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Volumn 74, Issue 11, 2000, Pages 5213-5223

The predicted metal-binding region of the arterivirus helicase protein is involved in subgenomic mRNA synthesis, genome replication, and virion biogenesis

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; HELICASE; HISTIDINE; MESSENGER RNA; RNA DIRECTED RNA POLYMERASE; VIRUS ENZYME; VIRUS RNA;

EID: 0034105481     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.74.11.5213-5223.2000     Document Type: Article
Times cited : (88)

References (73)
  • 2
    • 0025765004 scopus 로고
    • A systematic mutational analysis of hormone-binding determinants in the human growth hormone receptor
    • Bass, S. H., M. G. Mulkerrin, and J. A. Wells. 1991. A systematic mutational analysis of hormone-binding determinants in the human growth hormone receptor. Proc. Natl. Acad. Sci. USA 88:4498-4502.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 4498-4502
    • Bass, S.H.1    Mulkerrin, M.G.2    Wells, J.A.3
  • 3
    • 0030959658 scopus 로고    scopus 로고
    • Crystal structure of the RAG1 dimerization domain reveals multiple zinc-binding motifs including a novel zinc binuclear cluster
    • Bellon, S. F., K. K. Rodgers, D. G. Schatz, J. E. Coleman, and T. A. Steitz. 1997. Crystal structure of the RAG1 dimerization domain reveals multiple zinc-binding motifs including a novel zinc binuclear cluster. Nat. Struct. Biol. 4:586-591.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 586-591
    • Bellon, S.F.1    Rodgers, K.K.2    Schatz, D.G.3    Coleman, J.E.4    Steitz, T.A.5
  • 5
    • 0029866646 scopus 로고    scopus 로고
    • The galvanization of biology: A growing appreciation for the roles of zinc
    • Berg, J. M., and Y. Shi. 1996. The galvanization of biology: a growing appreciation for the roles of zinc. Science 271:1081-1085.
    • (1996) Science , vol.271 , pp. 1081-1085
    • Berg, J.M.1    Shi, Y.2
  • 6
    • 0028932963 scopus 로고
    • The solution structure of the RING finger domain from the acute promyelocytic leukaemia proto-oncoprotein PML
    • Borden, K. L. B., M. N. Boddy, J. Lally, N. J. O'Reilly, S. Martin, K. Howe, E. Solomon, and P. S. Freemont. 1995. The solution structure of the RING finger domain from the acute promyelocytic leukaemia proto-oncoprotein PML. EMBO J. 14:1532-1541.
    • (1995) EMBO J. , vol.14 , pp. 1532-1541
    • Borden, K.L.B.1    Boddy, M.N.2    Lally, J.3    O'Reilly, N.J.4    Martin, S.5    Howe, K.6    Solomon, E.7    Freemont, P.S.8
  • 7
    • 0030634897 scopus 로고    scopus 로고
    • Nidovirales: A new order comprising Coronaviridae and Arteriviridae
    • Cavanagh, D. 1997. Nidovirales: a new order comprising Coronaviridae and Arteriviridae. Arch. Virol. 142:629-633.
    • (1997) Arch. Virol. , vol.142 , pp. 629-633
    • Cavanagh, D.1
  • 8
    • 0028326844 scopus 로고
    • Specific binding of HIV-1 nucleocapsid protein to PSI RNA in vitro requires N-terminal zinc finger and flanking basic amino acid residues
    • Dannull, J., A. Surovoy, G. Jung, and K. Moelling. 1994. Specific binding of HIV-1 nucleocapsid protein to PSI RNA in vitro requires N-terminal zinc finger and flanking basic amino acid residues. EMBO J. 13:1525-1533.
    • (1994) EMBO J. , vol.13 , pp. 1525-1533
    • Dannull, J.1    Surovoy, A.2    Jung, G.3    Moelling, K.4
  • 9
    • 0029974217 scopus 로고    scopus 로고
    • Equine arteritis virus subgenomic mRNA synthesis: Analysis of leader-body junctions and replicative-form RNAs
    • den Boon, J. A., M. F. Kleijnen, W. J. M. Spaan, and E. J. Snijder. 1996. Equine arteritis virus subgenomic mRNA synthesis: analysis of leader-body junctions and replicative-form RNAs. J. Virol. 70:4291-4298.
