메뉴 건너뛰기




Volumn 80, Issue 8, 1999, Pages 1879-1888

Virus-encoded proteinases of the Togaviridae

Author keywords

[No Author keywords available]

Indexed keywords

PROTEINASE; VIRUS ENZYME; VIRUS PROTEIN;

EID: 0032772365     PISSN: 00221317     EISSN: None     Source Type: Journal    
DOI: 10.1099/0022-1317-80-8-1879     Document Type: Review
Times cited : (23)

References (72)
  • 2
    • 0018885514 scopus 로고
    • Partial amino acid sequences of sindbis and semliki forest virus-specific core proteins
    • Boege, U., Wengler, G. & Wittmann-Liebold, B. (1980). Partial amino acid sequences of Sindbis and Semliki Forest virus-specific core proteins. Virology 103, 178-190.
    • (1980) Virology , vol.103 , pp. 178-190
    • Boege, U.1    Wengler, G.2    Wittmann-Liebold, B.3
  • 3
    • 0019601764 scopus 로고
    • Primary structure of the core proteins of the alphaviruses semliki forest virus and sindbis virus
    • Boege, U., Wengler, G., Wengler, G. & Wittmann-Liebold, B. (1981). Primary structure of the core proteins of the alphaviruses Semliki Forest virus and Sindbis virus. Virology 113, 293-303.
    • (1981) Virology , vol.113 , pp. 293-303
    • Boege, U.1    Wengler, G.2    Wengler, G.3    Wittmann-Liebold, B.4
  • 4
    • 0031028291 scopus 로고    scopus 로고
    • Characterization of a second cleavage site and demonstration of activity in trans by the papain-like proteinase of the murine coronavirus mouse hepatitis virus strain A59
    • Bonilla, P. J., Hughes, S. A. & Weiss, S. R. (1997). Characterization of a second cleavage site and demonstration of activity in trans by the papain-like proteinase of the murine coronavirus mouse hepatitis virus strain A59. Journal of Virology 71, 900-909.
    • (1997) Journal of Virology , vol.71 , pp. 900-909
    • Bonilla, P.J.1    Hughes, S.A.2    Weiss, S.R.3
  • 5
    • 0024747611 scopus 로고
    • Autocatalytic processing of the potyvirus helper component proteinase in escherichia coli and in vitro
    • Carrington, J. C., Freed, D. D. & Sanders, T. C. (1989). Autocatalytic processing of the potyvirus helper component proteinase in Escherichia coli and in vitro. Journal of Virology 63, 4459-4463.
    • (1989) Journal of Virology , vol.63 , pp. 4459-4463
    • Carrington, J.C.1    Freed, D.D.2    Sanders, T.C.3
  • 6
    • 0029982325 scopus 로고    scopus 로고
    • Characterization of the rubella virus nonstructural protease domain and its cleavage site
    • Chen, J. P., Strauss, J. H., Strauss, E. G. & Frey, T. K. (1996). Characterization of the rubella virus nonstructural protease domain and its cleavage site. Journal of Virology 70, 4707-4713.
    • (1996) Journal of Virology , vol.70 , pp. 4707-4713
    • Chen, J.P.1    Strauss, J.H.2    Strauss, E.G.3    Frey, T.K.4
  • 7
    • 0025767921 scopus 로고
    • The autocatalytic protease p29 encoded by a hypo virulence-associated virus of the chestnut blight fungus resembles the poty virus-encoded protease HC-Pro
    • Choi, G. H., Pawlyk, D. M. & Nuss, D. L. (1991). The autocatalytic protease p29 encoded by a hypo virulence-associated virus of the chestnut blight fungus resembles the poty virus-encoded protease HC-Pro. Virology 183, 747-752.
