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Volumn 6, Issue 7, 2000, Pages 1056-1068

The human coronavirus 229E superfamily 1 helicase has RNA and DNA duplex-unwinding activities with 5'-to-3' polarity

Author keywords

5' to 3' polarity; Helicase; Nucleoside triphosphatase; Superfamily 1

Indexed keywords

ADENOSINE TRIPHOSPHATASE; DOUBLE STRANDED DNA; DOUBLE STRANDED RNA; HELICASE; ZINC FINGER PROTEIN;

EID: 0033941814     PISSN: 13558382     EISSN: None     Source Type: Journal    
DOI: 10.1017/S1355838200000728     Document Type: Article
Times cited : (119)

References (70)
  • 1
    • 0032489041 scopus 로고    scopus 로고
    • Polymerases and the replisome: Machines with machines
    • Baker TA, Bell SP. 1998. Polymerases and the replisome: Machines with machines. Cell 92:295-305.
    • (1998) Cell , vol.92 , pp. 295-305
    • Baker, T.A.1    Bell, S.P.2
  • 2
    • 0030050010 scopus 로고    scopus 로고
    • Vaccinia virion protein I8R has both DNA and RNA helicase activities: Implications for vaccinia virus transcription
    • Bayliss CD, Smith GL. 1996. Vaccinia virion protein I8R has both DNA and RNA helicase activities: Implications for vaccinia virus transcription. J Virol 70:794-800.
    • (1996) J Virol , vol.70 , pp. 794-800
    • Bayliss, C.D.1    Smith, G.L.2
  • 4
    • 0030332528 scopus 로고    scopus 로고
    • Comparison of the replication of positive-stranded RNA viruses of plants and animals
    • Buck KW. 1996. Comparison of the replication of positive-stranded RNA viruses of plants and animals. Adv Virus Res 47:159-251.
    • (1996) Adv Virus Res , vol.47 , pp. 159-251
    • Buck, K.W.1
  • 5
    • 0032510963 scopus 로고    scopus 로고
    • Crystal structure of RNA helicase from genotype 1b hepatitis C virus. A feasible mechanism of unwinding duplex RNA
    • Cho HS, Ha NC, Kang LW, Chung KM, Back SH, Jang SK, Oh BH. 1998. Crystal structure of RNA helicase from genotype 1b hepatitis C virus. A feasible mechanism of unwinding duplex RNA. J Biol Chem 273:15045-15052.
    • (1998) J Biol Chem , vol.273 , pp. 15045-15052
    • Cho, H.S.1    Ha, N.C.2    Kang, L.W.3    Chung, K.M.4    Back, S.H.5    Jang, S.K.6    Oh, B.H.7
  • 6
    • 0033081226 scopus 로고    scopus 로고
    • Human DNA helicase VIII: A DNA and RNA helicase corresponding to the G3BP protein, an element of the ras transduction pathway
    • Costa M, Ochem A, Staub A, Falaschi A. 1999. Human DNA helicase VIII: A DNA and RNA helicase corresponding to the G3BP protein, an element of the ras transduction pathway. Nucleic Acids Res 27:817-821.
    • (1999) Nucleic Acids Res , vol.27 , pp. 817-821
    • Costa, M.1    Ochem, A.2    Staub, A.3    Falaschi, A.4
  • 7
    • 0029348072 scopus 로고
    • Purification and characterization of the Upf1 protein: A factor involved in translation and mRNA degradation
    • Czaplinski K, Wenig Y, Hagan KW, Peltz SW. 1995. Purification and characterization of the Upf1 protein: A factor involved in translation and mRNA degradation. RNA 1:610-623.
    • (1995) RNA , vol.1 , pp. 610-623
    • Czaplinski, K.1    Wenig, Y.2    Hagan, K.W.3    Peltz, S.W.4
  • 8
    • 0029881285 scopus 로고    scopus 로고
    • Sindbis virus RNA-negative mutants that fail to convert from minus-strand to plus-strand synthesis: Role of the nsP2 protein
    • Dé I, Sawicki SG, Sawicki DL. 1996. Sindbis virus RNA-negative mutants that fail to convert from minus-strand to plus-strand synthesis: Role of the nsP2 protein. J Virol 70:2706-2719.
