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Volumn 71, Issue 12, 1997, Pages 8962-8972

Poliovirus 2C protein determinants of membrane binding and rearrangements in mammalian cells

Author keywords

[No Author keywords available]

Indexed keywords

POLIOMYELITIS VIRUS PROTEIN 2 C; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 0030807887     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.71.12.8962-8972.1997     Document Type: Article
Times cited : (136)

References (64)
  • 1
    • 0029814801 scopus 로고    scopus 로고
    • Membrane permeabilization by poliovirus proteins 2B and 2BC
    • Aldabe, R., A. Barco, and L. Carrasco. 1996. Membrane permeabilization by poliovirus proteins 2B and 2BC. J. Biol. Chem. 271:23134-23137.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23134-23137
    • Aldabe, R.1    Barco, A.2    Carrasco, L.3
  • 2
    • 0028812170 scopus 로고
    • Induction of membrane proliferation by poliovirus proteins 2C and 2BC
    • Aldabe, R., and L. Carrasco. 1995. Induction of membrane proliferation by poliovirus proteins 2C and 2BC. Biochem. Biophys. Res. Commun. 206:64-76.
    • (1995) Biochem. Biophys. Res. Commun. , vol.206 , pp. 64-76
    • Aldabe, R.1    Carrasco, L.2
  • 4
    • 0343852219 scopus 로고
    • Mechanisms of integration of de novo-synthesized polypeptides into membranes: Signal recognition particle is required for integration into microsomal membranes of calcium ATPase and of lens MP but not cytochrome b5
    • Anderson, D. J., K. E. Mostov, and G. Blobel. 1983. Mechanisms of integration of de novo-synthesized polypeptides into membranes: signal recognition particle is required for integration into microsomal membranes of calcium ATPase and of lens MP but not cytochrome b5. Proc. Natl. Acad. Sci. USA 80:7249-7253.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 7249-7253
    • Anderson, D.J.1    Mostov, K.E.2    Blobel, G.3
  • 5
    • 0020972383 scopus 로고
    • Ultrastructural analysis of crystalloid endoplasmic reticulum in UT-1 cells and its disappearance in response to cholesterol
    • Anderson, R. G. W., L. Orci, M. S. Brown, L. M. Garcia-Segura, and J. L. Goldstein. 1983. Ultrastructural analysis of crystalloid endoplasmic reticulum in UT-1 cells and its disappearance in response to cholesterol. J. Cell Sci. 63:1-20.
    • (1983) J. Cell Sci. , vol.63 , pp. 1-20
    • Anderson, R.G.W.1    Orci, L.2    Brown, M.S.3    Garcia-Segura, L.M.4    Goldstein, J.L.5
  • 6
    • 0028990292 scopus 로고
    • Immunocytochemistry and in situ hybridization in the electron microscope: Combined application in the study of virus-infected cells
    • Bienz, K., and D. Egger. 1995. Immunocytochemistry and in situ hybridization in the electron microscope: combined application in the study of virus-infected cells. Histochemistry 103:325-338.
    • (1995) Histochemistry , vol.103 , pp. 325-338
    • Bienz, K.1    Egger, D.2
  • 7
    • 0023415083 scopus 로고
    • Association of polioviral proteins of the P2 genomic region with the viral replication complex and virus-induced membrane synthesis as visualized by electron microscopic immunocytochemistry and autoradiography
    • Bienz, K., D. Egger, and L. Pasamontes. 1987. Association of polioviral proteins of the P2 genomic region with the viral replication complex and virus-induced membrane synthesis as visualized by electron microscopic immunocytochemistry and autoradiography. Virology 160:220-226.
    • (1987) Virology , vol.160 , pp. 220-226
    • Bienz, K.1    Egger, D.2    Pasamontes, L.3
  • 8
    • 0021069227 scopus 로고
    • Intracellular distribution of poliovirus proteins and the induction of virus-specific cytoplasmic structures
    • Bienz, K., D. Egger, Y. Rasser, and W. Bossart. 1983 Intracellular distribution of poliovirus proteins and the induction of virus-specific cytoplasmic structures. Virology 131:39-48.
