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Volumn 287, Issue 35, 2012, Pages 29729-29738

Inhibition of Pokeweed Antiviral Protein (PAP) by turnip mosaic virus genome-linked protein (VPg)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIVIRAL AGENTS; CAP-BINDING; CAP-INDEPENDENT TRANSLATION; CYTOTOXIC ACTIVITIES; DEPURINATION; HIGH AFFINITY; HUMAN VIRUS; N-GLYCOSIDASE; PLANT DEFENSE MECHANISMS; POKEWEED ANTIVIRAL PROTEINS; POTENT INHIBITOR; PROTEIN SYNTHESIS; RIBOSOME-INACTIVATING PROTEIN; TOBACCO ETCH VIRUS; TURNIP MOSAIC VIRUS; WHEAT GERM;

EID: 84865465564     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.367581     Document Type: Article
Times cited : (17)

References (53)
  • 1
    • 0015609581 scopus 로고
    • The effect of an antiviral peptide on the ribosomal reactions of the peptide elongation enzymes, EF-I and EF-II
    • Obrig, T. G., Irvin, J. D., and Hardesty, B. (1973) The effect of an antiviral peptide on the ribosomal reactions of the peptide elongation enzymes, EF-I and EF-II. Arch. Biochem. Biophys. 155, 278-289
    • (1973) Arch. Biochem. Biophys. , vol.155 , pp. 278-289
    • Obrig, T.G.1    Irvin, J.D.2    Hardesty, B.3
  • 2
    • 0001514476 scopus 로고
    • The effect of treating virus of tobacco mosaic with juice of various plants
    • Duggar, B. M., and Armstrong, J. K. (1925) The effect of treating virus of tobacco mosaic with juice of various plants. Ann. Mol. Bot. Gard. 12, 359-365
    • (1925) Ann. Mol. Bot. Gard. , vol.12 , pp. 359-365
    • Duggar, B.M.1    Armstrong, J.K.2
  • 3
    • 0017829068 scopus 로고
    • Enzymatic inactivation of eukaryotic ribosomes by the pokeweed antiviral protein
    • Dallal, J. A., and Irvin, J. D. (1978) Enzymatic inactivation of eukaryotic ribosomes by the pokeweed antiviral protein. FEBS Lett. 89, 257-259
    • (1978) FEBS Lett. , vol.89 , pp. 257-259
    • Dallal, J.A.1    Irvin, J.D.2
  • 4
    • 0025064610 scopus 로고
    • Dual effects of the ricin A chain on protein synthesis in rabbit reticulocyte lysate. Inhibition of initiation and translocation
    • Osborn, R. W., and Hartley, M. R. (1990) Dual effects of the ricin A chain on protein synthesis in rabbit reticulocyte lysate. Inhibition of initiation and translocation. Eur. J. Biochem. 193, 401-407
    • (1990) Eur. J. Biochem. , vol.193 , pp. 401-407
    • Osborn, R.W.1    Hartley, M.R.2
  • 5
    • 0024589101 scopus 로고
    • Effect of α-sarcin and ribosome-inactivating proteins on the interaction of elongation factors with ribosomes
    • Brigotti, M., Rambelli, F., Zamboni, M., Montanaro, L., and Sperti, S. (1989) Effect of α-sarcin and ribosome-inactivating proteins on the interaction of elongation factors with ribosomes. Biochem. J. 257, 723-727
    • (1989) Biochem. J. , vol.257 , pp. 723-727
    • Brigotti, M.1    Rambelli, F.2    Zamboni, M.3    Montanaro, L.4    Sperti, S.5
  • 6
    • 33748178290 scopus 로고    scopus 로고
    • Pokeweed antiviral protein depurinates the sarcin/ricin loop of the rRNA prior to binding of aminoacyl-tRNA to the ribosomal A-site
    • Mansouri, S., Nourollahzadeh, E., and Hudak, K. A. (2006) Pokeweed antiviral protein depurinates the sarcin/ricin loop of the rRNA prior to binding of aminoacyl-tRNA to the ribosomal A-site. RNA 12, 1683-1692
    • (2006) RNA , vol.12 , pp. 1683-1692
    • Mansouri, S.1    Nourollahzadeh, E.2    Hudak, K.A.3
  • 7