    • (1996) J. Virol. , vol.70 , pp. 4291-4298
    • Den Boon, J.A.1    Kleijnen, M.F.2    Spaan, W.J.M.3    Snijder, E.J.4
  • 11
    • 0028840838 scopus 로고
    • Equine arteritis virus subgenomic RNA transcription: UV inactivation and translation inhibition studies
    • den Boon, J. A., W. J. M. Spaan, and E. J. Snijder. 1995. Equine arteritis virus subgenomic RNA transcription: UV inactivation and translation inhibition studies. Virology 213:364-372.
    • (1995) Virology , vol.213 , pp. 364-372
    • Den Boon, J.A.1    Spaan, W.J.M.2    Snijder, E.J.3
  • 12
    • 0032787420 scopus 로고    scopus 로고
    • The putative helicase of the coronavirus mouse hepatitis virus is processed from the replicase gene polyprotein and localizes in complexes that are active in viral RNA synthesis
    • Denison, M. R., W. J. M. Spaan, Y. van der Meer, C. A. Gibson, A. C. Sims, E. Prentice, and X. T. Lu. 1999. The putative helicase of the coronavirus mouse hepatitis virus is processed from the replicase gene polyprotein and localizes in complexes that are active in viral RNA synthesis. J. Virol. 73: 6862-6871.
    • (1999) J. Virol. , vol.73 , pp. 6862-6871
    • Denison, M.R.1    Spaan, W.J.M.2    Van Der Meer, Y.3    Gibson, C.A.4    Sims, A.C.5    Prentice, E.6    Lu, X.T.7
  • 15
    • 0030861788 scopus 로고    scopus 로고
    • The genome organization of the Nidovirales: Similarities and differences between arteri-, toro-, and coronaviruses
    • de Vries, A. A. F., M. C. Horzinek, P. J. M. Rottier, and R. J. de Groot. 1997. The genome organization of the Nidovirales: similarities and differences between arteri-, toro-, and coronaviruses. Semin. Virol. 8:33-47.
    • (1997) Semin. Virol. , vol.8 , pp. 33-47
    • De Vries, A.A.F.1    Horzinek, M.C.2    Rottier, P.J.M.3    De Groot, R.J.4
  • 16
    • 0028044755 scopus 로고
    • Clustered charged-to-alanine mutagenesis of poliovirus RNA-dependent RNA polymerase yields multiple temperature-sensitive mutants defective in RNA synthesis
    • Diamond, S. E., and K. Kirkegaard. 1994. Clustered charged-to-alanine mutagenesis of poliovirus RNA-dependent RNA polymerase yields multiple temperature-sensitive mutants defective in RNA synthesis. J. Virol. 68:863-876.
    • (1994) J. Virol. , vol.68 , pp. 863-876
    • Diamond, S.E.1    Kirkegaard, K.2
  • 17
    • 0002425455 scopus 로고
    • Isolation of a filterable agent causing arteritis of horses and abortion by mares. Its differentiation from the equine abortion (influenza) virus
    • Doll, E. R., J. T. Bryans, W. H. McCollum, and M. E. W. Crowe. 1957. Isolation of a filterable agent causing arteritis of horses and abortion by mares. Its differentiation from the equine abortion (influenza) virus. Cornell Vet. 47:3-41.
    • (1957) Cornell Vet. , vol.47 , pp. 3-41
    • Doll, E.R.1    Bryans, J.T.2    McCollum, W.H.3    Crowe, M.E.W.4
  • 18
    • 0028998313 scopus 로고
    • Identification of the primase active site of the herpes simplex virus type 1 helicase-primase
    • Dracheva, S., E. V. Koonin, and J. J. Crute. 1995. Identification of the primase active site of the herpes simplex virus type 1 helicase-primase. J. Biol. Chem. 270:14148-14153.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14148-14153
    • Dracheva, S.1    Koonin, E.V.2    Crute, J.J.3
  • 19
    • 0027239790 scopus 로고
    • The RING finger: A novel protein sequence motif related to the zinc finger
    • Freemont, P. S. 1993. The RING finger: a novel protein sequence motif related to the zinc finger. Ann. N. Y. Acad. Sci. 684:174-192.
    • (1993) Ann. N. Y. Acad. Sci. , vol.684 , pp. 174-192
    • Freemont, P.S.1
  • 20
    • 0029119673 scopus 로고
    • Comparison of equine arteritis virus isolates using neutralizing monoclonal antibodies and identification of sequence changes in GL associated with neutralization resistance
    • Glaser, A. L., A. A. F. de Vries, and E. J. Dubovi. 1995. Comparison of equine arteritis virus isolates using neutralizing monoclonal antibodies and identification of sequence changes in GL associated with neutralization resistance. J. Gen. Virol. 76:2223-2233.
