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Volumn 9, Issue 5, 1998, Pages 534-548

Recent advances in producing and selecting functional proteins by using cell-free translation

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; MEMBRANE PROTEIN; MESSENGER RNA; MUTANT PROTEIN;

EID: 0032191388     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-1669(98)80042-6     Document Type: Article
Times cited : (130)

References (121)
  • 1
    • 0002688443 scopus 로고
    • Ribosome preparation and cell-free protein synthesis
    • A. Dahlberg, R.A. Garrot, P.B. Moore, D. Schlessinger, Warner J.R. Washington DC: American Society for Microbiology
    • Spirin AS. Ribosome preparation and cell-free protein synthesis. Dahlberg A, Garrot RA, Moore PB, Schlessinger D, Warner JR. The Ribosome: Structure, Function and Evolution. 2 ieHill EH:1990;56-70 American Society for Microbiology, Washington DC.
    • (1990) The Ribosome: Structure, Function and Evolution , vol.2 , pp. 56-70
    • Spirin, A.S.1
  • 2
    • 0029152885 scopus 로고
    • The potentials of the in vitro biosynthesis system
    • Stiege W, Erdmann VA. The potentials of the in vitro biosynthesis system. J Biotechnol. 41:1995;81-90.
    • (1995) J Biotechnol , vol.41 , pp. 81-90
    • Stiege, W.1    Erdmann, V.A.2
  • 3
    • 0015871909 scopus 로고
    • In vitro synthesis of protein in microbial systems
    • Zubay G. In vitro synthesis of protein in microbial systems. Annu Rev Genet. 7:1973;267-287.
    • (1973) Annu Rev Genet , vol.7 , pp. 267-287
    • Zubay, G.1
  • 4
    • 0000339265 scopus 로고
    • Efficient translation of tobacco mosaic virus RNA and rabbit globin 9S RNA in a cell-free system from commercial wheat germ
    • Roberts BE, Patterson BM. Efficient translation of tobacco mosaic virus RNA and rabbit globin 9S RNA in a cell-free system from commercial wheat germ. Proc Natl Sci USA. 70:1973;2330-2334.
    • (1973) Proc Natl Sci USA , vol.70 , pp. 2330-2334
    • Roberts, B.E.1    Patterson, B.M.2
  • 5
    • 0029256490 scopus 로고
    • Continously coupled transcription-translation system for the production of rice cytoplasmic aldolase
    • Tulin EE, Ken-Ichi T, Shin-Ichiro E. Continously coupled transcription-translation system for the production of rice cytoplasmic aldolase. Biotechnol Bioeng. 45:1995;511-516.
    • (1995) Biotechnol Bioeng , vol.45 , pp. 511-516
    • Tulin, E.E.1    Ken-Ichi, T.2    Shin-Ichiro, E.3
  • 6
    • 0017191401 scopus 로고
    • An efficient mRNA-dependent translation system from reticulocyte lysates
    • Pelham HRB, Jackson RJ. An efficient mRNA-dependent translation system from reticulocyte lysates. Eur J Biochem. 67:1976;247-256.
    • (1976) Eur J Biochem , vol.67 , pp. 247-256
    • Pelham, H.R.B.1    Jackson, R.J.2
  • 7
    • 0030817097 scopus 로고    scopus 로고
    • Biochemical energy consumption by wheat germ extract during cell-free systhesis
    • of special interest. The report shows that the sudden cessation of protein synthesis in a wheat germ cell-free system is mainly caused by the rapid dephosphorylation of ATP and GTP. The authors demonstrate that energy replenishment is necessary for continuous protein synthesis.
    • Yao SL, Shen XC, Suzuki E. Biochemical energy consumption by wheat germ extract during cell-free systhesis. of special interest J Ferment Bioeng. 84:1997;7-13 The report shows that the sudden cessation of protein synthesis in a wheat germ cell-free system is mainly caused by the rapid dephosphorylation of ATP and GTP. The authors demonstrate that energy replenishment is necessary for continuous protein synthesis.
    • (1997) J Ferment Bioeng , vol.84 , pp. 7-13
    • Yao, S.L.1    Shen, X.C.2    Suzuki, E.3
  • 9
    • 0021107166 scopus 로고
    • Restoration of protein synthesis in lysed rabbit reticulocytes by the enzymatic removal of adenosine 5′-monophosphate with either AMP deaminase or AMP nucleosidase
    • Mosca JD, Wu JM, Suhadolnik PJ. Restoration of protein synthesis in lysed rabbit reticulocytes by the enzymatic removal of adenosine 5′-monophosphate with either AMP deaminase or AMP nucleosidase. Biochemistry. 22:1983;346-354.
    • (1983) Biochemistry , vol.22 , pp. 346-354
    • Mosca, J.D.1    Wu, J.M.2    Suhadolnik, P.J.3
  • 10
    • 0022382593 scopus 로고
    • Nucleoside diphosphate regulation of overall rates of protein biosynthesis acting on the level of initiation
    • Hucul JA, Henshaw EC, Young DA. Nucleoside diphosphate regulation of overall rates of protein biosynthesis acting on the level of initiation. J Biol Chem. 260:1985;15585-15591.