    • (1991) Virology , vol.183 , pp. 747-752
    • Choi, G.H.1    Pawlyk, D.M.2    Nuss, D.L.3
  • 10
    • 0025352629 scopus 로고
    • Cleavage-site preferences of sindbis virus polyproteins containing the non-structural proteinase. Evidence for temporal regulation of polyprotein processing in vivo
    • de Groot, R. J., Hardy, W. R., Shirako, Y. & Strauss, J. H. (1990). Cleavage-site preferences of Sindbis virus polyproteins containing the non-structural proteinase. Evidence for temporal regulation of polyprotein processing in vivo. EMBO Journal 9, 2631-2638.
    • (1990) EMBO Journal , vol.9 , pp. 2631-2638
    • De Groot, R.J.1    Hardy, W.R.2    Shirako, Y.3    Strauss, J.H.4
  • 11
    • 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, S. G. & Sawicki, D. L (1996). Sindbis virus RNA-negative mutants that fail to convert from minus-strand to plus-strand synthesis: role of the nsP2 protein. Journal of Virology 70, 2706-2719.
    • (1996) Journal of Virology , vol.70 , pp. 2706-2719
    • Dé, I.1    Sawicki, S.G.2    Sawicki, D.L.3
  • 12
    • 0024315805 scopus 로고
    • Evidence that sindbis virus NSP2 is an autoprotease which processes the virus nonstructural polyprotein
    • Ding, M. X. & Schlesinger, M. J. (1989). Evidence that Sindbis virus NSP2 is an autoprotease which processes the virus nonstructural polyprotein. Virology 171, 280-284.
    • (1989) Virology , vol.171 , pp. 280-284
    • Ding, M.X.1    Schlesinger, M.J.2
  • 13
    • 0025287319 scopus 로고
    • Sequence of the genome RNA of rubella virus; evidence for genetic rearrangement during togavirus evolution
    • Dominguez, G., Wang, C.-Y. & Frey, T. K. (1990). Sequence of the genome RNA of rubella virus; evidence for genetic rearrangement during togavirus evolution. Virology 177, 225-238.
    • (1990) Virology , vol.177 , pp. 225-238
    • Dominguez, G.1    Wang, C.-Y.2    Frey, T.K.3
  • 14
    • 0027138172 scopus 로고
    • Expression of virus-encoded proteinases: Functional and structural similarities with cellular enzymes
    • Dougherty, W. G. & Semler, B. L. (1993). Expression of virus-encoded proteinases: functional and structural similarities with cellular enzymes. Microbiological Reviews 57, 781-822.
    • (1993) Microbiological Reviews , vol.57 , pp. 781-822
    • Dougherty, W.G.1    Semler, B.L.2
  • 15
    • 0025864149 scopus 로고
    • Both nonstructural proteins NS2B and NS3 are required for the proteolytic processing of dengue virus nonstructural proteins
    • Falgout, B., Pethel, M., Zhang, Y. M. & Lai, C. J. (1991). Both nonstructural proteins NS2B and NS3 are required for the proteolytic processing of dengue virus nonstructural proteins. Journal of Virology 65, 2467-2475.
    • (1991) Journal of Virology , vol.65 , pp. 2467-2475
    • Falgout, B.1    Pethel, M.2    Zhang, Y.M.3    Lai, C.J.4
  • 16
    • 0023904047 scopus 로고
    • Genome sequences of a mouse-avirulent and a mouse-virulent strain of Ross River virus
    • Faragher, S. G., Meek, A. D., Rice, C. M. & Dalgarno, L. (1988). Genome sequences of a mouse-avirulent and a mouse-virulent strain of Ross River virus. Virology 163, 509-526.
    • (1988) Virology , vol.163 , pp. 509-526
    • Faragher, S.G.1    Meek, A.D.2    Rice, C.M.3    Dalgarno, L.4
  • 17
    • 0025203579 scopus 로고
    • Identification of amino acids inserted during suppression of UAA and UGA termination codons at the gag-pol junction of moloney murine leukemia virus
    • Feng, Y.-X., Copeland, T. D., Oroszlan, S., Rein, A. & Levin, J. G. (1990). Identification of amino acids inserted during suppression of UAA and UGA termination codons at the gag-pol junction of Moloney murine leukemia virus. Proceedings of the National Academy of Sciences, USA 87, 8860-8863.