    • (1995) J. Gen. Virol. , vol.76 , pp. 2223-2233
    • Glaser, A.L.1    De Vries, A.A.F.2    Dubovi, E.J.3
  • 21
    • 0027325337 scopus 로고
    • Complete genomic sequence and phylogenetic analysis of the lactate dehydrogenase-elevating virus (LDV)
    • Godeny, E. K., L. Chen, S. N. Kumar, S. L. Methven, E. V. Koonin, and M. A. Brinton. 1993. Complete genomic sequence and phylogenetic analysis of the lactate dehydrogenase-elevating virus (LDV). Virology 194:585-596.
    • (1993) Virology , vol.194 , pp. 585-596
    • Godeny, E.K.1    Chen, L.2    Kumar, S.N.3    Methven, S.L.4    Koonin, E.V.5    Brinton, M.A.6
  • 22
    • 0001868907 scopus 로고
    • Comparative analysis of the amino acid sequences of the key enzymes of the replication and expression of positive-strand RNA viruses. Validity of the approach and functional and evolutionary implications
    • Gorbalenya, A. E., and E. V. Koonin. 1993. Comparative analysis of the amino acid sequences of the key enzymes of the replication and expression of positive-strand RNA viruses. Validity of the approach and functional and evolutionary implications. Sov. Sci. Rev. Sect. D 11:1-84.
    • (1993) Sov. Sci. Rev. Sect. D , vol.11 , pp. 1-84
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 23
    • 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
  • 24
    • 0029986494 scopus 로고    scopus 로고
    • Genetic analysis of the zinc finger in the Moloney murine leukemia virus nucleocapsid domain: Replacement of zinc-coordinating residues with other zinc-coordinating residues yields noninfectious particles containing genomic RNA
    • Gorelick, R. J., D. J. Chabot, D. E. Ott, T. D. Gagliardi, A. Rein, L. E. Henderson, and L. O. Arthur. 1996. Genetic analysis of the zinc finger in the Moloney murine leukemia virus nucleocapsid domain: replacement of zinc-coordinating residues with other zinc-coordinating residues yields noninfectious particles containing genomic RNA. J. Virol. 70:2593-2597.
    • (1996) J. Virol. , vol.70 , pp. 2593-2597
    • Gorelick, R.J.1    Chabot, D.J.2    Ott, D.E.3    Gagliardi, T.D.4    Rein, A.5    Henderson, L.E.6    Arthur, L.O.7
  • 25
    • 0032863131 scopus 로고    scopus 로고
    • Characterization of the block in replication of nucleocapsid protein zinc finger mutants from Moloney murine leukemia virus
    • Gorelick, R. J., W. Fu, T. D. Gagliardi, W. J. Bosche, A. Rein, L. E. Henderson, and L. O. Arthur. 1999. Characterization of the block in replication of nucleocapsid protein zinc finger mutants from Moloney murine leukemia virus. J. Virol. 73:8185-8195.
    • (1999) J. Virol. , vol.73 , pp. 8185-8195
    • Gorelick, R.J.1    Fu, W.2    Gagliardi, T.D.3    Bosche, W.J.4    Rein, A.5    Henderson, L.E.6    Arthur, L.O.7
  • 26
    • 0028296721 scopus 로고
    • Targeted construction of temperature-sensitive mutations in vaccinia virus by replacing clustered charged residues with alanine
    • Hassett, D. E., and R. C. Condit. 1994. Targeted construction of temperature-sensitive mutations in vaccinia virus by replacing clustered charged residues with alanine. Proc. Natl. Acad. Sci. USA 91:4554-4558.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4554-4558
    • Hassett, D.E.1    Condit, R.C.2
  • 27
    • 0030476454 scopus 로고    scopus 로고
    • Cloning, characterization, and steroid-dependent post-transcriptional processing of RUSH-1 alpha and beta, two uteroglobin promoter-binding proteins
    • Hayward-Lester, A., A. Hewetson, E. G. Beale, P. J. Oefner, P. A. Doris, and B. S. Chilton. 1996. Cloning, characterization, and steroid-dependent post-transcriptional processing of RUSH-1 alpha and beta, two uteroglobin promoter-binding proteins. Mol. Endocrinol. 10:1335-1349.