    • (1985) J Biol Chem , vol.260 , pp. 15585-15591
    • Hucul, J.A.1    Henshaw, E.C.2    Young, D.A.3
  • 11
    • 0023653333 scopus 로고
    • 5′-adenosin monophosphate inhibits ternary complex formation by rat liver elF2
    • Felipo V, Grosolia S. 5′-adenosin monophosphate inhibits ternary complex formation by rat liver elF2. Biochem Biophys Res Commun. 146:1987;1079-1083.
    • (1987) Biochem Biophys Res Commun , vol.146 , pp. 1079-1083
    • Felipo, V.1    Grosolia, S.2
  • 12
    • 0030592121 scopus 로고    scopus 로고
    • Cooperativity of stabilized mRNA and enhanced translational activity in the cell-free system
    • Kitaoka Y, Nishimura N, Niwano M. Cooperativity of stabilized mRNA and enhanced translational activity in the cell-free system. J Biotechnol. 48:1996;1-8.
    • (1996) J Biotechnol , vol.48 , pp. 1-8
    • Kitaoka, Y.1    Nishimura, N.2    Niwano, M.3
  • 13
    • 0030974381 scopus 로고    scopus 로고
    • Accumulation of translational inhibitor during multi-hour cell-free protein synthesis reaction using rabbit reticulocyte lysate
    • Nakano H, Matsuda K, Okumura R, Yamane T. Accumulation of translational inhibitor during multi-hour cell-free protein synthesis reaction using rabbit reticulocyte lysate. J Ferment Bioeng. 83:1997;470-473.
    • (1997) J Ferment Bioeng , vol.83 , pp. 470-473
    • Nakano, H.1    Matsuda, K.2    Okumura, R.3    Yamane, T.4
  • 14
    • 0021066891 scopus 로고
    • Activation of the heme-stabilized translational inhibitor of reticulocyte lysates by calcium ions and phospholipid
    • de Haro C, de Herreros AG, Ochoa S. Activation of the heme-stabilized translational inhibitor of reticulocyte lysates by calcium ions and phospholipid. Proc Natl Acad Sci USA. 80:1983;6843-6847.
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 6843-6847
    • De Haro, C.1    De Herreros, A.G.2    Ochoa, S.3
  • 16
    • 85007941447 scopus 로고
    • Prolonged cell-free protein synthesis in a batch system using wheat germ extract
    • Kawarasaki Y, Nakano H, Yamane T. Prolonged cell-free protein synthesis in a batch system using wheat germ extract. Biosci Biotechnol Biochem. 58:1994;1911-1913.
    • (1994) Biosci Biotechnol Biochem , vol.58 , pp. 1911-1913
    • Kawarasaki, Y.1    Nakano, H.2    Yamane, T.3
  • 17
    • 0031361629 scopus 로고    scopus 로고
    • A novel method of high yield cell-free protein synthesis
    • Yao S, Shen XC, Terada S, Suzuki E. A novel method of high yield cell-free protein synthesis. J Ferment Bioeng. 84:1997;548-552.
    • (1997) J Ferment Bioeng , vol.84 , pp. 548-552
    • Yao, S.1    Shen, X.C.2    Terada, S.3    Suzuki, E.4
  • 18
    • 0028954219 scopus 로고
    • A long-lived batch reaction system of cell-free protein synthesis
    • Kawarasaki Y, Kawai T, Nakano H, Yamane T. A long-lived batch reaction system of cell-free protein synthesis. Anal Biochem. 226:1995;320-324.
    • (1995) Anal Biochem , vol.226 , pp. 320-324
    • Kawarasaki, Y.1    Kawai, T.2    Nakano, H.3    Yamane, T.4
  • 19
    • 85007974354 scopus 로고
    • An increased rate of cell-free protein synthesis by condensing wheat germ extract with ultrafiltration membranes
    • Nakano H, Tananka T, Kawarasaki Y, Yamane T. An increased rate of cell-free protein synthesis by condensing wheat germ extract with ultrafiltration membranes. Biosci Biotechnol Biochem. 58:1994;631-634.
    • (1994) Biosci Biotechnol Biochem , vol.58 , pp. 631-634
    • Nakano, H.1    Tananka, T.2    Kawarasaki, Y.3    Yamane, T.4
  • 20
    • 0029956987 scopus 로고    scopus 로고
    • A highly efficient cell-free protein synthesis system from Escherichia coli
    • Kim DM, Kigawa T, Chen CY, Yokoyama S. A highly efficient cell-free protein synthesis system from Escherichia coli. Eur J Biochem. 239:1996;881-886.
    • (1996) Eur J Biochem , vol.239 , pp. 881-886
    • Kim, D.M.1    Kigawa, T.2    Chen, C.Y.3    Yokoyama, S.4
  • 21
    • 0029956987 scopus 로고    scopus 로고
    • A highly efficient cell-free protein synthesis system from Escherichia coli
    • Kudlicki W, Kramer G, Hardesty B. A highly efficient cell-free protein synthesis system from Escherichia coli. Eur J Biochem. 239:1992;881-886.