    • (1996) J Virol , vol.70 , pp. 2706-2719
    • Dé, I.1    Sawicki, S.G.2    Sawicki, D.L.3
  • 9
    • 0033133863 scopus 로고    scopus 로고
    • Unwinding RNA in Saccharomyces cerevisiae: DEAD-box proteins and related families
    • de la Cruz J, Kressler D, Linder P. 1999. Unwinding RNA in Saccharomyces cerevisiae: DEAD-box proteins and related families. Trends Biochem Sci 24:192-198.
    • (1999) Trends Biochem Sci , vol.24 , pp. 192-198
    • De La Cruz, J.1    Kressler, D.2    Linder, P.3
  • 11
    • 0027301893 scopus 로고
    • DbpA: A DEAD box protein specifically activated by 23S rRNA
    • Fuller-Pace FV, Nicol SM, Reid AD, Lane DP. 1993. DbpA: A DEAD box protein specifically activated by 23S rRNA. EMBO J 12:3619-3626.
    • (1993) EMBO J , vol.12 , pp. 3619-3626
    • Fuller-Pace, F.V.1    Nicol, S.M.2    Reid, A.D.3    Lane, D.P.4
  • 13
    • 0024462161 scopus 로고
    • Viral proteins containing the purine NTP-binding sequence pattern
    • Gorbalenya AE, Koonin EV. 1989. Viral proteins containing the purine NTP-binding sequence pattern. Nucleic Acids Res 17:8413-8440.
    • (1989) Nucleic Acids Res , vol.17 , pp. 8413-8440
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 14
    • 0027182114 scopus 로고
    • Helicases: Amino acid sequence comparisons and structure-function relationships
    • Gorbalenya AE, Koonin EV. 1993. Helicases: Amino acid sequence comparisons and structure-function relationships. Curr Opin Struct Biol 3:419-429.
    • (1993) Curr Opin Struct Biol , vol.3 , pp. 419-429
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 15
    • 0024398958 scopus 로고
    • Coronavirus genome: Prediction of putative functional domains in the non-structural polyprotein by comparative amino acid sequence analysis
    • Gorbalenya AE, Koonin EV, Donchenko AP, Blinov VM. 1989a. 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
  • 16
    • 0024344173 scopus 로고
    • Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes
    • Gorbalenya AE, Koonin EV, Donchenko AP, Blinov VM. 1989b. Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes. Nucleic Acids Res 17:4713-4730.
    • (1989) Nucleic Acids Res , vol.17 , pp. 4713-4730
    • Gorbalenya, A.E.1    Koonin, E.V.2    Donchenko, A.P.3    Blinov, V.M.4
  • 17
    • 0029911607 scopus 로고    scopus 로고
    • Identification of an RNA-stimulated NT-Pase in the predicted helicase sequence of the Rubella virus nonstructural polyprotein
    • Gros C, Wengler G. 1996. Identification of an RNA-stimulated NT-Pase in the predicted helicase sequence of the Rubella virus nonstructural polyprotein. Virology 217:367-372.
    • (1996) Virology , vol.217 , pp. 367-372
    • Gros, C.1    Wengler, G.2
  • 18
    • 0029079703 scopus 로고
    • Mutational analysis of vaccinia virus nucleoside triphosphate phosphohydrolase II, a DExH box RNA helicase
    • Gross CH, Shuman S. 1995. Mutational analysis of vaccinia virus nucleoside triphosphate phosphohydrolase II, a DExH box RNA helicase. J Virol 69:4727-4736.