    • (1983) Virology , vol.131 , pp. 39-48
    • Bienz, K.1    Egger, D.2    Rasser, Y.3    Bossart, W.4
  • 9
    • 0025236535 scopus 로고
    • Structural organization of poliovirus RNA replication is mediated by viral proteins of P2 genomic region
    • Bienz, K., D. Egger, M. Troxler, and L. Pasamontes. 1990. Structural organization of poliovirus RNA replication is mediated by viral proteins of P2 genomic region. J. Virol. 64:1156-1163.
    • (1990) J. Virol. , vol.64 , pp. 1156-1163
    • Bienz, K.1    Egger, D.2    Troxler, M.3    Pasamontes, L.4
  • 10
    • 0028037893 scopus 로고
    • Membrane rearrangement and vesicle induction by recombinant poliovirus 2C and 2BC in human cells
    • Cho, M. W., N. Teterina, D. Egger, K. Bienz, and E. Ehrenfeld. 1994. Membrane rearrangement and vesicle induction by recombinant poliovirus 2C and 2BC in human cells. Virology 202:129-145.
    • (1994) Virology , vol.202 , pp. 129-145
    • Cho, M.W.1    Teterina, N.2    Egger, D.3    Bienz, K.4    Ehrenfeld, E.5
  • 11
    • 0028300959 scopus 로고
    • Expression and subcellular localization of poliovirus VPg-precursor protein 3AB in eukaryotic cells: Evidence for glycosylation in vitro
    • Datta, U., and A. Dasgupta. 1994. Expression and subcellular localization of poliovirus VPg-precursor protein 3AB in eukaryotic cells: evidence for glycosylation in vitro. J. Virol. 68:4468-4477.
    • (1994) J. Virol. , vol.68 , pp. 4468-4477
    • Datta, U.1    Dasgupta, A.2
  • 13
    • 0345482977 scopus 로고
    • GTP-binding domain: Three consensus sequence elements with distinct spacing
    • Dever, T. E., M. J. Glynias, and W. C. Merrick. 1987. GTP-binding domain: three consensus sequence elements with distinct spacing. Proc. Natl. Acad. Sci. USA 84:1814-1818.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 1814-1818
    • Dever, T.E.1    Glynias, M.J.2    Merrick, W.C.3
  • 14
    • 0028918959 scopus 로고
    • Inhibition of cellular protein secretion by poliovirus proteins 2B and 3A
    • Doedens, J. R., and K. Kirkegaard. 1995. Inhibition of cellular protein secretion by poliovirus proteins 2B and 3A. EMBO J. 14:894-907.
    • (1995) EMBO J. , vol.14 , pp. 894-907
    • Doedens, J.R.1    Kirkegaard, K.2
  • 15
    • 0029063814 scopus 로고
    • Amino terminal regions of poliovirus 2C protein mediate membrane binding
    • Echeverri, A. C., and A. Dasgupta. 1995. Amino terminal regions of poliovirus 2C protein mediate membrane binding. Virology 208:540-553.
    • (1995) Virology , vol.208 , pp. 540-553
    • Echeverri, A.C.1    Dasgupta, A.2
  • 16
    • 0029910194 scopus 로고    scopus 로고
    • Reversible dissociation of the poliovirus replication complex: Functions and interactions of its components in viral RNA synthesis
    • Egger, D., L. Pasamontes, R. Bolten, V. Boyko, and K. Bienz. 1996. Reversible dissociation of the poliovirus replication complex: functions and interactions of its components in viral RNA synthesis. J. Virol. 70:8675-8683.