    • (1992) Eur J Biochem , vol.239 , pp. 881-886
    • Kudlicki, W.1    Kramer, G.2    Hardesty, B.3
  • 22
    • 0029839889 scopus 로고    scopus 로고
    • Use of bacteriophage RNA polymerase in RNA synthesis
    • Gurevich VV. Use of bacteriophage RNA polymerase in RNA synthesis. Methods Enzymol. 275:1996;382-397.
    • (1996) Methods Enzymol , vol.275 , pp. 382-397
    • Gurevich, V.V.1
  • 23
    • 0030974119 scopus 로고    scopus 로고
    • In vitro selection and evolution of functional proteins by using ribosome display
    • of outstanding interest. First experimental demonstration of selection of a folded protein for ligand binding using ribosome display. Selected antigen-binding antibody fragments were shown to have evolved over many cycles.
    • Hanes J, Plückthun A. In vitro selection and evolution of functional proteins by using ribosome display. of outstanding interest Proc Natl Acad Sci USA. 94:1997;4937-4942 First experimental demonstration of selection of a folded protein for ligand binding using ribosome display. Selected antigen-binding antibody fragments were shown to have evolved over many cycles.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4937-4942
    • Hanes, J.1    Plückthun, A.2
  • 25
    • 0020645081 scopus 로고
    • Prokaryotic coupled transcription-translation
    • Chen HZ, Zubay G. Prokaryotic coupled transcription-translation. Methods Enzymol. 101:1983;674-690.
    • (1983) Methods Enzymol , vol.101 , pp. 674-690
    • Chen, H.Z.1    Zubay, G.2
  • 26
    • 0025989820 scopus 로고
    • A coupled in vitro transcription-translation system for the exclusive synthesis of polypeptides from the T7 promotor
    • Nevin DE, Pratt JM. A coupled in vitro transcription-translation system for the exclusive synthesis of polypeptides from the T7 promotor. FEBS Lett. 291:1991;259-263.
    • (1991) FEBS Lett , vol.291 , pp. 259-263
    • Nevin, D.E.1    Pratt, J.M.2
  • 27
    • 0029867421 scopus 로고    scopus 로고
    • Use of T7 RNA polymerase in an optimized Escherichia coli coupled in vitro transcription-translation system. Application in regulatory studies and expression of long transcription units
    • Köhrer C, Mayer C, Grübner P, Piendl W. Use of T7 RNA polymerase in an optimized Escherichia coli coupled in vitro transcription-translation system. Application in regulatory studies and expression of long transcription units. Eur J Biochem. 236:1996;234-239.
    • (1996) Eur J Biochem , vol.236 , pp. 234-239
    • Köhrer, C.1    Mayer, C.2    Grübner, P.3    Piendl, W.4
  • 28
    • 0026715079 scopus 로고
    • Plasmid cDNA-directed synthesis in a coupled eukaryotic in vitro transcription-translation system
    • Craig D, Howell MT, Gibbs CL, Hunt T, Jackson RJ. Plasmid cDNA-directed synthesis in a coupled eukaryotic in vitro transcription-translation system. Nucleic Acids Res. 20:1992;4987-4995.
    • (1992) Nucleic Acids Res , vol.20 , pp. 4987-4995
    • Craig, D.1    Howell, M.T.2    Gibbs, C.L.3    Hunt, T.4    Jackson, R.J.5
  • 29
    • 0027191822 scopus 로고
    • Gene expression in cell-free systems on preparative scale
    • Baranov VI, Spirin AS. Gene expression in cell-free systems on preparative scale. Methods Enzymol. 217:1993;123-142.
    • (1993) Methods Enzymol , vol.217 , pp. 123-142
    • Baranov, V.I.1    Spirin, A.S.2
  • 30
    • 0024988991 scopus 로고
    • Translation initiation in Escherichia coli: Old and new questions
    • Jacques N, Dreyfus M. Translation initiation in Escherichia coli: old and new questions. Mol Microbiol. 4:1990;1063-1067.
    • (1990) Mol Microbiol , vol.4 , pp. 1063-1067
    • Jacques, N.1    Dreyfus, M.2
  • 31
    • 0031029555 scopus 로고    scopus 로고
    • In vitro scanning saturation mutagenesis of an antibody binding pocket
    • of special interest. By combining PCR-mutagenesis and direct in vitro expression of the resulting PCR products the authors could rapidly analyze the influence of each amino acid in an antibody binding pocket.
    • Burks EA, Chen G, Georgiou G, Iverson BL. In vitro scanning saturation mutagenesis of an antibody binding pocket. of special interest Proc Natl Acad Sci USA. 94:1997;412-417 By combining PCR-mutagenesis and direct in vitro expression of the resulting PCR products the authors could rapidly analyze the influence of each amino acid in an antibody binding pocket.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 412-417
    • Burks, E.A.1    Chen, G.2    Georgiou, G.3    Iverson, B.L.4
  • 32
    • 0025737880 scopus 로고
    • Use in in vitro protein synthesis from polymerase chain reaction-generated templates to study interaction of Escherichia coli transcription factors with core RNA polymerase and for epitope mapping of monoclonal antibodies
    • Lesley SA, Brow MA, Burgess RR. Use in in vitro protein synthesis from polymerase chain reaction-generated templates to study interaction of Escherichia coli transcription factors with core RNA polymerase and for epitope mapping of monoclonal antibodies. J Biol Chem. 266:1991;2632-2638.