    • (1995) J Virol , vol.69 , pp. 4727-4736
    • Gross, C.H.1    Shuman, S.2
  • 19
    • 0242673508 scopus 로고    scopus 로고
    • Characterization of a 105-kDa polypeptide encoded in gene 1 of the human coronavirus HCV 229E
    • Grötzinger C, Heusipp G, Ziebuhr J, Harms U, Süss J, Siddell SG. 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
  • 20
    • 0030735535 scopus 로고    scopus 로고
    • DNA helicase activity of the hepatitis C virus nonstructural protein 3
    • Gwack Y, Kim DW, Han JH, Choe J. 1997. DNA helicase activity of the hepatitis C virus nonstructural protein 3. Eur J Biochem 250:47-54.
    • (1997) Eur J Biochem , vol.250 , pp. 47-54
    • Gwack, Y.1    Kim, D.W.2    Han, J.H.3    Choe, J.4
  • 21
    • 0033428970 scopus 로고    scopus 로고
    • Helicase motifs: The engine that powers DNA unwinding
    • Hall MC, Matson SW. 1999. Helicase motifs: The engine that powers DNA unwinding. Mol Microbiol 34:867-877.
    • (1999) Mol Microbiol , vol.34 , pp. 867-877
    • Hall, M.C.1    Matson, S.W.2
  • 22
    • 0030924142 scopus 로고    scopus 로고
    • Reversal in the direction of movement of a molecular motor
    • Henningsen U, Schliwa M. 1997. Reversal in the direction of movement of a molecular motor. Nature 389:93-96.
    • (1997) Nature , vol.389 , pp. 93-96
    • Henningsen, U.1    Schliwa, M.2
  • 23
    • 0027313298 scopus 로고
    • Nucleotide sequence of the human coronavirus 229E RNA polymerase locus
    • Herold J, Raabe T, Schelle-Prinz B, Siddell SG. 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
  • 24
    • 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, Harms U, Siddell SG, Ziebuhr J. 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
  • 25
    • 0032478255 scopus 로고    scopus 로고
    • Brome mosaic virus RNA replication protein 1a dramatically increases in vivo stability but not translation of viral genomic RNA3
    • Janda M, Ahlquist P. 1998. Brome mosaic virus RNA replication protein 1a dramatically increases in vivo stability but not translation of viral genomic RNA3. Proc Natl Acad Sci USA 95:2227-2232.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 2227-2232
    • Janda, M.1    Ahlquist, P.2
  • 26
    • 0034719392 scopus 로고    scopus 로고
    • The DExH protein NPH-II is a processive and directional motor for unwinding RNA
    • Jankowsky E, Gross CH, Shuman S, Pyle AM. 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
  • 27
    • 0029820585 scopus 로고    scopus 로고
    • ATPase, GTPase, and RNA binding activities associated with the 206-kilodalton protein of turnip yellow mosaic virus
    • Kadaré G, David C, Haenni, AL. 1996. ATPase, GTPase, and RNA binding activities associated with the 206-kilodalton protein of turnip yellow mosaic virus. J Virol 70:8169-8174.
    • (1996) J Virol , vol.70 , pp. 8169-8174
    • Kadaré, G.1    David, C.2    Haenni, A.L.3
  • 28
    • 0030897821 scopus 로고    scopus 로고
    • Virus-encoded RNA helicases
    • Kadaré G, Haenni AL 1997. Virus-encoded RNA helicases. J Virol 71:2583-2590.
    • (1997) J Virol , vol.71 , pp. 2583-2590
    • Kadaré, G.1    Haenni, A.L.2
  • 29
    • 0033517855 scopus 로고    scopus 로고
    • The sen1(+) gene of Schizosaccharomyces pombe, a homologue of budding yeast SEN1, encodes an RNA and DNA helicase
    • Kim HD, Choe J, Seo YS. 1999. The sen1(+) gene of Schizosaccharomyces pombe, a homologue of budding yeast SEN1, encodes an RNA and DNA helicase. Biochemistry 38:14697-14710.
    • (1999) Biochemistry , vol.38 , pp. 14697-14710
    • Kim, H.D.1    Choe, J.2    Seo, Y.S.3
  • 30
    • 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 JL, Morgenstern KA, Griffith JP, Dwyer MD, Thomson JA, Murcko MA, Lin C, Caron PR. 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
  • 31
    • 0027504136 scopus 로고
    • Evolution and taxonomy of positive-strand RNA viruses: Implications of comparative analysis of amino acid sequences
    • Koonin EV, Dolja VV. 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
  • 32
    • 0030740262 scopus 로고    scopus 로고
    • Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP
    • Korolev S, Hsieh J, Gauss GH, Lohman TM, Waksman G. 1997. Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP. Cell 90:635-647.