    • (1990) Proceedings of the National Academy of Sciences, USA , vol.87 , pp. 8860-8863
    • Feng, Y.-X.1    Copeland, T.D.2    Oroszlan, S.3    Rein, A.4    Levin, J.G.5
  • 18
    • 0028890264 scopus 로고
    • Identification of the rubella virus nonstructural proteins
    • Forng, R. Y. & Frey, T. K. (1995). Identification of the rubella virus nonstructural proteins. Virology 206, 843-853.
    • (1995) Virology , vol.206 , pp. 843-853
    • Forng, R.Y.1    Frey, T.K.2
  • 19
    • 0028028506 scopus 로고
    • Molecular biology of rubella virus
    • Frey, T. K. (1994). Molecular biology of rubella virus. Advances in Virus Research 44, 69-160.
    • (1994) Advances in Virus Research , vol.44 , pp. 69-160
    • Frey, T.K.1
  • 21
    • 0019300295 scopus 로고
    • Nudeotide sequence of cDNA coding for semliki forest virus membrane glycoproteins
    • Garoff, H., Frischauf, A. M., Simons, K., Lehrach, H. & Delius, H. (1980b). Nudeotide sequence of cDNA coding for Semliki Forest virus membrane glycoproteins. Nature 288, 236-241.
    • (1980) Nature , vol.288 , pp. 236-241
    • Garoff, H.1    Frischauf, A.M.2    Simons, K.3    Lehrach, H.4    Delius, H.5
  • 22
    • 0023770852 scopus 로고
    • Evolution of plus-strand RNA viruses
    • Goldbach, R. & Wellink, J. (1988). Evolution of plus-strand RNA viruses. Intervirology 29, 260-267.
    • (1988) Intervirology , vol.29 , pp. 260-267
    • Goldbach, R.1    Wellink, J.2
  • 24
    • 0025739985 scopus 로고
    • Putative papain-related thiol proteases of positive-strand RNA viruses. Identification of rubi-and aphthovirus proteases and delineation of a novel conserved domain associated with proteases of rubi-, alpha-and corona viruses
    • Gorbalenya, A. E., Koonin, E. V. & Lai, M. M. (1991). Putative papain-related thiol proteases of positive-strand RNA viruses. Identification of rubi-and aphthovirus proteases and delineation of a novel conserved domain associated with proteases of rubi-, alpha-and corona viruses. FEBS Letters 288, 201-205.
    • (1991) FEBS Letters , vol.288 , pp. 201-205
    • Gorbalenya, A.E.1    Koonin, E.V.2    Lai, M.M.3
  • 25
    • 0025352036 scopus 로고
    • Site-directed mutagenesis of the proposed catalytic amino acids of the sindbis virus capsid protein autoprotease
    • Hahn, C. S. & Strauss, J. H. (1990). Site-directed mutagenesis of the proposed catalytic amino acids of the Sindbis virus capsid protein autoprotease. Journal of Virology 64, 3069-3073.
    • (1990) Journal of Virology , vol.64 , pp. 3069-3073
    • Hahn, C.S.1    Strauss, J.H.2
  • 27
    • 0024358586 scopus 로고
    • Mapping of RNA-temperature sensitive mutants of sindbis virus: Assignment of complementation groups A, B, and G to nonstructural proteins
    • Hahn, Y. S., Strauss, E. G. & Strauss, J. H. (1989). Mapping of RNA-temperature sensitive mutants of Sindbis virus: assignment of complementation groups A, B, and G to nonstructural proteins. Journal of Virology 63, 3142-3150.
