메뉴 건너뛰기




Volumn 234, Issue 2, 1997, Pages 203-214

Mutational analyses support a model for the HRV2 2A proteinase

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE PROTEINASE; ELASTASE; SERINE PROTEINASE; VIRUS PROTEIN; ZINC;

EID: 0030854488     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1997.8595     Document Type: Article
Times cited : (18)

References (41)
  • 1
    • 0028328469 scopus 로고
    • Picornaviral 3C cysteine proteinase have a fold similar to chymotrypsin-like serine proteinases
    • Allaire M., Chernaia M. M., Malcolm B. A., James M. N. G. Picornaviral 3C cysteine proteinase have a fold similar to chymotrypsin-like serine proteinases. Nature. 369:1994;72-76.
    • (1994) Nature , vol.369 , pp. 72-76
    • Allaire, M.1    Chernaia, M.M.2    Malcolm, B.A.3    James, M.N.G.4
  • 2
    • 0021770918 scopus 로고
    • Similarity in gene organization and homology between proteins of animal picornaviruses and a plant comovirus suggest common ancestry of these virus families
    • Argos P., Kamer G., Nicklin M. J. H., Wimmer E. Similarity in gene organization and homology between proteins of animal picornaviruses and a plant comovirus suggest common ancestry of these virus families. Nucleic Acids Res. 12:1984;7251-7267.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 7251-7267
    • Argos, P.1    Kamer, G.2    Nicklin, M.J.H.3    Wimmer, E.4
  • 3
    • 0000686943 scopus 로고
    • Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: Structural and functional implications
    • Bazan J. F., Fletterick R. J. Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: Structural and functional implications. Proc. Natl. Acad. Sci. USA. 85:1988;7872-7876.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7872-7876
    • Bazan, J.F.1    Fletterick, R.J.2
  • 4
    • 0021994338 scopus 로고
    • Internal homology in the primary structure of the poliovirus polyprotein: The possibility of existence of two viral proteinases
    • Blinov V. M., Donchenko A. P., Gorbalenya A. E. Internal homology in the primary structure of the poliovirus polyprotein: The possibility of existence of two viral proteinases. Lectures Acad. Sci. USSR. 281:1985;984-987.
    • (1985) Lectures Acad. Sci. USSR , vol.281 , pp. 984-987
    • Blinov, V.M.1    Donchenko, A.P.2    Gorbalenya, A.E.3
  • 5
    • 0025273933 scopus 로고
    • Site-directed mutagenesis suggests close functional relationship between human rhinovirus 3C cysteine protease and cellular trypsin-like serine proteases
    • Cheah K. C., Leong L. E. C., Porter A. G. Site-directed mutagenesis suggests close functional relationship between human rhinovirus 3C cysteine protease and cellular trypsin-like serine proteases. J. Biol. Chem. 265:1990;7180-7187.
    • (1990) J. Biol. Chem. , vol.265 , pp. 7180-7187
    • Cheah, K.C.1    Leong, L.E.C.2    Porter, A.G.3
  • 6
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux J., Haeberli P., Smithies O. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12:1984;387-395.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 7
    • 0022570578 scopus 로고
    • Poliovirus-encoded proteinase 3C: A possible evolutionary link between cellular serine and cysteine proteinase families
    • Gorbalenya A. E., Blinov V. M., Donchenko A. M. Poliovirus-encoded proteinase 3C: A possible evolutionary link between cellular serine and cysteine proteinase families. FEBS Lett. 194:1986;253-257.
    • (1986) FEBS Lett. , vol.194 , pp. 253-257
    • Gorbalenya, A.E.1    Blinov, V.M.2    Donchenko, A.M.3
  • 8
    • 0024495898 scopus 로고
    • Cysteine proteases of positive strand RNA viruses and chymotrypsin-like serine proteases: A distinct protein superfamily with a common structural fold
    • Gorbalenya A. E., Donchenko A. P., Blinov V. M., Koonin E. V. Cysteine proteases of positive strand RNA viruses and chymotrypsin-like serine proteases: A distinct protein superfamily with a common structural fold. FEBS Lett. 243:1989;103-114.