    • (1997) Cell , vol.90 , pp. 635-647
    • Korolev, S.1    Hsieh, J.2    Gauss, G.H.3    Lohman, T.M.4    Waksman, G.5
  • 33
    • 0031911760 scopus 로고    scopus 로고
    • Comparisons between the structures of HCV and Rep helicases reveal structural similarities between SF1 and SF2 super-families of helicases
    • Korolev S, Yao N, Lohman TM, Weber PC, Waksman G. 1998. Comparisons between the structures of HCV and Rep helicases reveal structural similarities between SF1 and SF2 super-families of helicases. Protein Sci 7:605-610.
    • (1998) Protein Sci , vol.7 , pp. 605-610
    • Korolev, S.1    Yao, N.2    Lohman, T.M.3    Weber, P.C.4    Waksman, G.5
  • 34
    • 0025251611 scopus 로고
    • Analysis of the role of brome mosaic virus 1a protein domains in RNA replication, using linker insertion mutagenesis
    • Kroner PA, Young BM, Ahlquist P. 1990. Analysis of the role of brome mosaic virus 1a protein domains in RNA replication, using linker insertion mutagenesis. J Virol 64:6110-6120.
    • (1990) J Virol , vol.64 , pp. 6110-6120
    • Kroner, P.A.1    Young, B.M.2    Ahlquist, P.3
  • 35
    • 0033992576 scopus 로고    scopus 로고
    • Structure and function of hepatitis C virus NS3 helicase
    • Kwong AD, Kim JL, 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
  • 36
    • 0031824880 scopus 로고    scopus 로고
    • Expression and characterization of the hepatitis G virus helicase
    • Laxton CD, McMillan D, Sullivan V, Ackrill AM. 1998. Expression and characterization of the hepatitis G virus helicase. J Viral Hepat 5:21-26.
    • (1998) J Viral Hepat , vol.5 , pp. 21-26
    • Laxton, C.D.1    McMillan, D.2    Sullivan, V.3    Ackrill, A.M.4
  • 37
    • 0027327132 scopus 로고
    • Human RNA helicase A is homologous to the maleless protein of Drosophila
    • Lee CG, Hurwitz J. 1993. Human RNA helicase A is homologous to the maleless protein of Drosophila. J Biol Chem 268:16822-16830.
    • (1993) J Biol Chem , vol.268 , pp. 16822-16830
    • Lee, C.G.1    Hurwitz, J.2
  • 38
    • 0033950596 scopus 로고    scopus 로고
    • Are DEAD-box proteins becoming respectable helicases?
    • Linder P, Daugeron MC. 2000. Are DEAD-box proteins becoming respectable helicases? Nat Struct Biol 7:97-99.
    • (2000) Nat Struct Biol , vol.7 , pp. 97-99
    • Linder, P.1    Daugeron, M.C.2
  • 39
    • 0029893874 scopus 로고    scopus 로고
    • Mechanisms of helicase-catalyzed DNA unwinding
    • Lohman TM, Bjornson KP. 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, Kp.2
  • 40
    • 0029417203 scopus 로고
    • The "DEAD box" protein Dbpa interacts specifically with the peptidyltransferase center in 23S rRNA
    • Nicol SM, Fuller-Pace FV. 1995. The "DEAD box" protein DbpA interacts specifically with the peptidyltransferase center in 23S rRNA. Proc Natl Acad Sci USA 92:11681-11685.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 11681-11685
    • Nicol, S.M.1    Fuller-Pace, F.V.2
  • 41
    • 0029736818 scopus 로고    scopus 로고
    • 18S rRNA processing requires the RNA helicase-like protein Rrp3
    • O'Day CL, Chavanikamannil F, Abelson J. 1996. 18S rRNA processing requires the RNA helicase-like protein Rrp3. Nucleic Acids Res 24:3201-3207.