    • (1991) J Biol Chem , vol.266 , pp. 2632-2638
    • Lesley, S.A.1    Brow, M.A.2    Burgess, R.R.3
  • 33
    • 0031559892 scopus 로고    scopus 로고
    • Direct expression of PCR products in a cell-free transcription/translation system: Synthesis of antibacterial peptide cecropin
    • Martemyanov KA, Spirin AS, Gudkov AT. Direct expression of PCR products in a cell-free transcription/translation system: synthesis of antibacterial peptide cecropin. FEBS Lett. 414:1997;268-270.
    • (1997) FEBS Lett , vol.414 , pp. 268-270
    • Martemyanov, K.A.1    Spirin, A.S.2    Gudkov, A.T.3
  • 34
    • 0028854756 scopus 로고
    • RQ RNA vectors: Prospects for cell-free gene amplification, expression and cloning
    • Chetverin AB, Spirin AS. RQ RNA vectors: prospects for cell-free gene amplification, expression and cloning. Prog Nucleic Acid Res Mol Biol. 51:1995;225-270.
    • (1995) Prog Nucleic Acid Res Mol Biol , vol.51 , pp. 225-270
    • Chetverin, A.B.1    Spirin, A.S.2
  • 35
    • 0021760394 scopus 로고
    • Selection of initiation sites by eukaryotic ribosomes: Effect of inserting AUG triplets upstream from the coding sequence for preproinsulin
    • Kozak M. Selection of initiation sites by eukaryotic ribosomes: effect of inserting AUG triplets upstream from the coding sequence for preproinsulin. Nucleic Acids Res. 12:1984;3873-3893.
    • (1984) Nucleic Acids Res , vol.12 , pp. 3873-3893
    • Kozak, M.1
  • 36
    • 0031010944 scopus 로고    scopus 로고
    • Recognition of AUG and alternative initiator codons is augmented by G in position of +4 but is not generally affected by the nucleotides in positions +5 and +6
    • Kozak M. Recognition of AUG and alternative initiator codons is augmented by G in position of +4 but is not generally affected by the nucleotides in positions +5 and +6. EMBO J. 16:1997;2482-2492.
    • (1997) EMBO J , vol.16 , pp. 2482-2492
    • Kozak, M.1
  • 37
    • 0030980469 scopus 로고    scopus 로고
    • Functional importance of RNA interactions in selection of translation initiation codons
    • Sprengart ML, Porter AG. Functional importance of RNA interactions in selection of translation initiation codons. Mol Microbiol. 24:1997;19-28.
    • (1997) Mol Microbiol , vol.24 , pp. 19-28
    • Sprengart, M.L.1    Porter, A.G.2
  • 38
    • 0025088597 scopus 로고
    • MRNA acetylated at 2′-OH groups of ribose residues in functionally active in the cell-free translation system for wheat embryos
    • Ovodov SY, Alakhov YB. mRNA acetylated at 2′-OH groups of ribose residues in functionally active in the cell-free translation system for wheat embryos. FEBS Lett. 270:1990;111-114.
    • (1990) FEBS Lett , vol.270 , pp. 111-114
    • Ovodov, S.Y.1    Alakhov, Y.B.2
  • 39
    • 0028280813 scopus 로고
    • Efficient expression of E. coli dihydrofolate reductase gene by an in vitro translation system using phosphorothioate mRNA
    • Tohda H, Chikazumi N, Ueda T, Nishikawa K, Watanabe K. Efficient expression of E. coli dihydrofolate reductase gene by an in vitro translation system using phosphorothioate mRNA. J Biotechnol. 34:1994;61-69.
    • (1994) J Biotechnol , vol.34 , pp. 61-69
    • Tohda, H.1    Chikazumi, N.2    Ueda, T.3    Nishikawa, K.4    Watanabe, K.5
  • 40
    • 0025974517 scopus 로고
    • Phosphorothioate-containing RNAs show mRNA activity in the prokaryotic translation system in vitro
    • Ueda T, Tohda H, Chikazumi N, Eckstein F, Watanabe K. Phosphorothioate-containing RNAs show mRNA activity in the prokaryotic translation system in vitro. Nucleic Acids Res. 19:1991;547-552.
    • (1991) Nucleic Acids Res , vol.19 , pp. 547-552
    • Ueda, T.1    Tohda, H.2    Chikazumi, N.3    Eckstein, F.4    Watanabe, K.5
  • 42
    • 0031951386 scopus 로고    scopus 로고
    • MRNA stabilization by the ompA 5′ untranslated region: Two protective elements hinder distinct pathways for mRNA degradation
    • Arnold TE, Belasco JG. mRNA stabilization by the ompA 5′ untranslated region: two protective elements hinder distinct pathways for mRNA degradation. RNA. 4:1998;319-330.