    • 0031883153 scopus 로고    scopus 로고
    • The pokeweed antiviral protein specifically inhibits Ty1-directed +1 ribosomal frameshifting and retrotransposition in Saccharomyces cerevisiae
    • Tumer, N. E., Parikh, B. A., Li, P., and Dinman, J. D. (1998) The pokeweed antiviral protein specifically inhibits Ty1-directed +1 ribosomal frameshifting and retrotransposition in Saccharomyces cerevisiae. J. Virol. 72, 1036-1042
    • (1998) J. Virol. , vol.72 , pp. 1036-1042
    • Tumer, N.E.1    Parikh, B.A.2    Li, P.3    Dinman, J.D.4
  • 8
    • 0035915986 scopus 로고    scopus 로고
    • A C-terminal deletion mutant of pokeweed antiviral protein inhibits programmed +1 ribosomal frameshifting and Ty1 retrotransposition without depurinating the sarcin/ricin loop of rRNA
    • Hudak, K. A., Hammell, A. B., Yasenchak, J., Tumer, N. E., and Dinman, J. D. (2001) A C-terminal deletion mutant of pokeweed antiviral protein inhibits programmed +1 ribosomal frameshifting and Ty1 retrotransposition without depurinating the sarcin/ricin loop of rRNA. Virology 279, 292-301
    • (2001) Virology , vol.279 , pp. 292-301
    • Hudak, K.A.1    Hammell, A.B.2    Yasenchak, J.3    Tumer, N.E.4    Dinman, J.D.5
  • 11
    • 0033524919 scopus 로고    scopus 로고
    • Pokeweed antiviral protein accesses ribosomes by binding to L3
    • Hudak, K. A., Dinman, J. D., and Tumer, N. E. (1999) Pokeweed antiviral protein accesses ribosomes by binding to L3. J. Biol. Chem. 274, 3859-3864
    • (1999) J. Biol. Chem. , vol.274 , pp. 3859-3864
    • Hudak, K.A.1    Dinman, J.D.2    Tumer, N.E.3
  • 12
    • 23044506167 scopus 로고    scopus 로고
    • Expression of a truncated form of ribosomal protein L3 confers resistance to pokeweed antiviral protein and the Fusarium mycotoxin deoxynivalenol
    • Di, R., and Tumer, N. E. (2005) Expression of a truncated form of ribosomal protein L3 confers resistance to pokeweed antiviral protein and the Fusarium mycotoxin deoxynivalenol. Mol. Plant Microbe Interact. 18, 762-770
    • (2005) Mol. Plant Microbe Interact. , vol.18 , pp. 762-770
    • Tumer, N.E.1
  • 13
    • 0033526850 scopus 로고    scopus 로고
    • Pokeweed antiviral protein isoforms PAP-I, PAP-II, and PAP-III depurinate RNA of human immunodeficiency virus (HIV)-1
    • Rajamohan, F., Venkatachalam, T. K., Irvin, J. D., and Uckun, F. M. (1999) Pokeweed antiviral protein isoforms PAP-I, PAP-II, and PAP-III depurinate RNA of human immunodeficiency virus (HIV)-1. Biochem. Biophys. Res. Commun. 260, 453-458
    • (1999) Biochem. Biophys. Res. Commun. , vol.260 , pp. 453-458
    • Rajamohan, F.1    Venkatachalam, T.K.2    Irvin, J.D.3    Uckun, F.M.4
  • 14
    • 0005489933 scopus 로고
    • A possible mechanism for the antiviral activity of pokeweed antiviral protein
    • Chen, Z., Antoniw, J. F., and White, R. F. (1993) A possible mechanism for the antiviral activity of pokeweed antiviral protein. Physiol. Mol. Plant Pathol. 42, 249-258
    • (1993) Physiol. Mol. Plant Pathol. , vol.42 , pp. 249-258
    • Chen, Z.1    Antoniw, J.F.2    White, R.F.3
  • 15
    • 0017620367 scopus 로고
    • Inhibition of poliovirus replication by a plant antiviral peptide
    • Ussery, M. A., Irvin, J. D., and Hardesty, B. (1977) Inhibition of poliovirus replication by a plant antiviral peptide. Ann. N.Y. Acad. Sci. 284, 431-440
    • (1977) Ann. N.Y. Acad. Sci. , vol.284 , pp. 431-440
    • Ussery, M.A.1    Irvin, J.D.2    Hardesty, B.3