    • (1989) FEBS Lett. , vol.243 , pp. 103-114
    • Gorbalenya, A.E.1    Donchenko, A.P.2    Blinov, V.M.3    Koonin, E.V.4
  • 9
    • 0019971712 scopus 로고
    • Proteolytic processing of poliovirus polypeptides: Antibodies to a polypeptide P3-7c inhibit cleavage at glutamine-glycine pairs
    • Hanecak R., Semler B., Anderson C. W., Wimmer E. Proteolytic processing of poliovirus polypeptides: Antibodies to a polypeptide P3-7c inhibit cleavage at glutamine-glycine pairs. Proc. Natl. Acad. Sci. USA. 79:1982;3973-3977.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 3973-3977
    • Hanecak, R.1    Semler, B.2    Anderson, C.W.3    Wimmer, E.4
  • 10
    • 0024830949 scopus 로고
    • Proteolytic processing of polyproteins in the replication of RNA viruses
    • Hellen C. U. T., Kräusslich H.-G., Wimmer E. Proteolytic processing of polyproteins in the replication of RNA viruses. Biochemistry. 28:1989;9881-9890.
    • (1989) Biochemistry , vol.28 , pp. 9881-9890
    • Hellen, C.U.T.1    Kräusslich, H.-G.2    Wimmer, E.3
  • 11
    • 0026210210 scopus 로고
    • Characterization of poliovirus 2A proteinase by mutational analysis: Residues required for autocatalytic activity are essential for induction of cleavage of eukaryotic initiation factor 4F polypeptide p220
    • Hellen C. U. T., Fäcke M., Kräusslich H.-G., Lee C.-K., Wimmer E. Characterization of poliovirus 2A proteinase by mutational analysis: Residues required for autocatalytic activity are essential for induction of cleavage of eukaryotic initiation factor 4F polypeptide p220. J. Virol. 65:1991;4226-4231.
    • (1991) J. Virol. , vol.65 , pp. 4226-4231
    • Hellen, C.U.T.1    Fäcke, M.2    Kräusslich, H.-G.3    Lee, C.-K.4    Wimmer, E.5
  • 13
    • 0025248761 scopus 로고
    • Limited expression of poliovirus by vaccinia virus recombinants due to inhibition of the vector by proteinase 2A
    • Jewell J. E., Ball L. A., Rueckert R. Limited expression of poliovirus by vaccinia virus recombinants due to inhibition of the vector by proteinase 2A. J. Virol. 64:1990;1388-1393.
    • (1990) J. Virol. , vol.64 , pp. 1388-1393
    • Jewell, J.E.1    Ball, L.A.2    Rueckert, R.3
  • 15
    • 0023201040 scopus 로고
    • Poliovirus proteinase 2A induces cleavge of eukaryontic initiation factor 4F polypeptide p220
    • Kräusslich H.-G., Nicklin M. J. H., Toyoda H., Etchison D., Wimmer E. Poliovirus proteinase 2A induces cleavge of eukaryontic initiation factor 4F polypeptide p220. J. Virol. 61:1987;2711-2718.
    • (1987) J. Virol. , vol.61 , pp. 2711-2718
    • Kräusslich, H.-G.1    Nicklin, M.J.H.2    Toyoda, H.3    Etchison, D.4    Wimmer, E.5
  • 16
    • 0020475449 scopus 로고
    • A simple method for describing the hydropathic character of a protein
    • Kyte J., Doolittle R. F. A simple method for describing the hydropathic character of a protein. J. Mol. Biol. 157:1982;105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 17
    • 0027182923 scopus 로고
    • Mapping the cleavage site in protein synthesis initation factor eIF-4γ of the 2A proteases from human coxsackievirus and rhinovirus
    • Lamphear B. J., Yan R., Yang F., Waters D., Liebig H.-D., Klump H., Kuechler E., Skern T., Rhoads R. E. Mapping the cleavage site in protein synthesis initation factor eIF-4γ of the 2A proteases from human coxsackievirus and rhinovirus. J. Biol. Chem. 268:1993;19200-19203.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19200-19203
    • Lamphear, B.J.1    Yan, R.2    Yang, F.3    Waters, D.4    Liebig, H.-D.5    Klump, H.6    Kuechler, E.7    Skern, T.8    Rhoads, R.E.9
  • 19
    • 0023192733 scopus 로고
    • Restriction of translation of capped mRNA in vitro as a model for poliovirus-induced inhibition of host cell protein synthesis: Relationship to p220 claevage
    • Lloyd R. E., Jense H. G., Ehrenfeld E. Restriction of translation of capped mRNA in vitro as a model for poliovirus-induced inhibition of host cell protein synthesis: Relationship to p220 claevage. J. Virol. 61:1987;2480-2488.