    • (1996) J. Virol. , vol.70 , pp. 8675-8683
    • Egger, D.1    Pasamontes, L.2    Bolten, R.3    Boyko, V.4    Bienz, K.5
  • 17
    • 0000233999 scopus 로고
    • Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase
    • Fuerst, T. R., E. G. Niles, F. W. Studier, and B. Moss. 1986. Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase. Proc. Natl. Acad. Sci. USA 83:8122-8126.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 8122-8126
    • Fuerst, T.R.1    Niles, E.G.2    Studier, F.W.3    Moss, B.4
  • 18
    • 0020039866 scopus 로고
    • Isolation of intracellular membranes by means of sodium carbonate treatment: Application to endoplasmic reticulum
    • Fujiki, Y., A. L. Hubbard, S. Fowler, and P. B. Lazarow. 1982. Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum. J. Cell Biol. 93:97-102.
    • (1982) J. Cell Biol. , vol.93 , pp. 97-102
    • Fujiki, Y.1    Hubbard, A.L.2    Fowler, S.3    Lazarow, P.B.4
  • 19
    • 0024595639 scopus 로고
    • An NTP-binding motif is the most conserved sequence in a highly diverged monophyletic group of proteins involved in positive strand viral replication
    • Gorbalenya, A. E., V. M. Blinov, A. P. Donchenko, and E. V. Koonin. 1989. An NTP-binding motif is the most conserved sequence in a highly diverged monophyletic group of proteins involved in positive strand viral replication. J. Mol. Evol. 28:256-268.
    • (1989) J. Mol. Evol. , vol.28 , pp. 256-268
    • Gorbalenya, A.E.1    Blinov, V.M.2    Donchenko, A.P.3    Koonin, E.V.4
  • 20
    • 17144459131 scopus 로고
    • Prediction of nucleic acid-binding properties of virus proteins from their amino acid sequences
    • Gorbalenya, A. E., V. M. Blinov, and E. V. Koonin. 1985. Prediction of nucleic acid-binding properties of virus proteins from their amino acid sequences. Mol. Genet. 11:30-36.
    • (1985) Mol. Genet. , vol.11 , pp. 30-36
    • Gorbalenya, A.E.1    Blinov, V.M.2    Koonin, E.V.3
  • 21
    • 0024462161 scopus 로고
    • Viral proteins containing the purine NTP-binding sequence pattern
    • Gorbalenya, A. E., and E. Koonin. 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.2
  • 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
  • 24
    • 0025261685 scopus 로고
    • A new superfamily of putative NTP-binding domains encoded by genomes of small DNA and RNA viruses
    • Gorbalenya, A. E., E. V. Koonin, and Y. I. Wolf. 1990. A new superfamily of putative NTP-binding domains encoded by genomes of small DNA and RNA viruses. FEBS Lett. 262:145-148.
    • (1990) FEBS Lett. , vol.262 , pp. 145-148
    • Gorbalenya, A.E.1    Koonin, E.V.2    Wolf, Y.I.3
  • 25
    • 0030069686 scopus 로고    scopus 로고
    • In vitro examination of membrane protein localization and degradation with green fluorescent protein
    • Hampton, R. Y., A. Koning, R. Wright, and J. Rine. 1996. In vitro examination of membrane protein localization and degradation with green fluorescent protein. Proc. Natl. Acad. Sci. USA 93:828-833.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 828-833
    • Hampton, R.Y.1    Koning, A.2    Wright, R.3    Rine, J.4
  • 26
    • 0019971712 scopus 로고
    • Proteolytic processing of poliovirus polypeptides: Antibodies to polypeptide P3-7c inhibit cleavage at glutamine-glycine pairs
    • Hanecak, R., B. L. Semler, C. W. Anderson, and E. Wimmer. 1982. Proteolytic processing of poliovirus polypeptides: antibodies to polypeptide P3-7c inhibit cleavage at glutamine-glycine pairs. Proc. Natl. Acad. Sci. USA 79: 3973-3977.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 3973-3977
    • Hanecak, R.1    Semler, B.L.2    Anderson, C.W.3    Wimmer, E.4
  • 27
    • 0026458378 scopus 로고
    • Amino acid substitution matrices from protein blocks
    • Henikoff, S., and J. G. Henikoff. 1992. Amino acid substitution matrices from protein blocks. Proc. Natl. Acad. Sci. USA 89:10915-10919.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10915-10919
    • Henikoff, S.1    Henikoff, J.G.2
  • 28
    • 0026605537 scopus 로고
    • Clustal-V-imported software for multiple sequence alignment
    • Higgins, D. G., A. J. Bleasby, and R. Fuchs. 1992. Clustal-V-imported software for multiple sequence alignment. Comp. Appl. Biosci. 8:189-191.