  • 16
    • 0018826093 scopus 로고
    • Inhibition of herpes simplex virus multiplication by the pokeweed antiviral protein
    • Aron, G. M., and Irvin, J. D. (1980) Inhibition of herpes simplex virus multiplication by the pokeweed antiviral protein. Antimicrob. Agents Chemother. 17, 1032-1033
    • (1980) Antimicrob. Agents Chemother. , vol.17 , pp. 1032-1033
    • Aron, G.M.1    Irvin, J.D.2
  • 17
    • 0015987890 scopus 로고
    • The inhibition of infection by cucumber mosaic virus and influenza virus by extracts from Phytolacca americana
    • Tomlinson, J. A., Walker, V. M., Flewett, T. H., and Barclay, G. R. (1974) The inhibition of infection by cucumber mosaic virus and influenza virus by extracts from Phytolacca americana. J. Gen. Virol. 22, 225-232
    • (1974) J. Gen. Virol. , vol.22 , pp. 225-232
    • Tomlinson, J.A.1    Walker, V.M.2    Flewett, T.H.3    Barclay, G.R.4
  • 18
    • 21244490435 scopus 로고    scopus 로고
    • Pokeweed antiviral protein inhibits brome mosaic virus replication in plant cells
    • Picard, D., Kao, C. C., and Hudak, K. A. (2005) Pokeweed antiviral protein inhibits brome mosaic virus replication in plant cells. J. Biol. Chem. 280, 20069-20075
    • (2005) J. Biol. Chem. , vol.280 , pp. 20069-20075
    • Picard, D.1    Kao, C.C.2    Hudak, K.A.3
  • 19
    • 0034022958 scopus 로고    scopus 로고
    • A novel mechanism for inhibition of translation by pokeweed antiviral protein. Depurination of the capped RNA template
    • Hudak, K. A., Wang, P., and Tumer, N. E. (2000) A novel mechanism for inhibition of translation by pokeweed antiviral protein. Depurination of the capped RNA template. RNA 6, 369-380
    • (2000) RNA , vol.6 , pp. 369-380
    • Hudak, K.A.1    Wang, P.2    Tumer, N.E.3
  • 20
    • 0036717810 scopus 로고    scopus 로고
    • Pokeweed antiviral protein binds to the cap structure of eukaryotic mRNA and depurinates the mRNA downstream of the cap
    • Hudak, K. A., Bauman, J. D., and Tumer, N. E. (2002) Pokeweed antiviral protein binds to the cap structure of eukaryotic mRNA and depurinates the mRNA downstream of the cap. RNA 8, 1148-1159
    • (2002) RNA , vol.8 , pp. 1148-1159
    • Hudak, K.A.1    Bauman, J.D.2    Tumer, N.E.3
  • 21
    • 0037407823 scopus 로고    scopus 로고
    • Translation inhibition of capped and uncapped viral RNAs mediated by ribosome-inactivating proteins
    • Vivanco, J. M., and Tumer, N. E. (2003) Translation inhibition of capped and uncapped viral RNAs mediated by ribosome-inactivating proteins. Phytopathology 93, 588-595
    • (2003) Phytopathology , vol.93 , pp. 588-595
    • Vivanco, J.M.1    Tumer, N.E.2
  • 22
    • 33644854446 scopus 로고    scopus 로고
    • Anovel interaction of pokeweed antiviral protein with translation initiation factors 4G and iso4G. A potential indirect mechanism to access viral RNAs
    • Wang, M., and Hudak, K. A. (2006)Anovel interaction of pokeweed antiviral protein with translation initiation factors 4G and iso4G. A potential indirect mechanism to access viral RNAs. Nucleic Acids Res. 34, 1174-1181
    • (2006) Nucleic Acids Res. , vol.34 , pp. 1174-1181
    • Wang, M.1    Hudak, K.A.2
  • 23
    • 58149525335 scopus 로고    scopus 로고
    • Characterization of pokeweed antiviral protein binding to mRNA cap analogs. Competition with nucleotides and enhancement by translation initiation factor iso4G