    • (1987) J. Virol. , vol.61 , pp. 2480-2488
    • Lloyd, R.E.1    Jense, H.G.2    Ehrenfeld, E.3
  • 20
    • 0028971177 scopus 로고
    • Analysis of picornavirus 2A(pro) proteins: Separation of proteinase from translation and replication functions
    • Lu H. H., Li X., Cuconati A., Wimmer E. Analysis of picornavirus 2A(pro) proteins: Separation of proteinase from translation and replication functions. J. Virol. 69:1995;7445-7452.
    • (1995) J. Virol. , vol.69 , pp. 7445-7452
    • Lu, H.H.1    Li, X.2    Cuconati, A.3    Wimmer, E.4
  • 23
    • 0002104779 scopus 로고
    • Structure of native porcine pancreatic elastase at 1.65 angstroms resolution
    • Meyer E., Cole G., Radhakrishnan R., Epp O. Structure of native porcine pancreatic elastase at 1.65 angstroms resolution. Acta Crystallogr. 44:1988;26-30.
    • (1988) Acta Crystallogr. , vol.44 , pp. 26-30
    • Meyer, E.1    Cole, G.2    Radhakrishnan, R.3    Epp, O.4
  • 24
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K. A., Honig B. Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins. 11:1991;281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 25
    • 0001952393 scopus 로고
    • Picornaviridae and Their Replication
    • New York: Raven Press. p. 507-548
    • Rueckert R. R. Picornaviridae and Their Replication. Fields Virology. 1990;Raven Press, New York. p. 507-548.
    • (1990) Fields Virology
    • Rueckert, R.R.1
  • 26
    • 0028457594 scopus 로고
    • Zinc mining for protein domains
    • Schwabe J. W. R., Klug A. Zinc mining for protein domains. J. Struct. Biol. 1:1994;345-349.
    • (1994) J. Struct. Biol. , vol.1 , pp. 345-349
    • Schwabe, J.W.R.1    Klug, A.2
  • 28
    • 0023132444 scopus 로고
    • A neutralizing epitope on human rhinovirus type 2 includes amino acid residues between 153 and 164 of virus capsid protein VP2
    • Skern T., Neubauer CH., Frasel L., Gruendler P., Sommergruber W., Zorn M., Kuechler E., Blaas D. A neutralizing epitope on human rhinovirus type 2 includes amino acid residues between 153 and 164 of virus capsid protein VP2. J. Gen. Virol. 68:1987;315-323.
    • (1987) J. Gen. Virol. , vol.68 , pp. 315-323
    • Skern, T.1    Neubauer, C.H.2    Frasel, L.3    Gruendler, P.4    Sommergruber, W.5    Zorn, M.6    Kuechler, E.7    Blaas, D.8
  • 33
    • 0028080452 scopus 로고
    • The 2A proteinase of human rhinovirus is a zinc containing enzyme
    • Sommergruber W., Casari G., Fessl F., Seipelt J., Skern T. The 2A proteinase of human rhinovirus is a zinc containing enzyme. Virology. 204:1994b;815-818.