    • (1989) Journal of Virology , vol.63 , pp. 3142-3150
    • Hahn, Y.S.1    Strauss, E.G.2    Strauss, J.H.3
  • 28
    • 0024421374 scopus 로고
    • Processing the nonstructural poly proteins of sindbis virus: Nonstructural proteinase is in the C-terminal half of nsP2 and functions both in cis and in trans
    • Hardy, W. R. & Strauss, J. H. (1989). Processing the nonstructural poly proteins of Sindbis virus: nonstructural proteinase is in the C-terminal half of nsP2 and functions both in cis and in trans. Journal of Virology 63, 4653-4664.
    • (1989) Journal of Virology , vol.63 , pp. 4653-4664
    • Hardy, W.R.1    Strauss, J.H.2
  • 29
    • 0025277442 scopus 로고
    • Synthesis and processing of the nonstructural polyproteins of several temperature-sensitive mutants of sindbis virus
    • Hardy, W. R., Hahn, Y. S., de Groot, R. J., Strauss, E. G. & Strauss, J. H. (1990). Synthesis and processing of the nonstructural polyproteins of several temperature-sensitive mutants of Sindbis virus. Virology 177, 199-208.
    • (1990) Virology , vol.177 , pp. 199-208
    • Hardy, W.R.1    Hahn, Y.S.2    De Groot, R.J.3    Strauss, E.G.4    Strauss, J.H.5
  • 30
    • 0028813105 scopus 로고
    • Identification of the murine coronavirus p28 cleavage site
    • Hughes, S. A., Bonilla, P. J. & Weiss, S. R. (1995). Identification of the murine coronavirus p28 cleavage site. Journal of Virology 69, 809-813.
    • (1995) Journal of Virology , vol.69 , pp. 809-813
    • Hughes, S.A.1    Bonilla, P.J.2    Weiss, S.R.3
  • 31
    • 0019601001 scopus 로고
    • Radio-sequence analysis of in vivo multilabeled nonstructural protein ns86 of semliki forest virus
    • Kalkkinen, N., Laaksonen, M., Soderiund, H. & Jornvall, H. (1981). Radio-sequence analysis of in vivo multilabeled nonstructural protein ns86 of Semliki Forest virus. Virology 113, 188-195.
    • (1981) Virology , vol.113 , pp. 188-195
    • Kalkkinen, N.1    Laaksonen, M.2    Soderiund, H.3    Jornvall, H.4
  • 33
    • 0024547862 scopus 로고
    • The full-length nucleotide sequences of the virulent trinidad donkey strain of venezuelan equine encephalitis virus and its attenuated vaccine derivative, strain TC-83
    • Kinney, R. M., Johnson, B. J., Welch, J. B., Tsuchiya, K. R. & Trent, D. W. (1989). The full-length nucleotide sequences of the virulent Trinidad donkey strain of Venezuelan equine encephalitis virus and its attenuated vaccine derivative, strain TC-83. Virology 170, 19-30.
    • (1989) Virology , vol.170 , pp. 19-30
    • Kinney, R.M.1    Johnson, B.J.2    Welch, J.B.3    Tsuchiya, K.R.4    Trent, D.W.5
  • 34
    • 0027504136 scopus 로고
    • Evolution and taxonomy of positive-strand RNA viruses: Implications of comparative analysis of amino acid sequences
    • Koonin, E. V. & Dolja, V. V. (1993). Evolution and taxonomy of positive-strand RNA viruses: implications of comparative analysis of amino acid sequences. Critical Reviews in Biochemistry and Molecular Biology 28, 375-430.
    • (1993) Critical Reviews in Biochemistry and Molecular Biology , vol.28 , pp. 375-430
    • Koonin, E.V.1    Dolja, V.V.2
  • 35
    • 0027463085 scopus 로고
    • Assembly of functional sindbis virus RNA replication complexes: Requirement for coexpression of P123 and p34
    • Lemm, J. A. & Rice, C. M. (1993a). Assembly of functional Sindbis virus RNA replication complexes: requirement for coexpression of P123 and P34. Journal of Virology 67, 1905-1915.