    • (1998) RNA , vol.4 , pp. 319-330
    • Arnold, T.E.1    Belasco, J.G.2
  • 43
    • 0029165020 scopus 로고    scopus 로고
    • MRNA stability in mammalian cells
    • Ross J. mRNA stability in mammalian cells. Microbiol Rev. 59:1996;423-450.
    • (1996) Microbiol Rev , vol.59 , pp. 423-450
    • Ross, J.1
  • 44
    • 0030836863 scopus 로고    scopus 로고
    • Structural determinants in AUF1 required for high affinity binding to A+U-rich elements
    • DeMaria CT, Sun Y, Wagner BJ, Brewer G. Structural determinants in AUF1 required for high affinity binding to A+U-rich elements. J Biol Chem. 272:1997;27635-27643.
    • (1997) J Biol Chem , vol.272 , pp. 27635-27643
    • DeMaria, C.T.1    Sun, Y.2    Wagner, B.J.3    Brewer, G.4
  • 45
    • 0030949303 scopus 로고    scopus 로고
    • Life and death in the cytoplasm: Messages from the 3′ end
    • Wickens M, Anderson P, Jackson RJ. Life and death in the cytoplasm: messages from the 3′ end. Curr Opin Gen Dev. 7:1997;220-232.
    • (1997) Curr Opin Gen Dev , vol.7 , pp. 220-232
    • Wickens, M.1    Anderson, P.2    Jackson, R.J.3
  • 46
    • 0030797564 scopus 로고    scopus 로고
    • Translational initiation factor elF-G mediates in vitro poly(A) tail-dependent translation
    • of outstanding interest. The authors provide evidence that yeast translation factor elF-4G features a binding site for poly(A)-binding protein Pab 1p. This leads to an interaction between elF-4G, a subunit of cap-associated initiation factor elF-4F at the 5′ end of the mRNA and poly(A)-Pab1p at the 3′ ends of the mRNA.
    • Tarun SZ, Wells SE, Deardoff JA, Sachs AB. Translational initiation factor elF-G mediates in vitro poly(A) tail-dependent translation. of outstanding interest Proc Natl Acad Sci USA. 94:1997;9046-9051 The authors provide evidence that yeast translation factor elF-4G features a binding site for poly(A)-binding protein Pab 1p. This leads to an interaction between elF-4G, a subunit of cap-associated initiation factor elF-4F at the 5′ end of the mRNA and poly(A)-Pab1p at the 3′ ends of the mRNA.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 9046-9051
    • Tarun, S.Z.1    Wells, S.E.2    Deardoff, J.A.3    Sachs, A.B.4
  • 47
    • 0030952218 scopus 로고    scopus 로고
    • Translation initiation factors elF-iso4G and elF-4B interact with the poly(A)-binding protein and increase its RNA binding activity
    • of outstanding interest. This report demonstrates the interaction between cap-associated initiation factor elF-iso4F and elF-4B with the poly(A)-binding protein (PABP) in plants. elF-iso4G, the subunit of elF-iso4F, was found to be involved in the binding of PABP. A similar mechanism in yeast and plants seems to participate in 3′-UTR regulation of mRNA initiation and turnover.
    • Le H, Tanguay RL, Balasta ML, Wei CC, Browning KS, Metz AM, Goss DJ, Gallie DR. Translation initiation factors elF-iso4G and elF-4B interact with the poly(A)-binding protein and increase its RNA binding activity. of outstanding interest J Biol Chem. 272:1997;16247-16255 This report demonstrates the interaction between cap-associated initiation factor elF-iso4F and elF-4B with the poly(A)-binding protein (PABP) in plants. elF-iso4G, the subunit of elF-iso4F, was found to be involved in the binding of PABP. A similar mechanism in yeast and plants seems to participate in 3′-UTR regulation of mRNA initiation and turnover.
    • (1997) J Biol Chem , vol.272 , pp. 16247-16255
    • Le, H.1    Tanguay, R.L.2    Balasta, M.L.3    Wei, C.C.4    Browning, K.S.5    Metz, A.M.6    Goss, D.J.7    Gallie, D.R.8
  • 48
    • 0032473972 scopus 로고    scopus 로고
    • Interaction of polyadenylate-binding protein with the eF4G homologue PAIP enhances translation
    • of special interest. The authors propose that the interaction between mRNA ends in mammals is mediated by a novel poly(A)-binding protein, PAIP, which is homologous to the central portion of eF-4G. PAIP also interacts with another subunit of cap-binding factor elF-4F, ATP-dependent RNA helicase, elF-4A.
    • Craig AWB, Haghighat A, Yu ATK, Sonenberg A. Interaction of polyadenylate-binding protein with the eF4G homologue PAIP enhances translation. of special interest Nature. 392:1998;520-522 The authors propose that the interaction between mRNA ends in mammals is mediated by a novel poly(A)-binding protein, PAIP, which is homologous to the central portion of eF-4G. PAIP also interacts with another subunit of cap-binding factor elF-4F, ATP-dependent RNA helicase, elF-4A.