    • (1994) Virology , vol.204 , pp. 815-818
    • Sommergruber, W.1    Casari, G.2    Fessl, F.3    Seipelt, J.4    Skern, T.5
  • 34
    • 0022648673 scopus 로고
    • Characterization of foot-and-mouth disease gene products with antisera against bacterially synthesised fusion proteins
    • Strebel K., Beck E., Strohmaier K., Schaller H. Characterization of foot-and-mouth disease gene products with antisera against bacterially synthesised fusion proteins. J. Virol. 57:1986;983-991.
    • (1986) J. Virol. , vol.57 , pp. 983-991
    • Strebel, K.1    Beck, E.2    Strohmaier, K.3    Schaller, H.4
  • 35
    • 0025122797 scopus 로고
    • Determination of sulfhydryl groups and disulfide bonds in a protein by polyacrylamide gel-electrophoresis
    • Takahashi N., Hirose M. Determination of sulfhydryl groups and disulfide bonds in a protein by polyacrylamide gel-electrophoresis. Anal. Biochem. 188:1990;359-365.
    • (1990) Anal. Biochem. , vol.188 , pp. 359-365
    • Takahashi, N.1    Hirose, M.2
  • 36
    • 0023043280 scopus 로고
    • A second virus-encoded proteinase involved in proteolytic processing of poliovirus polyprotein
    • Toyoda H., Nicklin M. J. H., Murray M. G., Anderson C. W., Dunn J. J., Studier F. W., Wimmer E. A second virus-encoded proteinase involved in proteolytic processing of poliovirus polyprotein. Cell. 45:1986;761-770.
    • (1986) Cell , vol.45 , pp. 761-770
    • Toyoda, H.1    Nicklin, M.J.H.2    Murray, M.G.3    Anderson, C.W.4    Dunn, J.J.5    Studier, F.W.6    Wimmer, E.7
  • 37
    • 0024077061 scopus 로고
    • Protein 3CD is the major poliovirus proteinase responsible for cleavage of the P1 capsid precursor
    • Ypma-Wong M. F., Dewalt P. G., Johnson V. H., Lamb J. G., Semler B. Protein 3CD is the major poliovirus proteinase responsible for cleavage of the P1 capsid precursor. Virology. 166:1988;265-270.
    • (1988) Virology , vol.166 , pp. 265-270
    • Ypma-Wong, M.F.1    Dewalt, P.G.2    Johnson, V.H.3    Lamb, J.G.4    Semler, B.5
  • 38
    • 0026463868 scopus 로고
    • Amino acid sequence of the human protein synthesis initiation factor eIF-4γ
    • Yan R., Rychlik W., Etchison D., Rhoads R. Amino acid sequence of the human protein synthesis initiation factor eIF-4γ J. Biol. Chem. 267:1992;23226-23231.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23226-23231
    • Yan, R.1    Rychlik, W.2    Etchison, D.3    Rhoads, R.4
  • 39
    • 0025825159 scopus 로고
    • Identification of essential amino acid residues in the functional activity of poliovirus 2A protease
    • Yu S. F., Lloyd R. E. Identification of essential amino acid residues in the functional activity of poliovirus 2A protease. Virology. 182:1991;615-625.
    • (1991) Virology , vol.182 , pp. 615-625
    • Yu, S.F.1    Lloyd, R.E.2
  • 40
    • 0026606515 scopus 로고
    • Characterization of the roles of conserved cysteine and histidine residues in poliovirus 2A protease
    • Yu S., Lloyd R. E. Characterization of the roles of conserved cysteine and histidine residues in poliovirus 2A protease. Virology. 186:1992;725-735.
    • (1992) Virology , vol.186 , pp. 725-735
    • Yu, S.1    Lloyd, R.E.2
  • 41
    • 0028846684 scopus 로고
    • Spectroscopic characterization of rhinoviral protease 2A: Zn is essential for the structural integrity
    • Voss T., Meyer R., Sommergruber W. Spectroscopic characterization of rhinoviral protease 2A: Zn is essential for the structural integrity. Protein Sci. 4:1995;2526-2531.
    • (1995) Protein Sci. , vol.4 , pp. 2526-2531
    • Voss, T.1    Meyer, R.2    Sommergruber, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.