.1
  • 31
    • 0036500976 scopus 로고    scopus 로고
    • The hepatitis C viral NS3 protein is a processive DNA helicase with cofactor enhanced RNA unwinding
    • Pang, P. S., E. Jankowsky, P. J. Planet, and A. M. Pyle. 2002. The hepatitis C viral NS3 protein is a processive DNA helicase with cofactor enhanced RNA unwinding. EMBO J. 21:1168-1176.
    • (2002) EMBO J. , vol.21 , pp. 1168-1176
    • Pang, P.S.1    Jankowsky, E.2    Planet, P.J.3    Pyle, A.M.4
  • 32
    • 0037126614 scopus 로고    scopus 로고
    • Sequence requirements for RNA strand transfer during nidovirus discontinuous subgenomic RNA synthesis
    • Pasternak, A. O., E. van den Born, W. J. Spaan, and E. J. Snijder. 2001. Sequence requirements for RNA strand transfer during nidovirus discontinuous subgenomic RNA synthesis. EMBO J. 20:7220-7228.
    • (2001) EMBO J. , vol.20 , pp. 7220-7228
    • Pasternak, A.O.1    Van Den Born, E.2    Spaan, W.J.3    Snijder, E.J.4
  • 33
    • 0025344888 scopus 로고
    • Nucleotide sequence of the gene encoding the spike glycoprotein of human coronavirus HCV 229E
    • Raabe, T., B. Schelle-Prinz, and S. G. Siddell. 1990. Nucleotide sequence of the gene encoding the spike glycoprotein of human coronavirus HCV 229E. J. Gen. Virol. 71:1065-1073.
    • (1990) J. Gen. Virol. , vol.71 , pp. 1065-1073
    • Raabe, T.1    Schelle-Prinz, B.2    Siddell, S.G.3
  • 34
    • 0025236253 scopus 로고
    • Coronavirus transcription: Subgenomic mouse hepatitis virus replicative intermediates function in RNA synthesis
    • Sawicki, S. G., and D. L. Sawicki. 1990. Coronavirus transcription: subgenomic mouse hepatitis virus replicative intermediates function in RNA synthesis. J. Virol. 64:1050-1056.
    • (1990) J. Virol. , vol.64 , pp. 1050-1056
    • Sawicki, S.G.1    Sawicki, D.L.2
  • 35
    • 0029444973 scopus 로고
    • Coronaviruses use discontinuous extension for synthesis of subgenome-length negative strands
    • Sawicki, S. G., and D. L. Sawicki. 1995. Coronaviruses use discontinuous extension for synthesis of subgenome-length negative strands. Adv. Exp. Med. Biol. 380:499-506.
    • (1995) Adv. Exp. Med. Biol. , vol.380 , pp. 499-506
    • Sawicki, S.G.1    Sawicki, D.L.2
  • 36
    • 0031783431 scopus 로고    scopus 로고
    • A new model for coronavirus transcription
    • Sawicki, S. G., and D. L. Sawicki. 1998. A new model for coronavirus transcription. Adv. Exp. Med. Biol. 440:215-219.
    • (1998) Adv. Exp. Med. Biol. , vol.440 , pp. 215-219
    • Sawicki, S.G.1    Sawicki, D.L.2
  • 37
    • 0033941814 scopus 로고    scopus 로고
    • The human coronavirus 229E superfamily 1 helicase has RNA and DNA duplex-unwinding activities with 5′-to-3′ polarity
    • Seybert, A., A. Hegyi, S. G. Siddell, and J. Ziebuhr. 2000. The human coronavirus 229E superfamily 1 helicase has RNA and DNA duplex-unwinding activities with 5′-to-3′ polarity. RNA 6:1056-1068.
    • (2000) RNA , vol.6 , pp. 1056-1068
    • Seybert, A.1    Hegyi, A.2    Siddell, S.G.3    Ziebuhr, J.4
  • 38
    • 0033818909 scopus 로고    scopus 로고
    • Biochemical characterization of the equine arteritis virus helicase suggests a close functional relationship between arterivirus and coronavirus helicases
    • Seybert, A., L. C. van Dinten, E. J. Snijder, and J. Ziebuhr. 2000. Biochemical characterization of the equine arteritis virus helicase suggests a close functional relationship between arterivirus and coronavirus helicases. J. Virol. 74:9586-9593.