    • (1998) Nature , vol.392 , pp. 520-522
    • Craig, A.W.B.1    Haghighat, A.2    Yu, A.T.K.3    Sonenberg, A.4
  • 49
    • 0023092598 scopus 로고
    • Enhanced translation of chimaeric messenger RNAs containing a plant viral untranslated leader sequence
    • Jobling SA, Gehrke L. Enhanced translation of chimaeric messenger RNAs containing a plant viral untranslated leader sequence. Nature. 325:1987;622-625.
    • (1987) Nature , vol.325 , pp. 622-625
    • Jobling, S.A.1    Gehrke, L.2
  • 50
    • 0023663363 scopus 로고
    • The 5′-leader sequence of tobacco mosaic virus RNA enhances the expression of foreign gene transcripts in vitro and in vivo
    • Gallie DR, Sleat DE, Watts JW, Turner PC, Wilson TMA. The 5′-leader sequence of tobacco mosaic virus RNA enhances the expression of foreign gene transcripts in vitro and in vivo. Nucleic Acids Res. 15:1987;3257-3273.
    • (1987) Nucleic Acids Res , vol.15 , pp. 3257-3273
    • Gallie, D.R.1    Sleat, D.E.2    Watts, J.W.3    Turner, P.C.4    Wilson, T.M.A.5
  • 51
    • 0027256025 scopus 로고
    • The 3′ untranslated region of satellite tobacco necrosis virus RNA stimulates translation in vitro
    • Danthinne X, Seurinck J, Meulewater F, van Montagu M, Cornelissen M. The 3′ untranslated region of satellite tobacco necrosis virus RNA stimulates translation in vitro. Mol Cell Biol. 13:1993;3340-3349.
    • (1993) Mol Cell Biol , vol.13 , pp. 3340-3349
    • Danthinne, X.1    Seurinck, J.2    Meulewater, F.3    Van Montagu, M.4    Cornelissen, M.5
  • 52
    • 85030346936 scopus 로고
    • The 5′ and 3′ untranslated regions of satellite tobacco necrosis virus RNA affect translational efficiency and dependence on a 5′ cap structure
    • Timmer RT, Benkowski LA, Schodin D, Lax SR, Metz AM, Ravel JM, Browning KS. The 5′ and 3′ untranslated regions of satellite tobacco necrosis virus RNA affect translational efficiency and dependence on a 5′ cap structure. Mol Cell Biol. 13:1993;3340-3349.
    • (1993) Mol Cell Biol , vol.13 , pp. 3340-3349
    • Timmer, R.T.1    Benkowski, L.A.2    Schodin, D.3    Lax, S.R.4    Metz, A.M.5    Ravel, J.M.6    Browning, K.S.7
  • 53
    • 0028113083 scopus 로고
    • Enhancing effect of the 3′-untranslated region of tobacco mosaic virus RNA on protein synthesis in vitro
    • Zeyenko VV, Ryabova LA, Gallie DR, Spirin AS. Enhancing effect of the 3′-untranslated region of tobacco mosaic virus RNA on protein synthesis in vitro. FEBS Lett. 354:1994;271-273.
    • (1994) FEBS Lett , vol.354 , pp. 271-273
    • Zeyenko, V.V.1    Ryabova, L.A.2    Gallie, D.R.3    Spirin, A.S.4
  • 54
    • 0028266931 scopus 로고
    • MRNA translation: Influence of the 5′ and 3′ untranslated regions
    • Sonnenberg N. mRNA translation: influence of the 5′ and 3′ untranslated regions. Curr Opin Genet Dev. 4:1994;310-315.
    • (1994) Curr Opin Genet Dev , vol.4 , pp. 310-315
    • Sonnenberg, N.1
  • 55
    • 0029888089 scopus 로고    scopus 로고
    • Synthesis and assembly of retrovirus Gag precursors into immature capsids in vitro
    • Sakalian M, Parker SD, Weldon RA, Hunter E. Synthesis and assembly of retrovirus Gag precursors into immature capsids in vitro. J Virol. 70:1996;3706-3715.
    • (1996) J Virol , vol.70 , pp. 3706-3715
    • Sakalian, M.1    Parker, S.D.2    Weldon, R.A.3    Hunter, E.4
  • 56
    • 0029971659 scopus 로고    scopus 로고
    • Cis-acting element and trans-acting factors for accurate translation of chloroplast psbA mRNAs: Development of an in vitro translation system from tobacco chloroplasts
    • Hirose T, Sugiura M. Cis-acting element and trans-acting factors for accurate translation of chloroplast psbA mRNAs: development of an in vitro translation system from tobacco chloroplasts. EMBO J. 15:1996;1687-1695.
    • (1996) EMBO J , vol.15 , pp. 1687-1695
    • Hirose, T.1    Sugiura, M.2
  • 57
    • 0030993197 scopus 로고    scopus 로고
    • Translation-competent extracts from Saccharomyces cerevisiae: Effects of L-A RNA, 5′ cap, 3′ poly(A) tail on translational efficiency of mRNAs
    • Iizuka N, Sarnow P. Translation-competent extracts from Saccharomyces cerevisiae: effects of L-A RNA, 5′ cap, 3′ poly(A) tail on translational efficiency of mRNAs. Methods. 11:1997;353-360.