    • (1992) Comp. Appl. Biosci. , vol.8 , pp. 189-191
    • Higgins, D.G.1    Bleasby, A.J.2    Fuchs, R.3
  • 29
    • 1842340370 scopus 로고
    • Rescue of drug-requiring and drug-inhibited enteroviruses
    • Ikegami, N., H. J. Eggers, and I. Tamm. 1964. Rescue of drug-requiring and drug-inhibited enteroviruses. Proc. Natl. Acad. Sci. USA 52:1419-1426.
    • (1964) Proc. Natl. Acad. Sci. USA , vol.52 , pp. 1419-1426
    • Ikegami, N.1    Eggers, H.J.2    Tamm, I.3
  • 30
    • 0003004335 scopus 로고
    • The replication of picornaviruses
    • D. J. Rowlands, B. W. J. Mahy, and M. Mayo (ed.) Academic Press, Inc., New York, N.Y.
    • Kuhn, R. J., and E. Wimmer. 1987. The replication of picornaviruses, p. 17-51. In D. J. Rowlands, B. W. J. Mahy, and M. Mayo (ed.), The molecular biology of positive strand RNA viruses. Academic Press, Inc., New York, N.Y.
    • (1987) The Molecular Biology of Positive Strand RNA Viruses , pp. 17-51
    • Kuhn, R.J.1    Wimmer, E.2
  • 31
    • 0026013773 scopus 로고
    • Novel catalytic activity associated with positive-strand RNA virus infection: Nucleic acid-stimulated ATPase activity of the plum pox potyvirus helicaselike protein
    • Laín, S., M. T. Martín, J. L. Riechmann, and J. A. García. 1991. Novel catalytic activity associated with positive-strand RNA virus infection: nucleic acid-stimulated ATPase activity of the plum pox potyvirus helicaselike protein. J. Virol. 65:1-6.
    • (1991) J. Virol. , vol.65 , pp. 1-6
    • Laín, S.1    Martín, M.T.2    Riechmann, J.L.3    García, J.A.4
  • 32
    • 0025685476 scopus 로고
    • RNA helicase: A novel activity associated with a protein encoded by a positive strand RNA virus
    • Laín, S., J. L. Riechmann, and J. A. García. 1990. RNA helicase: a novel activity associated with a protein encoded by a positive strand RNA virus. Nucleic Acids Res. 18:7003-7006.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 7003-7006
    • Laín, S.1    Riechmann, J.L.2    García, J.A.3
  • 33
    • 0027308170 scopus 로고
    • Construction of the full local similarity map for 2 biopolymers
    • Leontovich, A. M., L. I. Brodsky, and A. E. Gorbalenya. 1993. Construction of the full local similarity map for 2 biopolymers. BioSystems 30:57-63.
    • (1993) BioSystems , vol.30 , pp. 57-63
    • Leontovich, A.M.1    Brodsky, L.I.2    Gorbalenya, A.E.3
  • 34
    • 0023724339 scopus 로고
    • Isolation of poliovirus 2C mutants defective in viral RNA synthesis
    • Li, J.-P., and D. Baltimore. 1988. Isolation of poliovirus 2C mutants defective in viral RNA synthesis. J. Virol. 62:4016-4021.
    • (1988) J. Virol. , vol.62 , pp. 4016-4021
    • Li, J.-P.1    Baltimore, D.2
  • 35
    • 0025213458 scopus 로고
    • An intragenic revertant of a poliovirus 2C mutant has an uncoating defect
    • Li, J.-P., and D. Baltimore. 1990. An intragenic revertant of a poliovirus 2C mutant has an uncoating defect. J. Virol. 64:1102-1107.