    • (1996) Mol. Endocrinol. , vol.10 , pp. 1335-1349
    • Hayward-Lester, A.1    Hewetson, A.2    Beale, E.G.3    Oefner, P.J.4    Doris, P.A.5    Chilton, B.S.6
  • 28
    • 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
  • 29
    • 0023758546 scopus 로고
    • A segment of the 5′ nontranslated region of encephalomyocarditis virus RNA directs internal entry of ribosomes during in vitro translation
    • Jang, S. K., H. G. Krausslich, M. J. Nicklin, G. M. Duke, A. C. Palmenberg, and E. Wimmer. 1988. A segment of the 5′ nontranslated region of encephalomyocarditis virus RNA directs internal entry of ribosomes during in vitro translation. J. Virol. 62:2636-2643.
    • (1988) J. Virol. , vol.62 , pp. 2636-2643
    • Jang, S.K.1    Krausslich, H.G.2    Nicklin, M.J.3    Duke, G.M.4    Palmenberg, A.C.5    Wimmer, E.6
  • 30
    • 0026661167 scopus 로고
    • Saccharomyces cerevisiae RAD5-encoded DNA repair protein contains DNA helicase and zinc-binding sequence motifs and affects the stability of simple repetitive sequences in the genome
    • Johnson, R. E., S. T. Henderson, T. D. Petes, S. Prakash, M. Bankmann, and L. Prakash. 1992. Saccharomyces cerevisiae RAD5-encoded DNA repair protein contains DNA helicase and zinc-binding sequence motifs and affects the stability of simple repetitive sequences in the genome. Mol. Cell. Biol. 12:3807-3818.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3807-3818
    • Johnson, R.E.1    Henderson, S.T.2    Petes, T.D.3    Prakash, S.4    Bankmann, M.5    Prakash, L.6
  • 31
    • 0031014022 scopus 로고    scopus 로고
    • Subgenomic replicons of the flavivirus Kunjin: Construction and applications
    • Khromykh, A. A., and E. G. Westaway. 1997. Subgenomic replicons of the flavivirus Kunjin: construction and applications. J. Virol. 71:1497-1505.
    • (1997) J. Virol. , vol.71 , pp. 1497-1505
    • Khromykh, A.A.1    Westaway, E.G.2
  • 32
    • 0025343206 scopus 로고
    • A mutation in the Zn-finger of the GAL4 homolog LAC9 results in glucose repression of its target genes
    • Kuger, P., A. Godecke, and K. D. Breunig. 1990. A mutation in the Zn-finger of the GAL4 homolog LAC9 results in glucose repression of its target genes. Nucleic Acids Res. 18:745-751.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 745-751
    • Kuger, P.1    Godecke, A.2    Breunig, K.D.3
  • 33
    • 0029776368 scopus 로고    scopus 로고
    • The role of the zinc motif in sequence recognition by DNA primases
    • Kusakabe, T., and C. C. Richardson. 1996. The role of the zinc motif in sequence recognition by DNA primases. J. Biol. Chem. 271:19563-19570.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19563-19570
    • Kusakabe, T.1    Richardson, C.C.2
  • 34
    • 0021220689 scopus 로고
    • Characterization of leader RNA sequences on the virion and mRNAs of mouse hepatitis virus, a cytoplasmic RNA virus
    • Lai, M. M. C., R. S. Baric, P. R. Brayton, and S. A. Stohlman. 1984. Characterization of leader RNA sequences on the virion and mRNAs of mouse hepatitis virus, a cytoplasmic RNA virus. Proc. Natl. Acad. Sci. USA 81:3626-3630.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 3626-3630
    • Lai, M.M.C.1    Baric, R.S.2    Brayton, P.R.3    Stohlman, S.A.4
  • 35
    • 0030633479 scopus 로고    scopus 로고
    • The molecular biology of coronaviruses
    • Lai, M. M. C., 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.C.1    Cavanagh, D.2
  • 36
    • 0025643362 scopus 로고
    • A general method for rapid site-directed mutagenesis using the polymerase chain reaction
    • Landt, O., H.-P. Grunert, and U. Hahn. 1990. A general method for rapid site-directed mutagenesis using the polymerase chain reaction. Gene 96:125-128.
    • (1990) Gene , vol.96 , pp. 125-128
    • Landt, O.1    Grunert, H.-P.2    Hahn, U.3
  • 37
    • 0030863401 scopus 로고    scopus 로고
    • 4 zinc ring finger reveals a requirement for ICP0 in the expression of the essential α27 gene
    • 4 zinc ring finger reveals a requirement for ICP0 in the expression of the essential α27 gene. J. Virol. 71:8602-8614.