    • Baldwin, A. E., Khan, M. A., Tumer, N. E., Goss, D. J., and Friedland, D. E. (2009) Characterization of pokeweed antiviral protein binding to mRNA cap analogs. Competition with nucleotides and enhancement by translation initiation factor iso4G. Biochim. Biophys. Acta 1789, 109-116
    • (2009) Biochim. Biophys. Acta , vol.1789 , pp. 109-116
    • Baldwin, A.E.1    Khan, M.A.2    Tumer, N.E.3    Goss, D.J.4    Friedland, D.E.5
  • 24
    • 0026084608 scopus 로고
    • A tyrosine residue in the small nuclear inclusion protein of tobacco vein mottling virus links the VPg to the viral RNA
    • Murphy, J. F., Rychlik, W., Rhoads, R. E., Hunt, A. G., and Shaw, J. G. (1991) A tyrosine residue in the small nuclear inclusion protein of tobacco vein mottling virus links the VPg to the viral RNA. J. Virol. 65, 511-513
    • (1991) J. Virol. , vol.65 , pp. 511-513
    • Murphy, J.F.1    Rychlik, W.2    Rhoads, R.E.3    Hunt, A.G.4    Shaw, J.G.5
  • 25
    • 0032006755 scopus 로고    scopus 로고
    • Potyvirus genome-linked protein (VPg) determines pea seed-borne mosaic virus pathotype-specific virulence in Pisum sativum
    • Keller, K. E., Johansen, I. E., Martin, R. R., and Hampton, R. O. (1998) Potyvirus genome-linked protein (VPg) determines pea seed-borne mosaic virus pathotype-specific virulence in Pisum sativum. Mol. Plant Microbe Interact. 11, 124-130
    • (1998) Mol. Plant Microbe Interact. , vol.11 , pp. 124-130
    • Keller, K.E.1    Johansen, I.E.2    Martin, R.R.3    Hampton, R.O.4
  • 26
    • 0033886549 scopus 로고    scopus 로고
    • Complex formation between potyvirus VPg and translation eukaryotic initiation factor 4E correlates with virus infectivity
    • Léonard, S., Plante, D., Wittmann, S., Daigneault, N., Fortin, M. G., and Laliberté, J. F. (2000) Complex formation between potyvirus VPg and translation eukaryotic initiation factor 4E correlates with virus infectivity. J. Virol. 74, 7730-7737
    • (2000) J. Virol. , vol.74 , pp. 7730-7737
    • Léonard, S.1    Plante, D.2    Wittmann, S.3    Daigneault, N.4    Fortin, M.G.5    Laliberté, J.F.6
  • 27
    • 0031582643 scopus 로고    scopus 로고
    • Interaction of the viral protein genome linked of turnip mosaic potyvirus with the translational eukaryotic initiation factor (iso) 4E of Arabidopsis thaliana using the yeast two-hybrid system
    • Wittmann, S., Chatel, H., Fortin, M. G., and Laliberté, J. F. (1997) Interaction of the viral protein genome linked of turnip mosaic potyvirus with the translational eukaryotic initiation factor (iso) 4E of Arabidopsis thaliana using the yeast two-hybrid system. Virology 234, 84-92
    • (1997) Virology , vol.234 , pp. 84-92
    • Wittmann, S.1    Chatel, H.2    Fortin, M.G.3    Laliberté, J.F.4
  • 28
    • 0030922351 scopus 로고    scopus 로고
    • Identification of a protein linked to the genomic and subgenomic mRNAs of feline calicivirus and its role in translation
    • Herbert, T. P., Brierley, I., and Brown, T. D. (1997) Identification of a protein linked to the genomic and subgenomic mRNAs of feline calicivirus and its role in translation. J. Gen. Virol. 78, 1033-1040
    • (1997) J. Gen. Virol. , vol.78 , pp. 1033-1040
    • Herbert, T.P.1    Brierley, I.2    Brown, T.D.3
  • 29
    • 33646001699 scopus 로고    scopus 로고
    • Binding analyses for the interaction between plant virus genome-linked protein (VPg) and plant translational initiation factors