    • (2000) J. Virol. , vol.74 , pp. 9586-9593
    • Seybert, A.1    Van Dinten, L.C.2    Snijder, E.J.3    Ziebuhr, J.4
  • 39
    • 0035703706 scopus 로고    scopus 로고
    • Guanosine triphosphatase activity of the human coronavirus helicase
    • Seybert, A., and J. Ziebuhr. 2001. Guanosine triphosphatase activity of the human coronavirus helicase. Adv. Exp. Med. Biol. 494:255-260.
    • (2001) Adv. Exp. Med. Biol. , vol.494 , pp. 255-260
    • Seybert, A.1    Ziebuhr, J.2
  • 41
    • 0141960168 scopus 로고    scopus 로고
    • The severe acute respiratory syndrome (SARS) coronavirus NTPase/helicase belongs to a distinct class of 5′ to 3′ viral helicases
    • Tanner, J. A., R. M. Watt, Y. B. Chai, L. Y. Lu, M. C. Lin, J. S. Peiris, L. L Poon, H. F. Kung, and J. D. Huang. 2003. The severe acute respiratory syndrome (SARS) coronavirus NTPase/helicase belongs to a distinct class of 5′ to 3′ viral helicases. J. Biol. Chem. 278:39578-39582.
    • (2003) J. Biol. Chem. , vol.278 , pp. 39578-39582
    • Tanner, J.A.1    Watt, R.M.2    Chai, Y.B.3    Lu, L.Y.4    Lin, M.C.5    Peiris, J.S.6    Poon, L.L.7    Kung, H.F.8    Huang, J.D.9
  • 43
    • 0032816239 scopus 로고    scopus 로고
    • Localization of mouse hepatitis virus nonstructural proteins and RNA synthesis indicates a role for late endosomes in viral replication
    • van der Meer, Y., E. J. Snijder, J. C. Dobbe, S. Schleich, M. R. Denison, W. J. Spaan, and J. Krijnse Locker. 1999. Localization of mouse hepatitis virus nonstructural proteins and RNA synthesis indicates a role for late endosomes in viral replication. J. Virol. 73:7641-7657.
    • (1999) J. Virol. , vol.73 , pp. 7641-7657
    • Van Der Meer, Y.1    Snijder, E.J.2    Dobbe, J.C.3    Schleich, S.4    Denison, M.R.5    Spaan, W.J.6    Krijnse Locker, J.7
  • 44
    • 0034105481 scopus 로고    scopus 로고
    • The predicted metal-binding region of the arterivirus helicase protein is involved in subgenomic mRNA synthesis, genome replication, and virion biogenesis
    • van Dinten, L. C., H. van Tol, A. E. Gorbalenya, and E. J. Snijder. 2000. The predicted metal-binding region of the arterivirus helicase protein is involved in subgenomic mRNA synthesis, genome replication, and virion biogenesis. J. Virol. 74:5213-5223.
    • (2000) J. Virol. , vol.74 , pp. 5213-5223
    • Van Dinten, L.C.1    Van Tol, H.2    Gorbalenya, A.E.3    Snijder, E.J.4
  • 45
    • 0034625437 scopus 로고    scopus 로고
    • Identification of a novel function of the alphavirus capping apparatus. RNA 5′-triphosphatase activity of Nsp2
    • Vasiljeva, L., A. Merits, P. Auvinen, and L. Kääriäinen. 2000. Identification of a novel function of the alphavirus capping apparatus. RNA 5′-triphosphatase activity of Nsp2. J. Biol. Chem. 275:17281-17287.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17281-17287
    • Vasiljeva, L.1    Merits, A.2    Auvinen, P.3    Kääriäinen, L.4
  • 46
    • 0035951425 scopus 로고    scopus 로고
    • A general model for nucleic acid helicases and their "coupling" within macromolecular machines
    • von Hippel, P. H., and E. Delagoutte. 2001. A general model for nucleic acid helicases and their "coupling" within macromolecular machines. Cell 104:177-190.