    • (1996) Nucleic Acids Res , vol.24 , pp. 3201-3207
    • O'Day, C.L.1    Chavanikamannil, F.2    Abelson, J.3
  • 42
    • 0028972782 scopus 로고
    • Biochemical and genetic analyses of the interaction between the helicase-like and polymerase-like proteins of the brome mosaic virus
    • O'Reilly EK, Tang N, Ahlquist P, Kao CC. 1995. Biochemical and genetic analyses of the interaction between the helicase-like and polymerase-like proteins of the brome mosaic virus. Virology 214:59-71.
    • (1995) Virology , vol.214 , pp. 59-71
    • O'Reilly, E.K.1    Tang, N.2    Ahlquist, P.3    Kao, C.C.4
  • 43
    • 0031851751 scopus 로고    scopus 로고
    • Interactions between the structural domains of the RNA replication proteins of plant-infecting RNA viruses
    • O'Reilly EK, Wang Z, French R, Kao CC. 1998. Interactions between the structural domains of the RNA replication proteins of plant-infecting RNA viruses. J Virol 72:7160-7169.
    • (1998) J Virol , vol.72 , pp. 7160-7169
    • O'Reilly, E.K.1    Wang, Z.2    French, R.3    Kao, C.C.4
  • 44
    • 0029833090 scopus 로고    scopus 로고
    • Complete replication in vitro of tobacco mosaic virus RNA by a template-dependent, membrane-bound RNA polymerase
    • Osman TA, Buck KW. 1996. Complete replication in vitro of tobacco mosaic virus RNA by a template-dependent, membrane-bound RNA polymerase. J Virol 70:6227-6234.
    • (1996) J Virol , vol.70 , pp. 6227-6234
    • Osman, T.A.1    Buck, K.W.2
  • 45
    • 0025011806 scopus 로고
    • Identification of barley stripe mosaic virus genes involved in viral RNA replication and systemic movement
    • Petty IT, French R, Jones RW, Jackson AO. 1990. Identification of barley stripe mosaic virus genes involved in viral RNA replication and systemic movement. EMBO J 9:3453-3457.
    • (1990) EMBO J , vol.9 , pp. 3453-3457
    • Petty, I.T.1    French, R.2    Jones, R.W.3    Jackson, A.O.4
  • 46
    • 0033548596 scopus 로고    scopus 로고
    • Characterization of the nucleoside triphosphatase activity of poliovirus protein 2C reveals a mechanism by which guanidine inhibits poliovirus replication
    • Pfister T, Wimmer E. 1999. Characterization of the nucleoside triphosphatase activity of poliovirus protein 2C reveals a mechanism by which guanidine inhibits poliovirus replication. J Biol Chem 274:6992-7001.
    • (1999) J Biol Chem , vol.274 , pp. 6992-7001
    • Pfister, T.1    Wimmer, E.2
  • 47
    • 0031576353 scopus 로고    scopus 로고
    • The crystal structure of a parallel-stranded guanine tetraplex at 0.95 Å resolution
    • Phillips K, Dauter Z, Murchie AI, Lilley DM, Luisi B. 1997. The crystal structure of a parallel-stranded guanine tetraplex at 0.95 Å resolution. J Mol Biol 273:171-182.
    • (1997) J Mol Biol , vol.273 , pp. 171-182
    • Phillips, K.1    Dauter, Z.2    Murchie, A.I.3    Lilley, D.M.4    Luisi, B.5
  • 48
    • 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 DR, Clarke BE, Porter DJT. 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    Clarke, B.E.3    Porter, D.J.T.4
  • 49
    • 0028018141 scopus 로고
    • AtPase and GTPase activities associated with Semliki Forest virus nonstructural protein nsP2
    • Rikkonen M, Peränen J, Kääriäinen L. 1994. ATPase and GTPase activities associated with Semliki Forest virus nonstructural protein nsP2. J Virol 68:5804-5810.