    • (1993) Journal of Virology , vol.67 , pp. 1905-1915
    • Lemm, J.A.1    Rice, C.M.2
  • 36
    • 0027475009 scopus 로고
    • Roles of nonstructural polyproteins and cleavage products in regulating sindbis virus RNA replication and transcription
    • Lemm, J. A. & Rice, C. M. (1993b). Roles of nonstructural polyproteins and cleavage products in regulating Sindbis virus RNA replication and transcription. Journal of Virology 67, 1916-1926.
    • (1993) Journal of Virology , vol.67 , pp. 1916-1926
    • Lemm, J.A.1    Rice, C.M.2
  • 37
    • 0028221438 scopus 로고
    • Polypeptide requirements for assembly of functional sindbis virus replication complexes: A model for the temporal regulation of minus-and plus-strand RNA synthesis
    • Lemm, J. A., Rumenapf, T., Strauss, E. G., Strauss, J. H. & Rice, C. M. (1994). Polypeptide requirements for assembly of functional Sindbis virus replication complexes: a model for the temporal regulation of minus-and plus-strand RNA synthesis. EMBO Journal 13, 2925-2934.
    • (1994) EMBO Journal , vol.13 , pp. 2925-2934
    • Lemm, J.A.1    Rumenapf, T.2    Strauss, E.G.3    Strauss, J.H.4    Rice, C.M.5
  • 38
    • 0031878237 scopus 로고    scopus 로고
    • Template-dependent initiation of sindbis virus RNA replication in vitro
    • Lemm, J. A., Bergqvist, A., Read, C. M. & Rice, C. M. (1998). Template-dependent initiation of Sindbis virus RNA replication in vitro. Journal of Virology 72, 6546-6553.
    • (1998) Journal of Virology , vol.72 , pp. 6546-6553
    • Lemm, J.A.1    Bergqvist, A.2    Read, C.M.3    Rice, C.M.4
  • 39
    • 0025268737 scopus 로고
    • Complete sequence of the genomic RNA of o'nyong-nyong virus and its use in the construction of alphavirus phylogenetic trees
    • Levinson, R. S., Strauss, J. H. & Strauss, E. G. (1990). Complete sequence of the genomic RNA of o'nyong-nyong virus and its use in the construction of alphavirus phylogenetic trees. Virology 175, 110-123.
    • (1990) Virology , vol.175 , pp. 110-123
    • Levinson, R.S.1    Strauss, J.H.2    Strauss, E.G.3
  • 40
    • 0027313140 scopus 로고
    • The signal for translational readthrough of a UGA codon in sindbis virus RNA involves a single cytidine residue immediately downstream of the termination codon
    • Li, G. & Rice, C. M. (1993). The signal for translational readthrough of a UGA codon in Sindbis virus RNA involves a single cytidine residue immediately downstream of the termination codon. Journal of Virology 67, 5062-5067.
    • (1993) Journal of Virology , vol.67 , pp. 5062-5067
    • Li, G.1    Rice, C.M.2
  • 41
    • 0031977295 scopus 로고    scopus 로고
    • The rubella virus nonstructural protease requires divalent cations for activity and functions in trans
    • Liu, X., Ropp, S. L., Jackson, R. J. & Frey, T. K. (1998). The rubella virus nonstructural protease requires divalent cations for activity and functions in trans. Journal of Virology 72, 4463-4466.
    • (1998) Journal of Virology , vol.72 , pp. 4463-4466
    • Liu, X.1    Ropp, S.L.2    Jackson, R.J.3    Frey, T.K.4
  • 42
    • 0030592514 scopus 로고    scopus 로고
    • The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site
    • Love, R. A., Parge, H. E., Wickersham, J. A., Hostomsky, Z., Habuka, N., Moomaw, E. W., Adachi, T. & Hostomska, Z. (1996). The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site. Cell 87, 331-42.