    • Miyoshi, H., Suehiro, N., Tomoo, K., Muto, S., Takahashi, T., Tsukamoto, T., Ohmori, T., and Natsuaki, T. (2006) Binding analyses for the interaction between plant virus genome-linked protein (VPg) and plant translational initiation factors. Biochimie 88, 329-340
    • (2006) Biochimie , vol.88 , pp. 329-340
    • Miyoshi, H.1    Suehiro, N.2    Tomoo, K.3    Muto, S.4    Takahashi, T.5    Tsukamoto, T.6    Ohmori, T.7    Natsuaki, T.8
  • 30
    • 1842865092 scopus 로고    scopus 로고
    • Interaction of VPg-Pro of turnip mosaic virus with the translation initiation factor 4E and the poly(A)-binding protein in planta
    • Léonard, S., Viel, C., Beauchemin, C., Daigneault, N., Fortin, M. G., and Laliberté, J. F. (2004) Interaction of VPg-Pro of turnip mosaic virus with the translation initiation factor 4E and the poly(A)-binding protein in planta. J. Gen. Virol. 85, 1055-1063
    • (2004) J. Gen. Virol. , vol.85 , pp. 1055-1063
    • Léonard, S.1    Viel, C.2    Beauchemin, C.3    Daigneault, N.4    Fortin, M.G.5    Laliberté, J.F.6
  • 31
    • 33748794208 scopus 로고    scopus 로고
    • Interaction of genome-linked protein (VPg) of turnip mosaic virus with wheat germ translation initiation factors eIFiso4E and eIFiso4F
    • Khan, M. A., Miyoshi, H., Ray, S., Natsuaki, T., Suehiro, N., and Goss, D. J. (2006) Interaction of genome-linked protein (VPg) of turnip mosaic virus with wheat germ translation initiation factors eIFiso4E and eIFiso4F. J. Biol. Chem. 281, 28002-28010
    • (2006) J. Biol. Chem. , vol.281 , pp. 28002-28010
    • Khan, M.A.1    Miyoshi, H.2    Ray, S.3    Natsuaki, T.4    Suehiro, N.5    Goss, D.J.6
  • 32
    • 38349147642 scopus 로고    scopus 로고
    • Potyvirus genome-linked protein, VPg, directly affects wheat germ in vitro translation. Interactions with translation initiation factors eIF4F and eIFiso4F
    • Khan, M. A., Miyoshi, H., Gallie, D. R., and Goss, D. J. (2008) Potyvirus genome-linked protein, VPg, directly affects wheat germ in vitro translation. Interactions with translation initiation factors eIF4F and eIFiso4F. J. Biol. Chem. 283, 1340-1349
    • (2008) J. Biol. Chem. , vol.283 , pp. 1340-1349
    • Khan, M.A.1    Miyoshi, H.2    Gallie, D.R.3    Goss, D.J.4
  • 33
    • 22844438327 scopus 로고    scopus 로고
    • Cap-independent translation of tobacco etch virus is conferred by an RNA pseudoknot in the 5′-leader
    • Zeenko, V., and Gallie, D. R. (2005) Cap-independent translation of tobacco etch virus is conferred by an RNA pseudoknot in the 5′-leader. J. Biol. Chem. 280, 26813-26824
    • (2005) J. Biol. Chem. , vol.280 , pp. 26813-26824
    • Zeenko, V.1    Gallie, D.R.2
  • 34
    • 33845995462 scopus 로고    scopus 로고
    • Tobacco etch virus mRNA preferentially binds wheat germ eukaryotic initiation factor (eIF) 4G rather than eIFiso4G
    • Ray, S., Yumak, H., Domashevskiy, A., Khan, M. A., Gallie, D. R., and Goss, D. J. (2006) Tobacco etch virus mRNA preferentially binds wheat germ eukaryotic initiation factor (eIF) 4G rather than eIFiso4G. J. Biol. Chem. 281, 35826-35834
    • (2006) J. Biol. Chem. , vol.281 , pp. 35826-35834
    • Ray, S.1    Yumak, H.2    Domashevskiy, A.3    Khan, M.A.4    Gallie, D.R.5    Goss, D.J.6
  • 35
    • 33646782967 scopus 로고    scopus 로고
    • Cap-independent translation of plant viral RNAs
    • Kneller, E. L., Rakotondrafara, A. M., and Miller, W. A. (2006) Cap-independent translation of plant viral RNAs. Virus Res. 119, 63-75