    • (1997) J. Virol. , vol.71 , pp. 8602-8614
    • Lium, E.K.1    Silverstein, S.2
  • 38
    • 0026058683 scopus 로고
    • The zinc finger region of simian virus 40 large T antigen is needed for hexamer assembly and origin melting
    • Loeber, G., J. E. Stenger, S. Ray, R. E. Parsons, M. E. Anderson, and P. Tegtmeyer. 1991. The zinc finger region of simian virus 40 large T antigen is needed for hexamer assembly and origin melting. J. Virol. 65:3167-3174.
    • (1991) J. Virol. , vol.65 , pp. 3167-3174
    • Loeber, G.1    Stenger, J.E.2    Ray, S.3    Parsons, R.E.4    Anderson, M.E.5    Tegtmeyer, P.6
  • 40
    • 0026594528 scopus 로고
    • Molecular analysis of yeast chromosome II between CMD1 and LYS2: The excision repair gene RAD16 located in this region belongs to a novel group of double-finger proteins
    • Mannhaupt, G., R. Stucka, S. Ehnle, I. Vetter, and H. Feldmann. 1992. Molecular analysis of yeast chromosome II between CMD1 and LYS2: the excision repair gene RAD16 located in this region belongs to a novel group of double-finger proteins. Yeast 8:397-408.
    • (1992) Yeast , vol.8 , pp. 397-408
    • Mannhaupt, G.1    Stucka, R.2    Ehnle, S.3    Vetter, I.4    Feldmann, H.5
  • 41
    • 0026547747 scopus 로고
    • DNA recognition by GAL4: Structure of a protein-DNA complex
    • Marmorstein, R., M. Carey, M. Ptashne, and S. C. Harrison. 1992. DNA recognition by GAL4: structure of a protein-DNA complex. Nature 356:379-380.
    • (1992) Nature , vol.356 , pp. 379-380
    • Marmorstein, R.1    Carey, M.2    Ptashne, M.3    Harrison, S.C.4
  • 42
    • 0027242413 scopus 로고
    • Subgenomic RNAs of Lelystad virus contain a conserved leader-body junction sequence
    • Meulenberg, J. J. M., E. J. de Meijer, and R. J. M. Moormann. 1993. Subgenomic RNAs of Lelystad virus contain a conserved leader-body junction sequence. J. Gen. Virol. 74:1697-1701.
    • (1993) J. Gen. Virol. , vol.74 , pp. 1697-1701
    • Meulenberg, J.J.M.1    De Meijer, E.J.2    Moormann, R.J.M.3
  • 44
    • 0034056493 scopus 로고    scopus 로고
    • Isolation and characterization of an arterivirus defective interfering RNA genome
    • Molenkamp, R., B. C. D. Rozier, S. Greve, W. J. M. Spaan, and E. J. Snijder. 2000. Isolation and characterization of an arterivirus defective interfering RNA genome. J. Virol. 74:3156-3165.
    • (2000) J. Virol. , vol.74 , pp. 3156-3165
    • Molenkamp, R.1    Rozier, B.C.D.2    Greve, S.3    Spaan, W.J.M.4    Snijder, E.J.5
  • 45
    • 0026356376 scopus 로고
    • Bacterial DNA replication initiation factor priA is related to proteins belonging to the 'DEAD-box' family
    • Ouzounis, C. A., and B. J. Blencowe. 1991. Bacterial DNA replication initiation factor priA is related to proteins belonging to the 'DEAD-box' family. Nucleic Acids Res. 19:6953.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 6953
    • Ouzounis, C.A.1    Blencowe, B.J.2
  • 46
    • 0033017866 scopus 로고    scopus 로고
    • Open reading frame 1a-encoded subunits of the arterivirus replicase induce endoplasmic reticulum-derived double-membrane vesicles which carry the viral replication complex
    • Pedersen, K. W., Y. van der Meer, N. Roos, and E. J. Snijder. 1999. Open reading frame 1a-encoded subunits of the arterivirus replicase induce endoplasmic reticulum-derived double-membrane vesicles which carry the viral replication complex. J. Virol. 73:2016-2026.
    • (1999) J. Virol. , vol.73 , pp. 2016-2026
    • Pedersen, K.W.1    Van Der Meer, Y.2    Roos, N.3    Snijder, E.J.4
  • 47
    • 0000100028 scopus 로고    scopus 로고
    • Lactate dehydrogenase-elevating virus and related viruses
    • B. N. Fields, D. M. Knipe, and P. M. Howley (ed.). Lippincott-Raven Publishers, Philadelphia, Pa
    • Plagemann, P. G. W. 1996. Lactate dehydrogenase-elevating virus and related viruses, p. 1105-1120. In B. N. Fields, D. M. Knipe, and P. M. Howley (ed.), Fields virology, 3rd ed. Lippincott-Raven Publishers, Philadelphia, Pa.