    • (1996) Cell , vol.87 , pp. 331-342
    • Love, R.A.1    Parge, H.E.2    Wickersham, J.A.3    Hostomsky, Z.4    Habuka, N.5    Moomaw, E.W.6    Adachi, T.7    Hostomska, Z.8
  • 43
    • 0028261083 scopus 로고
    • Expression of the rubella virus nonstructural protein ORF and demonstration of proteolytic processing
    • Marr, L. D., Wang, C. Y. & Frey, T. K. (1994). Expression of the rubella virus nonstructural protein ORF and demonstration of proteolytic processing. Virology 198, 586-592.
    • (1994) Virology , vol.198 , pp. 586-592
    • Marr, L.D.1    Wang, C.Y.2    Frey, T.K.3
  • 44
    • 0023275581 scopus 로고
    • Processing of the semliki forest virus structural polyprotein: Role of the capsid protease
    • Melancon, P. & Garoff, H. (1987). Processing of the Semliki Forest virus structural polyprotein: role of the capsid protease. Journal of Virology 61, 1301-1309.
    • (1987) Journal of Virology , vol.61 , pp. 1301-1309
    • Melancon, P.1    Garoff, H.2
  • 45
    • 0026794755 scopus 로고
    • A regulatory role for the 32K protein in proteolytic processing of cowpea mosaic virus polyproteins
    • Peters, S. A., Voorhorst, W. G., Wery, J., Wellink, J. & van Kammen, A. (1992). A regulatory role for the 32K protein in proteolytic processing of cowpea mosaic virus polyproteins. Virology 191, 81-89.
    • (1992) Virology , vol.191 , pp. 81-89
    • Peters, S.A.1    Voorhorst, W.G.2    Wery, J.3    Wellink, J.4    Van Kammen, A.5
  • 46
    • 0031060534 scopus 로고    scopus 로고
    • Improvement of the specific infectivity of the rubella virus (RUB) infectious clone: Determinants of cytopathogenicity induced by RUB map to the nonstructural proteins
    • Pugachev, K. V., Abernathy, E. S. & Frey, T. K. (1997). Improvement of the specific infectivity of the rubella virus (RUB) infectious clone: determinants of cytopathogenicity induced by RUB map to the nonstructural proteins. Journal of Virology 71, 562-568.
    • (1997) Journal of Virology , vol.71 , pp. 562-568
    • Pugachev, K.V.1    Abernathy, E.S.2    Frey, T.K.3
  • 47
    • 0028989915 scopus 로고
    • Aura virus is a new world representative of sindbis-like viruses
    • Rumenapf, T., Strauss, E. G. & Strauss, J. H. (1995). Aura virus is a New World representative of Sindbis-like viruses. Virology 208, 621-633.
    • (1995) Virology , vol.208 , pp. 621-633
    • Rumenapf, T.1    Strauss, E.G.2    Strauss, J.H.3
  • 48
    • 0030887314 scopus 로고    scopus 로고
    • Virus-encoded proteinases of the picornavirus super-group
    • Ryan, M. D. & Flint, M. (1997). Virus-encoded proteinases of the picornavirus super-group. Journal of General Virology 78, 699-723.
    • (1997) Journal of General Virology , vol.78 , pp. 699-723
    • Ryan, M.D.1    Flint, M.2
  • 50
    • 0027166774 scopus 로고
    • A second nonstructural protein functions in the regulation of alphavirus negative-strand RNA synthesis
    • Sawicki, D. L. & Sawicki, S. G. (1993). A second nonstructural protein functions in the regulation of alphavirus negative-strand RNA synthesis. Journal of Virology 67, 3605-3610.
    • (1993) Journal of Virology , vol.67 , pp. 3605-3610
    • Sawicki, D.L.1    Sawicki, S.G.2
  • 51
    • 0028319950 scopus 로고
    • Alphavirus positive and negative strand RNA synthesis and the role of polyproteins in formation of viral replication complexes
    • Sawicki, D. L. & Sawicki, S. G. (1994). Alphavirus positive and negative strand RNA synthesis and the role of polyproteins in formation of viral replication complexes. Archives of Virology Suppl. 9, 393-405.