    • (1990) J. Virol. , vol.64 , pp. 1102-1107
    • Li, J.-P.1    Baltimore, D.2
  • 36
    • 0027535384 scopus 로고
    • Bidirectional membrane traffic between the endoplasmic reticulum and Golgi apparatus
    • Lippincott-Schwartz, J. 1993. Bidirectional membrane traffic between the endoplasmic reticulum and Golgi apparatus. Trends Cell Biol. 3:81-88.
    • (1993) Trends Cell Biol. , vol.3 , pp. 81-88
    • Lippincott-Schwartz, J.1
  • 37
    • 0026769791 scopus 로고
    • Genetic analysis of an NTP-binding motif in poliovirus polypeptide 2C
    • Mirzayan, C., and E. Wimmer. 1992. Genetic analysis of an NTP-binding motif in poliovirus polypeptide 2C. Virology 189:547-555.
    • (1992) Virology , vol.189 , pp. 547-555
    • Mirzayan, C.1    Wimmer, E.2
  • 38
    • 0028355633 scopus 로고
    • Biochemical studies on poliovirus polypeptide 2C: Evidence for ATPase activity
    • Mirzayan, C., and E. Wimmer. 1994. Biochemical studies on poliovirus polypeptide 2C: evidence for ATPase activity. Virology 199:176-187.
    • (1994) Virology , vol.199 , pp. 176-187
    • Mirzayan, C.1    Wimmer, E.2
  • 39
    • 0028319318 scopus 로고
    • Classification of protein folds
    • Orengo, C. 1994. Classification of protein folds. Curr. Opin. Struct. Biol. 4:429-440.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 429-440
    • Orengo, C.1
  • 40
    • 0022967929 scopus 로고
    • Production of monoclonal and monospecific antibodies against non-capsid proteins of poliovirus
    • Pasamontes, L., D. Egger, and K. Bienz. 1986. Production of monoclonal and monospecific antibodies against non-capsid proteins of poliovirus. J. Gen. Virol. 67:2415-2422.
    • (1986) J. Gen. Virol. , vol.67 , pp. 2415-2422
    • Pasamontes, L.1    Egger, D.2    Bienz, K.3
  • 41
    • 0028331981 scopus 로고
    • Studies of a putative amphipathic helix in the N-terminus of poliovirus protein 2C
    • Paul, A. V., A. Molla, and E. Wimmer. 1994. Studies of a putative amphipathic helix in the N-terminus of poliovirus protein 2C. Virology 199:188-199.
    • (1994) Virology , vol.199 , pp. 188-199
    • Paul, A.V.1    Molla, A.2    Wimmer, E.3
  • 42
    • 0027422866 scopus 로고
    • Picornavirus nonstructural proteins: Emerging roles in virus replication and inhibition of host cell functions
    • Porter, A. G. 1993. Picornavirus nonstructural proteins: emerging roles in virus replication and inhibition of host cell functions. J. Virol. 67:6917-6921.
    • (1993) J. Virol. , vol.67 , pp. 6917-6921
    • Porter, A.G.1
  • 43
    • 0028261803 scopus 로고
    • The tobacco etch potyvirus 6-kilodalton protein is membrane associated and involved in viral replication
    • Restrepo-Hartwig, M. A., and J. C. Carrington. 1994. The tobacco etch potyvirus 6-kilodalton protein is membrane associated and involved in viral replication. J. Virol. 68:2388-2397.