    • (2006) Virus Res. , vol.119 , pp. 63-75
    • Kneller, E.L.1    Rakotondrafara, A.M.2    Miller, W.A.3
  • 36
    • 0025835303 scopus 로고
    • Post-transcriptional regulation in higher eukaryotes. The role of the reporter gene in controlling expression
    • Gallie, D. R., Feder, J. N., Schimke, R. T., and Walbot, V. (1991) Post-transcriptional regulation in higher eukaryotes. The role of the reporter gene in controlling expression. Mol. Gen. Genet. 228, 258-264
    • (1991) Mol. Gen. Genet. , vol.228 , pp. 258-264
    • Gallie, D.R.1    Feder, J.N.2    Schimke, R.T.3    Walbot, V.4
  • 37
    • 0024597110 scopus 로고
    • High-pressure liquid chromatographic and fluorimetric methods for the determination of adenine released from ribosomes by ricin and gelonin
    • Zamboni, M., Brigotti, M., Rambelli, F., Montanaro, L., and Sperti, S. (1989) High-pressure liquid chromatographic and fluorimetric methods for the determination of adenine released from ribosomes by ricin and gelonin. Biochem. J. 259, 639-643
    • (1989) Biochem. J. , vol.259 , pp. 639-643
    • Zamboni, M.1    Brigotti, M.2    Rambelli, F.3    Montanaro, L.4    Sperti, S.5
  • 38
    • 0025897623 scopus 로고
    • Improved high-pressure liquid chromatographic-fluorometric assay for measurement of adenosine in plasma
    • Zhang, Y., Geiger, J. D., and Lautt, W. W. (1991) Improved high-pressure liquid chromatographic-fluorometric assay for measurement of adenosine in plasma. Am. J. Physiol. 260, G658-G664
    • (1991) Am. J. Physiol. , vol.260
    • Zhang, Y.1    Geiger, J.D.2    Lautt, W.W.3
  • 39
    • 0025766506 scopus 로고
    • Fluorometric determination of plasma adenosine concentrations using high-performance liquid chromatography
    • Miura, K., Okumura, M., Yukimura, T., and Yamamoto, K. (1991) Fluorometric determination of plasma adenosine concentrations using high-performance liquid chromatography. Anal. Biochem. 196, 84-88
    • (1991) Anal. Biochem. , vol.196 , pp. 84-88
    • Miura, K.1    Okumura, M.2    Yukimura, T.3    Yamamoto, K.4
  • 40
    • 0029790461 scopus 로고    scopus 로고
    • Synthesis of a fluorescent 7-methylguanosine analog and a fluorescence spectroscopic study of its reaction with wheat germ cap-binding proteins
    • Ren, J., and Goss, D. J. (1996) Synthesis of a fluorescent 7-methylguanosine analog and a fluorescence spectroscopic study of its reaction with wheat germ cap-binding proteins. Nucleic Acids Res. 24, 3629-3634
    • (1996) Nucleic Acids Res. , vol.24 , pp. 3629-3634
    • Ren, J.1    Goss, D.J.2
  • 41
    • 0020674810 scopus 로고
    • New ribose-modified fluorescent analogs of adenine and guanine nucleotides available as substrates for various enzymes
    • Hiratsuka, T. (1983) New ribose-modified fluorescent analogs of adenine and guanine nucleotides available as substrates for various enzymes. Biochim. Biophys. Acta 742, 496-508
    • (1983) Biochim. Biophys. Acta , vol.742 , pp. 496-508
    • Hiratsuka, T.1
  • 43
    • 0029966505 scopus 로고    scopus 로고
    • Mutations at two invariant nucleotides in the 3′-minor domain of Escherichia coli 16 S rRNA affecting translational initiation and initiation factor 3 function
    • Firpo, M. A., Connelly, M. B., Goss, D. J., and Dahlberg, A. E. (1996) Mutations at two invariant nucleotides in the 3′-minor domain of Escherichia coli 16 S rRNA affecting translational initiation and initiation factor 3 function. J. Biol. Chem. 271, 4693-4698