    • (1994) J Virol , vol.68 , pp. 5804-5810
    • Rikkonen, M.1    Peränen, J.2    Kääriäinen, L.3
  • 50
    • 0027537974 scopus 로고
    • Poliovirus protein 2C has ATPase and GTPase activities
    • Rodriguez PL, Carrasco L. 1993. Poliovirus protein 2C has ATPase and GTPase activities. J Biol Chem 268:8105-8110.
    • (1993) J Biol Chem , vol.268 , pp. 8105-8110
    • Rodriguez, P.L.1    Carrasco, L.2
  • 51
    • 0027990470 scopus 로고
    • Purification, properties, and subcellular localization of foxtail mosaic potexvirus 26-kDa protein
    • Rouleau M, Smith RJ, Bancroft JB, Mackie, GA. 1994. Purification, properties, and subcellular localization of foxtail mosaic potexvirus 26-kDa protein. Virology 204:254-265.
    • (1994) Virology , vol.204 , pp. 254-265
    • Rouleau, M.1    Smith, R.J.2    Bancroft, J.B.3    Mackie, G.A.4
  • 53
    • 0024371790 scopus 로고
    • RNA unwinding activity of SV40 large T antigen
    • Scheffner M, Knippers R, Stahl H. 1989. RNA unwinding activity of SV40 large T antigen. Cell 57:955-963.
    • (1989) Cell , vol.57 , pp. 955-963
    • Scheffner, M.1    Knippers, R.2    Stahl, H.3
  • 54
    • 0026569419 scopus 로고
    • D-E-A-D protein family of putative RNA helicases
    • Schmid SR, Linder P. 1992. D-E-A-D protein family of putative RNA helicases. Mol Microbiol 6:283-291.
    • (1992) Mol Microbiol , vol.6 , pp. 283-291
    • Schmid, S.R.1    Linder, P.2
  • 55
    • 0033516596 scopus 로고    scopus 로고
    • DNA binding mediates conformational changes and metal ion coordination in the active site of PcrA helicase
    • Soultanas P, Dillingham MS, Velankar SS, Wigley DB. 1999. DNA binding mediates conformational changes and metal ion coordination in the active site of PcrA helicase. J Mol Biol 290:137-148.
    • (1999) J Mol Biol , vol.290 , pp. 137-148
    • Soultanas, P.1    Dillingham, M.S.2    Velankar, S.S.3    Wigley, D.B.4
  • 56
    • 0022763344 scopus 로고
    • DNA helicase activity of SV40 large tumor antigen
    • Stahl H, Droge P, Knippers R. 1986. DNA helicase activity of SV40 large tumor antigen. EMBO J 5:1939-1944.
    • (1986) EMBO J , vol.5 , pp. 1939-1944
    • Stahl, H.1    Droge, P.2    Knippers, R.3
  • 58
    • 0027199917 scopus 로고
    • Hepatitis C virus NS3 protein polynucleotide-stimulated nucleoside triphosphatase and comparison with the related pestivirus and flavivirus enzymes
    • Suzich JA, Tamura JK, Palmer-Hill F, Warrener P, Grakoui A, Rice CM, Feinstone SM, Collett MS. 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
  • 59
    • 0003149856 scopus 로고
    • Coronavirus replication, transcription, and RNA recombination
    • Siddell SG, ed. New York: Plenum Press
    • van der Most RG, Spaan WJM. 1995. Coronavirus replication, transcription, and RNA recombination. In: Siddell SG, ed. The Coronaviridae. New York: Plenum Press, pp 11-31.