    • (1994) J. Virol. , vol.68 , pp. 2388-2397
    • Restrepo-Hartwig, M.A.1    Carrington, J.C.2
  • 44
    • 0027537974 scopus 로고
    • Poliovirus protein 2C has ATPase and GTPase activities
    • Rodriguez, P. L., and L. Carrasco. 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
  • 45
    • 0028925901 scopus 로고
    • Poliovirus protein 2C contains two regions involved in RNA binding activity
    • Rodriguez, P. L., and L. Carrasco. 1995. Poliovirus protein 2C contains two regions involved in RNA binding activity. J. Biol. Chem. 270:10105-10112.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10105-10112
    • Rodriguez, P.L.1    Carrasco, L.2
  • 46
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better than 70-percent accuracy
    • Rost, B., and C. Sander. 1993. Prediction of protein secondary structure at better than 70-percent accuracy. J. Mol. Biol. 232:584-599.
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 48
    • 0025048136 scopus 로고
    • The P-loop - A common motif in ATP- and GTP-binding proteins
    • Saraste, M., P. R. Sibbald, and A. Wittinghofer. 1990. The P-loop - a common motif in ATP-and GTP-binding proteins. Trends Biochem. Sci. 15:430-434.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 430-434
    • Saraste, M.1    Sibbald, P.R.2    Wittinghofer, A.3
  • 49
    • 0029794678 scopus 로고    scopus 로고
    • Cellular origin and ultrastructure of membranes induced during poliovirus infection
    • Schlegel, A., T. H. Giddings, M. S. Ladinsky, and K. Kirkegaard. 1996. Cellular origin and ultrastructure of membranes induced during poliovirus infection. J. Virol. 70:6576-6588.
    • (1996) J. Virol. , vol.70 , pp. 6576-6588
    • Schlegel, A.1    Giddings, T.H.2    Ladinsky, M.S.3    Kirkegaard, K.4
  • 50
    • 0026100921 scopus 로고
    • A workbench for multiple alignment construction and analysis
    • Schuler, G. D., S. F. Altschul, and D. Lipman. 1991. A workbench for multiple alignment construction and analysis. Proteins 9:180-190.
    • (1991) Proteins , vol.9 , pp. 180-190
    • Schuler, G.D.1    Altschul, S.F.2    Lipman, D.3
  • 51
    • 12944300317 scopus 로고
    • Binding of nucleotides by proteins
    • Schulz, G. E. 1992. Binding of nucleotides by proteins. Curr. Opin. Struct. Biol. 2:61-67.
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 61-67
    • Schulz, G.E.1
  • 52
    • 0010612316 scopus 로고
    • Biocomputing Research Unit, University of Edinburgh, Edinburgh, United Kingdom
    • Sturrock, S. S., and J. F. Collins. 1993. MPsrch version 1.3. Biocomputing Research Unit, University of Edinburgh, Edinburgh, United Kingdom.
    • (1993) MPsrch Version 1.3
    • Sturrock, S.S.1    Collins, J.F.2
  • 54
    • 0020521818 scopus 로고
    • Membrane fraction active in poliovirus RNA replication contain VPg precursor polypeptides
    • Takegami, T., B. L. Semler, C. W. Anderson, and E. Wimmer. 1983. Membrane fraction active in poliovirus RNA replication contain VPg precursor polypeptides. Virology 128:33-47.
    • (1983) Virology , vol.128 , pp. 33-47
    • Takegami, T.1    Semler, B.L.2    Anderson, C.W.3    Wimmer, E.4
  • 55
    • 0021720256 scopus 로고
    • Association of poliovirus proteins with the endoplasmic reticulum
    • Tershak, D. R. 1984. Association of poliovirus proteins with the endoplasmic reticulum. J. Virol. 52:777-783.
    • (1984) J. Virol. , vol.52 , pp. 777-783
    • Tershak, D.R.1
  • 56
    • 0026799231 scopus 로고
    • Analysis of the functional significance of amino acid residues in the putative NTP-binding pattern of the poliovirus 2C protein
    • Teterina, N. L., K. M. Kean, E. Gorbalenya, V. I. Agol, and M. Girard. 1992. Analysis of the functional significance of amino acid residues in the putative NTP-binding pattern of the poliovirus 2C protein. J. Gen. Virol. 73:1977-1986.