    • (1994) Archives of Virology Suppl. , vol.9 , pp. 393-405
    • Sawicki, D.L.1    Sawicki, S.G.2
  • 52
    • 0026054706 scopus 로고
    • Gene expression by a hypovirulence-associated virus of the chestnut blight fungus involves two papain-like protease activities. Essential residues and cleavage site requirements for p48 autoproteolysis
    • Shapira, R. & Nuss, D. L. (1991). Gene expression by a hypovirulence-associated virus of the chestnut blight fungus involves two papain-like protease activities. Essential residues and cleavage site requirements for p48 autoproteolysis. Journal of Biological Chemistry 266, 19419-19425.
    • (1991) Journal of Biological Chemistry , vol.266 , pp. 19419-19425
    • Shapira, R.1    Nuss, D.L.2
  • 53
    • 0025336486 scopus 로고
    • Cleavage between nsP1 and nsP2 initiates the processing pathway of sindbis virus nonstructural polyprotein P123
    • Shirako, Y. & Strauss, J. H. (1990). Cleavage between nsP1 and nsP2 initiates the processing pathway of Sindbis virus nonstructural polyprotein P123. Virology 177, 54-64.
    • (1990) Virology , vol.177 , pp. 54-64
    • Shirako, Y.1    Strauss, J.H.2
  • 54
    • 0025755356 scopus 로고
    • Structure of the ockelbo virus genome and its relationship to other sindbis viruses
    • Shirako, Y., Niklasson, B., Dalrymple, J. M., Strauss, E. G. & Strauss, J. H. (1991). Structure of the Ockelbo virus genome and its relationship to other Sindbis viruses. Virology 182, 753-764.
    • (1991) Virology , vol.182 , pp. 753-764
    • Shirako, Y.1    Niklasson, B.2    Dalrymple, J.M.3    Strauss, E.G.4    Strauss, J.H.5
  • 56
    • 0028067318 scopus 로고
    • Proteolytic processing of the replicase ORF1a protein of equine arteritis virus
    • Snijder, E. J., Wassenaar, A. L. & Spaan, W. J. (1994). Proteolytic processing of the replicase ORF1a protein of equine arteritis virus. Journal of Virology 68, 5755-5764.
    • (1994) Journal of Virology , vol.68 , pp. 5755-5764
    • Snijder, E.J.1    Wassenaar, A.L.2    Spaan, W.J.3
  • 57
    • 0028080452 scopus 로고
    • The 2A proteinase of human rhinovirus is a zinc containing enzyme
    • Sommergruber, W., Casari, G., Fessl, F., Seipelt, J. & Skem, T. (1994). The 2A proteinase of human rhinovirus is a zinc containing enzyme. Virology 204, 815-818.
    • (1994) Virology , vol.204 , pp. 815-818
    • Sommergruber, W.1    Casari, G.2    Fessl, F.3    Seipelt, J.4    Skem, T.5
  • 58
    • 0028088152 scopus 로고
    • The alphaviruses: Gene expression, replication, and evolution
    • Strauss, J. H. & Strauss, E. G. (1994). The alphaviruses: gene expression, replication, and evolution. Microbiological Reviews 58, 491-562.
    • (1994) Microbiological Reviews , vol.58 , pp. 491-562
    • Strauss, J.H.1    Strauss, E.G.2
  • 60
    • 0021319456 scopus 로고
    • Complete nucleotide sequence of the genomic RNA of sindbis virus
    • Strauss, E. G., Rice, C. M. & Strauss, J. H. (1984). Complete nucleotide sequence of the genomic RNA of Sindbis virus. Virology 133, 92-110.
    • (1984) Virology , vol.133 , pp. 92-110
    • Strauss, E.G.1    Rice, C.M.2    Strauss, J.H.3
  • 61
    • 0027067063 scopus 로고
    • Identification of the active site residues in the nsP2 proteinase of sindbis virus
    • Strauss, E. G., De Groot, R. J., Levinson, R. & Strauss, J. H. (1992). Identification of the active site residues in the nsP2 proteinase of Sindbis virus. Virology 191, 932-940.