    • (2001) Cell , vol.104 , pp. 177-190
    • Von Hippel, P.H.1    Delagoutte, E.2
  • 47
    • 0027366948 scopus 로고
    • The NS 3 nonstructural protein of flaviviruses contains an RNA triphosphatase activity
    • Wengler, G. 1993. The NS 3 nonstructural protein of flaviviruses contains an RNA triphosphatase activity. Virology 197:265-273.
    • (1993) Virology , vol.197 , pp. 265-273
    • Wengler, G.1
  • 49
    • 0029017145 scopus 로고
    • Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity
    • Ziebuhr, J., J. Herold, and S. G. Siddell. 1995. Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity. J. Virol. 69:4331-4338.
    • (1995) J. Virol. , vol.69 , pp. 4331-4338
    • Ziebuhr, J.1    Herold, J.2    Siddell, S.G.3
  • 50
    • 0030970783 scopus 로고    scopus 로고
    • Biosynthesis, purification, and characterization of the human coronavirus 229E 3C-like proteinase
    • Ziebuhr, J., G. Heusipp, and S. G. Siddell. 1997. Biosynthesis, purification, and characterization of the human coronavirus 229E 3C-like proteinase. J. Virol. 71:3992-3997.
    • (1997) J. Virol. , vol.71 , pp. 3992-3997
    • Ziebuhr, J.1    Heusipp, G.2    Siddell, S.G.3
  • 51
    • 0032888958 scopus 로고    scopus 로고
    • Processing of the human coronavirus 229E replicase polyproteins by the virus-encoded 3C-like proteinase: Identification of proteolytic products and cleavage sites common to pp1a and pp1ab
    • Ziebuhr, J., and S. G. Siddell. 1999. Processing of the human coronavirus 229E replicase polyproteins by the virus-encoded 3C-like proteinase: identification of proteolytic products and cleavage sites common to pp1a and pp1ab. J. Virol. 73:177-185.
    • (1999) J. Virol. , vol.73 , pp. 177-185
    • Ziebuhr, J.1    Siddell, S.G.2
  • 52
    • 0034072633 scopus 로고    scopus 로고
    • Virus-encoded proteinases and proteolytic processing in the Nidovirales
    • Ziebuhr, J., E. J. Snijder, and A. E. Gorbalenya. 2000. Virus-encoded proteinases and proteolytic processing in the Nidovirales. J. Gen. Virol. 81:853-879.
    • (2000) J. Gen. Virol. , vol.81 , pp. 853-879
    • Ziebuhr, J.1    Snijder, E.J.2    Gorbalenya, A.E.3
  • 53
    • 0035980126 scopus 로고    scopus 로고
    • The autocatalytic release of a putative RNA virus transcription factor from its polyprotein precursor involves two paralogous papain-like proteases that cleave the same peptide bond
    • Ziebuhr, J., V. Thiel, and A. E. Gorbalenya. 2001. The autocatalytic release of a putative RNA virus transcription factor from its polyprotein precursor involves two paralogous papain-like proteases that cleave the same peptide bond. J. Biol. Chem. 276:33220-33232.
    • (2001) J. Biol. Chem. , vol.276 , pp. 33220-33232
    • Ziebuhr, J.1    Thiel, V.2    Gorbalenya, A.E.3
  • 54
    • 0347319103 scopus 로고    scopus 로고
    • Sequence motifs involved in the regulation of discontinuous coronavirus subgenomic RNA synthesis
    • Zúñiga, S., I. Sola, S. Alonso, and L. Enjuanes. 2004. Sequence motifs involved in the regulation of discontinuous coronavirus subgenomic RNA synthesis. J. Virol. 78:980-994.
    • (2004) J. Virol. , vol.78 , pp. 980-994
    • Zúñiga, S.1    Sola, I.2    Alonso, S.3    Enjuanes, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.