    • (1996) Fields Virology, 3rd Ed. , pp. 1105-1120
    • Plagemann, P.G.W.1
  • 48
    • 0024784519 scopus 로고
    • Identification of four conserved motifs among the RNA dependent polymerase encoding elements
    • Poch, O., I. Sauvaget, M. Delarue, and N. Tordo. 1989. Identification of four conserved motifs among the RNA dependent polymerase encoding elements. EMBO J. 8:3867-3874.
    • (1989) EMBO J. , vol.8 , pp. 3867-3874
    • Poch, O.1    Sauvaget, I.2    Delarue, M.3    Tordo, N.4
  • 49
    • 0023046315 scopus 로고
    • Analysis of the Kluyveromyces lactis positive regulatory gene LAC9 reveals functional homology to, but sequence divergence from, the Saccharomyces cerevisiae GAL4 gene
    • Salmeron, J. M., Jr., and S. A. Johnston. 1986. Analysis of the Kluyveromyces lactis positive regulatory gene LAC9 reveals functional homology to, but sequence divergence from, the Saccharomyces cerevisiae GAL4 gene. Nucleic Acids Res. 14:7767-7781.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 7767-7781
    • Salmeron J.M., Jr.1    Johnston, S.A.2
  • 51
    • 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. Biol. Med. 380:499-506.
    • (1995) Adv. Exp. Biol. Med. , vol.380 , pp. 499-506
    • Sawicki, S.G.1    Sawicki, D.L.2
  • 52
    • 0025168429 scopus 로고
    • The carboxyl-terminal part of the putative berne virus polymerase is expressed by ribosomal frameshifting and contains sequence motifs which indicate that toro-and coronaviruses are evolutionarily related
    • Snijder, E. J., J. A. den Boon, P. J. Bredenbeek, M. C. Horzinek, R. Rijnbrand, and W. J. M. Spaan. 1990. The carboxyl-terminal part of the putative Berne virus polymerase is expressed by ribosomal frameshifting and contains sequence motifs which indicate that toro-and coronaviruses are evolutionarily related. Nucleic Acids Res. 18:4535-4542.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 4535-4542
    • Snijder, E.J.1    Den Boon, J.A.2    Bredenbeek, P.J.3    Horzinek, M.C.4    Rijnbrand, R.5    Spaan, W.J.M.6
  • 53
    • 0031925071 scopus 로고    scopus 로고
    • The molecular biology of arteriviruses
    • Snijdir, E. J., and J. J. M. Meulenberg. 1998. The molecular biology of arteriviruses. J. Gen. Virol. 79:961-979.
    • (1998) J. Gen. Virol. , vol.79 , pp. 961-979
    • Snijdir, E.J.1    Meulenberg, J.J.M.2
  • 55
    • 0026475757 scopus 로고
    • The 5′ end of the equine arteritis virus replicase gene encodes a papainlike cysteine protease
    • Snijder, E. J., A. L. M. Wassenaar, and W. J. M. Spaan. 1992. The 5′ end of the equine arteritis virus replicase gene encodes a papainlike cysteine protease. J. Virol. 66:7040-7048.
    • (1992) J. Virol. , vol.66 , pp. 7040-7048
    • Snijder, E.J.1    Wassenaar, A.L.M.2    Spaan, W.J.M.3
  • 56
    • 0028067318 scopus 로고
    • Proteolytic processing of the replicase ORF1a protein of equine arteritis virus
    • Snijder, E. J., A. L. M. Wassenaar, and W. J. M. Spaan. 1994. Proteolytic processing of the replicase ORF1a protein of equine arteritis virus. J. Virol. 68:5755-5764.