    • (1996) J. Biol. Chem. , vol.271 , pp. 4693-4698
    • Firpo, M.A.1    Connelly, M.B.2    Goss, D.J.3    Dahlberg, A.E.4
  • 44
    • 0017613454 scopus 로고
    • Fluorescence-quenching studies of the binding of bilirubin to albumin
    • Levine, R. (1977) Fluorescence-quenching studies of the binding of bilirubin to albumin. Clin. Chem. 23, 2292-2301
    • (1977) Clin. Chem. , vol.23 , pp. 2292-2301
    • Levine, R.1
  • 45
    • 65249171997 scopus 로고    scopus 로고
    • Detecting ricin. Sensitive luminescent assay for ricin A-chain ribosome depurination kinetics
    • Sturm, M. B., and Schramm, V. L. (2009) Detecting ricin. Sensitive luminescent assay for ricin A-chain ribosome depurination kinetics. Anal. Chem. 81, 2847-2853
    • (2009) Anal. Chem. , vol.81 , pp. 2847-2853
    • Sturm, M.B.1    Schramm, V.L.2
  • 46
    • 0032876556 scopus 로고    scopus 로고
    • Identification and characterization of the functional elements within the tobacco etch virus 5′ leader required for cap-independent translation
    • Niepel, M., and Gallie, D. R. (1999) Identification and characterization of the functional elements within the tobacco etch virus 5′ leader required for cap-independent translation. J. Virol. 73, 9080-9088
    • (1999) J. Virol. , vol.73 , pp. 9080-9088
    • Niepel, M.1    Gallie, D.R.2
  • 47
    • 0028369223 scopus 로고
    • Pokeweed antiviral protein inactivates pokeweed ribosomes. Implications for the antiviral mechanism
    • Bonness, M. S., Ready, M. P., Irvin, J. D., and Mabry, T. J. (1994) Pokeweed antiviral protein inactivates pokeweed ribosomes. Implications for the antiviral mechanism. Plant J. 5, 173-183
    • (1994) Plant J. , vol.5 , pp. 173-183
    • Bonness, M.S.1    Ready, M.P.2    Irvin, J.D.3    Mabry, T.J.4
  • 50
    • 0016412390 scopus 로고
    • Energetics of ligand binding to proteins
    • Weber, G. (1975) Energetics of ligand binding to proteins. Adv. Protein Chem. 29, 1-83
    • (1975) Adv. Protein Chem. , vol.29 , pp. 1-83
    • Weber, G.1
  • 51
    • 0021766663 scopus 로고
    • Cooperative interactions in the system ribosomes-ribosomal protein S1-polynucleotide triplets
    • Goss, D. J., Parkhurst, L. J., Mehta, A. M., and Wahba, A. J. (1984) Cooperative interactions in the system ribosomes-ribosomal protein S1-polynucleotide triplets. Biochemistry 23, 6522-6529
    • (1984) Biochemistry , vol.23 , pp. 6522-6529
    • Goss, D.J.1    Parkhurst, L.J.2    Mehta, A.M.3    Wahba, A.J.4
  • 52
    • 0025807995 scopus 로고
    • Interaction of wheat germ protein synthesis initiation factors eIF-3, eIF-(iso)4F, and eIF-4F with mRNA analogues
    • Carberry, S. E., and Goss, D. J. (1991) Interaction of wheat germ protein synthesis initiation factors eIF-3, eIF-(iso)4F, and eIF-4F with mRNA analogues. Biochemistry 30, 6977-6982
    • (1991) Biochemistry , vol.30 , pp. 6977-6982
    • Carberry, S.E.1    Goss, D.J.2
  • 53
    • 0014481723 scopus 로고
    • Electron microscopy of pokeweed leaf cells infected with pokeweed mosaic virus
    • Kim, K. S., and Fulton, J.P. (1969) Electron microscopy of pokeweed leaf cells infected with pokeweed mosaic virus. Virology 37, 297-308
    • (1969) Virology , vol.37 , pp. 297-308
    • Kim, K.S.1    Fulton, J.P.2


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