    • (1995) The Coronaviridae , pp. 11-31
    • Van Der Most, R.G.1    Spaan, W.J.M.2
  • 60
    • 0031017109 scopus 로고    scopus 로고
    • An infectious arterivirus cDNA clone: Identification of a replicase point mutation that abolishes discontinuous mRNA transcription
    • van Dinten LC, den Boon JA, Wassenaar AL, Spaan WJ, Snijder EJ. 1997. An infectious arterivirus cDNA clone: Identification of a replicase point mutation that abolishes discontinuous mRNA transcription. Proc Natl Acad Sci USA 94:991-996.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 991-996
    • Van Dinten, L.C.1    Den Boon, J.A.2    Wassenaar, A.L.3    Spaan, W.J.4    Snijder, E.J.5
  • 61
    • 0032982143 scopus 로고    scopus 로고
    • Proteolytic processing of the open reading frame 1b-encoded part of arterivirus replicase is mediated by nsp4 serine protease and is essential for virus replication
    • van Dinten LC, Rensen S, Gorbalenya AE, Snijder EJ. 1999. Proteolytic processing of the open reading frame 1b-encoded part of arterivirus replicase is mediated by nsp4 serine protease and is essential for virus replication. J Virol 73:2027-2037.
    • (1999) J Virol , vol.73 , pp. 2027-2037
    • Van Dinten, L.C.1    Rensen, S.2    Gorbalenya, A.E.3    Snijder, E.J.4
  • 62
    • 0029844841 scopus 로고    scopus 로고
    • Processing of the equine arteritis virus replicase ORF 1b protein: Identification of cleavage products containing the putative viral polymerase and helicase domains
    • van Dinten LC, Wassenaar AL, Gorbalenya AE, Spaan WJ, Snijder, EJ. 1996. Processing of the equine arteritis virus replicase ORF 1b protein: Identification of cleavage products containing the putative viral polymerase and helicase domains. J Virol 70:6625-6633.
    • (1996) J Virol , vol.70 , pp. 6625-6633
    • Van Dinten, L.C.1    Wassenaar, A.L.2    Gorbalenya, A.E.3    Spaan, W.J.4    Snijder, E.J.5
  • 63
    • 0033515425 scopus 로고    scopus 로고
    • Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism
    • Velankar SS, Soultanas P, Dillingham MS, Subramanya HS, Wigley DB. 1999. Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism. Cell 97:75-84.
    • (1999) Cell , vol.97 , pp. 75-84
    • Velankar, S.S.1    Soultanas, P.2    Dillingham, M.S.3    Subramanya, H.S.4    Wigley, D.B.5
  • 64
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker JE, Saraste M, Runswick MJ, Gay NJ. 1982. Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J 1:945-951.
    • (1982) EMBO J , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 65
    • 0029888811 scopus 로고    scopus 로고
    • An RNA-dependent ATPase associated with U2/U6 snRNAs in pre-mRNA splicing
    • Xu D, Nouraini S, Field D, Tang SJ, Friesen JD. 1996. An RNA-dependent ATPase associated with U2/U6 snRNAs in pre-mRNA splicing. Nature 381:709-713.
    • (1996) Nature , vol.381 , pp. 709-713
    • Xu, D.1    Nouraini, S.2    Field, D.3    Tang, S.J.4    Friesen, J.D.5
  • 67
    • 0026816908 scopus 로고
    • Site-directed mutagenesis of herpesvirus glycoprotein phosphorylation sites by recombination polymerase chain reaction
    • Yao Z, Jones DH, Grose C. 1992. Site-directed mutagenesis of herpesvirus glycoprotein phosphorylation sites by recombination polymerase chain reaction. PCR Methods Appl 1:205-207.
    • (1992) PCR Methods Appl , vol.1 , pp. 205-207
    • Yao, Z.1    Jones, D.H.2    Grose, C.3
  • 68
    • 0028297111 scopus 로고
    • Nuclear DNA helicase II unwinds both DNA and RNA
    • Zhang S, Grosse F. 1994. Nuclear DNA helicase II unwinds both DNA and RNA. Biochemistry 33:3906-3912.
    • (1994) Biochemistry , vol.33 , pp. 3906-3912
    • Zhang, S.1    Grosse, F.2
  • 69
    • 0029017145 scopus 로고
    • Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity
    • Ziebuhr J, Herold J, Siddell SG. 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
  • 70
    • 0034072633 scopus 로고    scopus 로고
    • Virus-encoded proteinases and proteolytic processing in the Nidovirales
    • Ziebuhr J, Snijder EJ, Gorbalenya AE. 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


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