    • (1997) Methods , vol.11 , pp. 353-360
    • Iizuka, N.1    Sarnow, P.2
  • 58
    • 0028884380 scopus 로고
    • A common function for mRNA 5′ and 3′ ends in translation initiation in yeast
    • Tarun SZ, Sachs AB. A common function for mRNA 5′ and 3′ ends in translation initiation in yeast. Genes Dev. 9:1995;2997-3007.
    • (1995) Genes Dev , vol.9 , pp. 2997-3007
    • Tarun, S.Z.1    Sachs, A.B.2
  • 59
    • 0024297305 scopus 로고
    • A continuous cell-free translation system capable of producing polypeptides in high yield
    • Spirin AS, Baranov VI, Ryabova LA, Ovodov SY, Alakhov YB. A continuous cell-free translation system capable of producing polypeptides in high yield. Science. 242:1988;1162-1164.
    • (1988) Science , vol.242 , pp. 1162-1164
    • Spirin, A.S.1    Baranov, V.I.2    Ryabova, L.A.3    Ovodov, S.Y.4    Alakhov, Y.B.5
  • 60
    • 0002587317 scopus 로고
    • Cell-free protein bioreactor
    • P. Todd, S.K. Skidar, Bier M. Washington DC: American Chemical Society
    • Spirin AS. Cell-free protein bioreactor. Todd P, Skidar SK, Bier M. Frontiers in Bioprocessing II. 1991;31-43 American Chemical Society, Washington DC.
    • (1991) Frontiers in Bioprocessing II , pp. 31-43
    • Spirin, A.S.1
  • 61
    • 0027613253 scopus 로고
    • Production of dihydrofolate reductase by an improved continous flow cell-free translation system using wheat germ extract
    • Endo Y, Oka T, Ogata K, Natori Y. Production of dihydrofolate reductase by an improved continous flow cell-free translation system using wheat germ extract. Tokshima J Exp Med. 40:1993;13-17.
    • (1993) Tokshima J Exp Med , vol.40 , pp. 13-17
    • Endo, Y.1    Oka, T.2    Ogata, K.3    Natori, Y.4
  • 62
    • 0027520038 scopus 로고
    • Synthesis of preparative amounts of biologically active interleukin-6 using a continous-flow cell-free translation system
    • Volyanik EV, Dalley A, McKay IA, Leigh I, Williams NS, Bustin SA. Synthesis of preparative amounts of biologically active interleukin-6 using a continous-flow cell-free translation system. Anal Biochem. 214:1993;289-294.
    • (1993) Anal Biochem , vol.214 , pp. 289-294
    • Volyanik, E.V.1    Dalley, A.2    McKay, I.A.3    Leigh, I.4    Williams, N.S.5    Bustin, S.A.6
  • 63
    • 0025787535 scopus 로고
    • A continuous cell-free protein synthesis system for coupled transcription-translation
    • Kigawa T, Yokoyama S. A continuous cell-free protein synthesis system for coupled transcription-translation. J Biochem. 110:1991;166-168.
    • (1991) J Biochem , vol.110 , pp. 166-168
    • Kigawa, T.1    Yokoyama, S.2
  • 65
    • 0030250637 scopus 로고    scopus 로고
    • A semicontinous prokaryotic coupled transcription/translation system using a dialysis membrane
    • Kim DM, Choi CY. A semicontinous prokaryotic coupled transcription/translation system using a dialysis membrane. Biotechnol Prog. 12:1996;645-649.
    • (1996) Biotechnol Prog , vol.12 , pp. 645-649
    • Kim, D.M.1    Choi, C.Y.2
  • 66
    • 0024842214 scopus 로고
    • Gene expression in a cell-free system on the preparative scale
    • Baranov VI, Morozov IY, Ortlepp SA, Spirin AS. Gene expression in a cell-free system on the preparative scale. Gene. 84:1989;463-466.
    • (1989) Gene , vol.84 , pp. 463-466
    • Baranov, V.I.1    Morozov, I.Y.2    Ortlepp, S.A.3    Spirin, A.S.4
  • 67
    • 0014353859 scopus 로고
    • The energy charge of the adenylate pool as a regulatory parameter: Interaction with feedback modifiers
    • Atkinson DE. The energy charge of the adenylate pool as a regulatory parameter: interaction with feedback modifiers. Biochemistry. 7:1968;4030-4034.
    • (1968) Biochemistry , vol.7 , pp. 4030-4034
    • Atkinson, D.E.1
  • 68
    • 0030224890 scopus 로고    scopus 로고
    • Dihydrofolate reductase synthesis in the presence of immobilized methotrexate. An approach to a continuous cell-free protein synthesis system
    • Marszal E, Scouten WH. Dihydrofolate reductase synthesis in the presence of immobilized methotrexate. An approach to a continuous cell-free protein synthesis system. J Mol Recognit. 9:1996;543-548.
    • (1996) J Mol Recognit , vol.9 , pp. 543-548
    • Marszal, E.1    Scouten, W.H.2
  • 71
    • 0031468437 scopus 로고    scopus 로고
    • Cotranslational protein folding
    • of special interest. Concise review about the early events in in vivo protein folding. The authors summarize the role of chaperones and folding kinetics during protein biosynthesis.