    • (1994) J. Virol. , vol.68 , pp. 5755-5764
    • Snijder, E.J.1    Wassenaar, A.L.M.2    Spaan, W.J.M.3
  • 57
    • 0029044301 scopus 로고
    • The arterivirus nsp2 protease: An unusual cysteine protease with primary structure similarities to both papain-like and chymotrypsin-like proteases
    • Snijder, E. J., A. L. M. Wassenaar, W. J. M. Spaan, and A. E. Gorbalenya. 1995. The arterivirus nsp2 protease: an unusual cysteine protease with primary structure similarities to both papain-like and chymotrypsin-like proteases. J. Biol. Chem. 270:16671-16676.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16671-16676
    • Snijder, E.J.1    Wassenaar, A.L.M.2    Spaan, W.J.M.3    Gorbalenya, A.E.4
  • 58
    • 0029966508 scopus 로고    scopus 로고
    • The arterivirus nsp4 protease is the prototype of a novel group of chymotrypsin-like enzymes, the 3C-like serine proteases
    • Snijder, E. J., A. L. M. Wassenaar, L. C. van Dinten, W. J. M. Spaan, and A. E. Gorbalenya. 1996. The arterivirus nsp4 protease is the prototype of a novel group of chymotrypsin-like enzymes, the 3C-like serine proteases. J. Biol. Chem. 271:4864-4871.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4864-4871
    • Snijder, E.J.1    Wassenaar, A.L.M.2    Van Dinten, L.C.3    Spaan, W.J.M.4    Gorbalenya, A.E.5
  • 60
    • 0019377977 scopus 로고
    • Isolation and identification of virus-specific mRNAs in cells infected with mouse hepatitis virus (MHV-A59)
    • Spaan, W. J. M., P. J. M. Rottier, M. C. Horzinek, and B. A. M. van der Zeijst. 1981. Isolation and identification of virus-specific mRNAs in cells infected with mouse hepatitis virus (MHV-A59). Virology 108:424-434.
    • (1981) Virology , vol.108 , pp. 424-434
    • Spaan, W.J.M.1    Rottier, P.J.M.2    Horzinek, M.C.3    Van Der Zeijst, B.A.M.4
  • 61
    • 0031879009 scopus 로고    scopus 로고
    • ORF1a-encoded replicase subunits are involved in the membrane association of the arterivirus replication complex
    • van der Meer, Y., H. van Tol, J. Krijnse Locker, and E. J. Snijder. 1998. ORF1a-encoded replicase subunits are involved in the membrane association of the arterivirus replication complex. J. Virol. 72:6689-6698.
    • (1998) J. Virol. , vol.72 , pp. 6689-6698
    • Van Der Meer, Y.1    Van Tol, H.2    Krijnse Locker, J.3    Snijder, E.J.4
  • 62
    • 0031017109 scopus 로고    scopus 로고
    • An infectious arterivirus cDNA clone: Identification of a replicase point mutation which abolishes discontinuous mRNA transcription
    • van Dinten, L. C., J. A. den Boon, A. L. M. Wassenaar, W. J. M. Spaan, and E. J. Snijder. 1997. An infectious arterivirus cDNA clone: identification of a replicase point mutation which 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.M.3    Spaan, W.J.M.4    Snijder, E.J.5
  • 63
    • 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, L. C., S. Rensen, A. E. Gorbalenya, and E. J. Snijder. 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
  • 64
    • 0029844841 scopus 로고    scopus 로고
    • Processing of the equine arteritis virus replicase ORF1b protein: Identification of cleavage products containing the putative viral polymerase and helicase domains
    • van Dinten, L. C., A. L. M. Wassenaar, A. E. Gorbalenya, W. J. M. Spaan, and E. J. Snijder. 1996. Processing of the equine arteritis virus replicase ORF1b 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.M.2    Gorbalenya, A.E.3    Spaan, W.J.M.4    Snijder, E.J.5
  • 65
    • 0032718485 scopus 로고    scopus 로고
    • Arterivirus discontinuous mRNA transcription is guided by base-pairing between sense and antisense transcription-regulating sequences
    • van Marle, G., J. C. Dobbe, A. P. Gultyaev, W. Luytjes, W. J. M. Spaan, and E. J. Snijder. 1999. Arterivirus discontinuous mRNA transcription is guided by base-pairing between sense and antisense transcription-regulating sequences. Proc. Natl. Acad. Sci. USA 96:12056-12061.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12056-12061
    • Van Marle, G.1    Dobbe, J.C.2    Gultyaev, A.P.3    Luytjes, W.4    Spaan, W.J.M.5    Snijder, E.J.6
  • 66
    • 0033031789 scopus 로고    scopus 로고
    • Characterization of an equine arteritis virus replicase mutant defective in subgenomic mRNA synthesis
    • van Marle, G., L. C. van Dinten, W. Luytjes, W. J. M. Spaan, and E. J. Snijder. 1999. Characterization of an equine arteritis virus replicase mutant defective in subgenomic mRNA synthesis. J. Virol. 73:5274-5281.