    • (1992) J. Gen. Virol. , vol.73 , pp. 1977-1986
    • Teterina, N.L.1    Kean, K.M.2    Gorbalenya, E.3    Agol, V.I.4    Girard, M.5
  • 57
    • 0028178889 scopus 로고
    • Genetic studies on the poliovirus 2C protein, an NTPase - A plausible mechanism of guanidine effect on the 2C function and evidence for the importance of 2C oligomerization
    • Tolskaya, E. A., L. I. Romanova, M. S. Kolesnikova, A. P. Gmyl, A. E. Gorbalenya, and V. I. Agol. 1994. Genetic studies on the poliovirus 2C protein, an NTPase - a plausible mechanism of guanidine effect on the 2C function and evidence for the importance of 2C oligomerization. J. Mol. Biol. 236:1310-1323.
    • (1994) J. Mol. Biol. , vol.236 , pp. 1310-1323
    • Tolskaya, E.A.1    Romanova, L.I.2    Kolesnikova, M.S.3    Gmyl, A.P.4    Gorbalenya, A.E.5    Agol, V.I.6
  • 58
    • 0021473099 scopus 로고
    • Physiological and morphological effects of overproduction of membrane-bound ATP synthase in Escherichia coli K-12
    • Von Meyenberg, K., B. B. Jorgensen, and B. Van Deurs. 1984. Physiological and morphological effects of overproduction of membrane-bound ATP synthase in Escherichia coli K-12. EMBO J. 3:1791-1797.
    • (1984) EMBO J. , vol.3 , pp. 1791-1797
    • Von Meyenberg, K.1    Jorgensen, B.B.2    Van Deurs, B.3
  • 59
    • 0029054827 scopus 로고
    • Functional characterization of the 180-kD ribosome receptor in vivo
    • Wanker, E. E., Y. Sun, A. J. Savitz, and D. I. Meyer. 1995. Functional characterization of the 180-kD ribosome receptor in vivo. J. Cell Biol. 130: 29-39.
    • (1995) J. Cell Biol. , vol.130 , pp. 29-39
    • Wanker, E.E.1    Sun, Y.2    Savitz, A.J.3    Meyer, D.I.4
  • 60
    • 1842278033 scopus 로고
    • Pestivirus NS3 (p80) protein possesses RNA helicase activity
    • Warrener, P., and M. S. Collett, 1995. Pestivirus NS3 (p80) protein possesses RNA helicase activity. J. Virol. 67:989-996.
    • (1995) J. Virol. , vol.67 , pp. 989-996
    • Warrener, P.1    Collett, M.S.2
  • 61
    • 0021324648 scopus 로고
    • Overproduction of fumarate reductase in Escherichia coli induces a novel intracellular lipid-protein organelle
    • Weiner, J. H., B. D. Lemire, M. L. Elmes, R. D. Bradley, and D. G. Scraba. 1984. Overproduction of fumarate reductase in Escherichia coli induces a novel intracellular lipid-protein organelle. J. Bacteriol. 158:590-596.
    • (1984) J. Bacteriol. , vol.158 , pp. 590-596
    • Weiner, J.H.1    Lemire, B.D.2    Elmes, M.L.3    Bradley, R.D.4    Scraba, D.G.5
  • 63
    • 0025740753 scopus 로고
    • The structure of Ras protein: A model for a universal molecular switch
    • Wittinghofer, A., and E. F. Pai. 1991. The structure of Ras protein: a model for a universal molecular switch. Trends Biochem. Sci. 16:382-387.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 382-387
    • Wittinghofer, A.1    Pai, E.F.2
  • 64
    • 85053971721 scopus 로고
    • Evolution of RNA viruses
    • J. J. Holland, E. Domingo, and P. Alquist (ed.) CRC Press, Boca Raton, Fla.
    • Zimmern, D. 1988. Evolution of RNA viruses, p. 211-240. In J. J. Holland, E. Domingo, and P. Alquist (ed.), RNA genetics, vol. 2. CRC Press, Boca Raton, Fla.
    • (1988) RNA Genetics , vol.2 , pp. 211-240
    • Zimmern, D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.