    • (1992) Virology , vol.191 , pp. 932-940
    • Strauss, E.G.1    De Groot, R.J.2    Levinson, R.3    Strauss, J.H.4
  • 63
    • 0023056888 scopus 로고
    • Complete nucleotide sequence of the nonstructural protein genes of semliki forest virus
    • Takkinen, K. (1986). Complete nucleotide sequence of the nonstructural protein genes of Semliki Forest virus. Nucleic Acids Research 14, 5667-5682.
    • (1986) Nucleic Acids Research , vol.14 , pp. 5667-5682
    • Takkinen, K.1
  • 65
    • 0025771072 scopus 로고
    • Proteolytic processing of semliki forest virus-specific non-structural polyprotein
    • Takkinen, K., Peranen, J. & Kaariainen, L. (1991). Proteolytic processing of Semliki Forest virus-specific non-structural polyprotein. Journal of General Virology 72, 1627-1633.
    • (1991) Journal of General Virology , vol.72 , pp. 1627-1633
    • Takkinen, K.1    Peranen, J.2    Kaariainen, L.3
  • 66
    • 0027474021 scopus 로고
    • Refined structure of sindbis virus core protein and comparison with other chymotrypsin-like serine proteinase structures
    • Tong, L., Wengler, G. & Rossmann, M. G. (1993). Refined structure of Sindbis virus core protein and comparison with other chymotrypsin-like serine proteinase structures. Journal of Molecular Biology 230, 228-247.
    • (1993) Journal of Molecular Biology , vol.230 , pp. 228-247
    • Tong, L.1    Wengler, G.2    Rossmann, M.G.3
  • 68
    • 0024296384 scopus 로고
    • Two viral proteins involved in the proteolytic processing of the cowpea mosaic virus polyproteins
    • Vos, P., Verver, J., Jaegle, M., Wellink, J., van Kammen, A. & Goldbach, R. (1988). Two viral proteins involved in the proteolytic processing of the cowpea mosaic virus polyproteins. Nucleic Acids Research 16, 1967-1985.
    • (1988) Nucleic Acids Research , vol.16 , pp. 1967-1985
    • Vos, P.1    Verver, J.2    Jaegle, M.3    Wellink, J.4    Van Kammen, A.5    Goldbach, R.6
  • 69
    • 0028846684 scopus 로고
    • Spectroscopic characterization of rhinoviral protease 2A: Zn is essential for the structural integrity
    • Voss, T., Meyer, R. & Sommergruber, W. (1995). Spectroscopic characterization of rhinoviral protease 2A: Zn is essential for the structural integrity. Protein Science 4, 2526-2531.
    • (1995) Protein Science , vol.4 , pp. 2526-2531
    • Voss, T.1    Meyer, R.2    Sommergruber, W.3
  • 70
    • 0028040383 scopus 로고
    • Alphavirus nsP3 functions to form replication complexes transcribing negative-strand RNA
    • Wang, Y.-F., Sawiki, S. G. & Sawiki, D. L. (1994). Alphavirus nsP3 functions to form replication complexes transcribing negative-strand RNA. Journal of Virology 68, 6466-6475.
    • (1994) Journal of Virology , vol.68 , pp. 6466-6475
    • Wang, Y.-F.1    Sawiki, S.G.2    Sawiki, D.L.3
  • 72
    • 0032551237 scopus 로고    scopus 로고
    • Proteolytic processing of rubella virus nonstructural proteins
    • Yao, J., Yang, D., Chong, P., Hwang, D., Liang, Y. & Gillam, S. (1998). Proteolytic processing of rubella virus nonstructural proteins. Virology 246, 74-82.
    • (1998) Virology , vol.246 , pp. 74-82
    • Yao, J.1    Yang, D.2    Chong, P.3    Hwang, D.4    Liang, Y.5    Gillam, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.