    • (1999) J. Virol. , vol.73 , pp. 5274-5281
    • Van Marle, G.1    Van Dinten, L.C.2    Luytjes, W.3    Spaan, W.J.M.4    Snijder, E.J.5
  • 67
    • 0027515237 scopus 로고
    • The first zinc-binding domain of UvrA is not essential for UvrABC-mediated DNA excision repair
    • Visse, R., M. de Ruijter, M. Ubbink, J. A. Brandsma, and P. van de Putte. 1993. The first zinc-binding domain of UvrA is not essential for UvrABC-mediated DNA excision repair. Mutat. Res. 294:263-274.
    • (1993) Mutat. Res. , vol.294 , pp. 263-274
    • Visse, R.1    De Ruijter, M.2    Ubbink, M.3    Brandsma, J.A.4    Van De Putte, P.5
  • 68
    • 0030856299 scopus 로고    scopus 로고
    • Alternative proteolytic processing of the arterivirus replicase ORF1a polyprotein: Evidence that NSP2 acts as a cofactor for the NSP4 serine protease
    • Wassenaar, A. L. M., W. J. M. Spaan, A. E. Gorbalenya, and E. J. Snijder. 1997. Alternative proteolytic processing of the arterivirus replicase ORF1a polyprotein: evidence that NSP2 acts as a cofactor for the NSP4 serine protease. J. Virol. 71:9313-9322.
    • (1997) J. Virol. , vol.71 , pp. 9313-9322
    • Wassenaar, A.L.M.1    Spaan, W.J.M.2    Gorbalenya, A.E.3    Snijder, E.J.4
  • 69
    • 0026737363 scopus 로고
    • Systematic mutational analysis of the yeast ACT1 gene
    • Wertman, K. F., D. G. Drubin, and D. Botstein. 1992. Systematic mutational analysis of the yeast ACT1 gene. Genetics 132:337-350.
    • (1992) Genetics , vol.132 , pp. 337-350
    • Wertman, K.F.1    Drubin, D.G.2    Botstein, D.3
  • 70
    • 0023707039 scopus 로고
    • Cysteine residues in the zinc finger and amino acids adjacent to the finger are necessary for DNA binding by the LAC9 regulatory protein of Kluyveromyces lactis
    • Witte, M. M., and R. C. Dickson. 1988. Cysteine residues in the zinc finger and amino acids adjacent to the finger are necessary for DNA binding by the LAC9 regulatory protein of Kluyveromyces lactis. Mol. Cell. Biol. 8:3726-3733.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 3726-3733
    • Witte, M.M.1    Dickson, R.C.2
  • 71
    • 0025194603 scopus 로고
    • The C6 zinc finger and adjacent amino acids determine DNA-binding specificity and affinity in the yeast activator proteins LAC9 and PPR1
    • Witte, M. M., and R. C. Dickson. 1990. The C6 zinc finger and adjacent amino acids determine DNA-binding specificity and affinity in the yeast activator proteins LAC9 and PPR1. Mol. Cell. Biol. 10:5128-5137.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 5128-5137
    • Witte, M.M.1    Dickson, R.C.2
  • 72
    • 0023131381 scopus 로고
    • Characterization of a positive regulatory gene, LAC9, that controls induction of the lactose-galactose regulon of Kluyveromyces lactis: Structural and functional relationship to GAL4 of Saccharomyces cerevisiae
    • Wray, L. V., Jr., M. M. Witte, R. C. Dickson, and M. I. Riley. 1987 Characterization of a positive regulatory gene, LAC9, that controls induction of the lactose-galactose regulon of Kluyveromyces lactis: structural and functional relationship to GAL4 of Saccharomyces cerevisiae. Mol. Cell. Biol. 7:1111-1121.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 1111-1121
    • Wray L.V., Jr.1    Witte, M.M.2    Dickson, R.C.3    Riley, M.I.4
  • 73
    • 0028851686 scopus 로고
    • Effects of zinc finger mutations on the nucleic acid binding activities of Xenopus transcription factor IIIA
    • Zang, W. Q., N. Veldhoen, and P. J. Romaniuk. 1995. Effects of zinc finger mutations on the nucleic acid binding activities of Xenopus transcription factor IIIA. Biochemistry 34:15545-15552.
    • (1995) Biochemistry , vol.34 , pp. 15545-15552
    • Zang, W.Q.1    Veldhoen, N.2    Romaniuk, P.J.3


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