    • Federov AN, Baldwin TO. Cotranslational protein folding. of special interest J Biol Chem. 272:1997;32715-32718 Concise review about the early events in in vivo protein folding. The authors summarize the role of chaperones and folding kinetics during protein biosynthesis.
    • (1997) J Biol Chem , vol.272 , pp. 32715-32718
    • Federov, A.N.1    Baldwin, T.O.2
  • 72
    • 0030844281 scopus 로고    scopus 로고
    • Recombination of protein domains facilitated by co-translational folding in eucaryotes
    • Netzer WJ, Hartl FU. Recombination of protein domains facilitated by co-translational folding in eucaryotes. Nature. 388:1997;343-349.
    • (1997) Nature , vol.388 , pp. 343-349
    • Netzer, W.J.1    Hartl, F.U.2
  • 73
    • 0028943041 scopus 로고
    • The importance of the N-terminal segment for DnaJ-mediated folding of rhodanese while bound to ribosomes as peptidyl-tRNA
    • Kudlicki W, Odom OW, Kramer G, Hardesty B, Merrill GA, Horowitz PM. The importance of the N-terminal segment for DnaJ-mediated folding of rhodanese while bound to ribosomes as peptidyl-tRNA. J Biol Chem. 18:1995;10650-10657.
    • (1995) J Biol Chem , vol.18 , pp. 10650-10657
    • Kudlicki, W.1    Odom, O.W.2    Kramer, G.3    Hardesty, B.4    Merrill, G.A.5    Horowitz, P.M.6
  • 74
    • 0028094779 scopus 로고
    • Folding of firefly luciferase during translation in a cell-free system
    • Kolb VA, Makeyev EV, Spirin AS. Folding of firefly luciferase during translation in a cell-free system. EMBO J. 13:1994;3631-3637.
    • (1994) EMBO J , vol.13 , pp. 3631-3637
    • Kolb, V.A.1    Makeyev, E.V.2    Spirin, A.S.3
  • 75
    • 0030025303 scopus 로고    scopus 로고
    • Enzymatic activity of the ribosome-bound nascent polypeptide
    • Makeyev EV, Kolb VA, Spirin AS. Enzymatic activity of the ribosome-bound nascent polypeptide. FEBS Lett. 378:1996;166-170.
    • (1996) FEBS Lett , vol.378 , pp. 166-170
    • Makeyev, E.V.1    Kolb, V.A.2    Spirin, A.S.3
  • 77
    • 0031574037 scopus 로고    scopus 로고
    • Antibody-ribosome-mRNA (ARM) complexes as efficient selection particles for in vitro display and evolution of antibody combining sites
    • of outstanding interest. Ribosome display of an antibody fragment with a commercial eukaryotic transcription/translation system
    • He M, Taussig MJ. Antibody-ribosome-mRNA (ARM) complexes as efficient selection particles for in vitro display and evolution of antibody combining sites. of outstanding interest Nucleic Acids Res. 25:1997;5132-5134 Ribosome display of an antibody fragment with a commercial eukaryotic transcription/translation system.
    • (1997) Nucleic Acids Res , vol.25 , pp. 5132-5134
    • He, M.1    Taussig, M.J.2
  • 78
    • 0030853281 scopus 로고    scopus 로고
    • Free luciferase may acquire a more favorable conformation than ribosome-associated luciferase for its activity expression
    • Yang F, Jing GZ, Zhou JM, Zheng YZ. Free luciferase may acquire a more favorable conformation than ribosome-associated luciferase for its activity expression. FEBS Lett. 417:1997;329-332.
    • (1997) FEBS Lett , vol.417 , pp. 329-332
    • Yang, F.1    Jing, G.Z.2    Zhou, J.M.3    Zheng, Y.Z.4
  • 79
    • 0030078788 scopus 로고    scopus 로고
    • Protein biogenesis: Chaperones for nascent polypeptides
    • Rassow J, Pfanner N. Protein biogenesis: chaperones for nascent polypeptides. Curr Biol. 6:1996;115-118.
    • (1996) Curr Biol , vol.6 , pp. 115-118
    • Rassow, J.1    Pfanner, N.2
  • 80
    • 0018647555 scopus 로고
    • Formation of intermolecular disulfide bonds on nascent immunoglobulin polypeptides
    • Bergman LW, Kuehl WM. Formation of intermolecular disulfide bonds on nascent immunoglobulin polypeptides. J Biol Chem. 254:1979;5690-5694.
    • (1979) J Biol Chem , vol.254 , pp. 5690-5694
    • Bergman, L.W.1    Kuehl, W.M.2
  • 81
    • 0028028387 scopus 로고
    • Building bridges: Disulphide bond formation in the cell
    • Bardwell JC. Building bridges: disulphide bond formation in the cell. Mol Microbiol. 14:1994;199-205.
    • (1994) Mol Microbiol , vol.14 , pp. 199-205
    • Bardwell, J.C.1
  • 83
    • 0031021109 scopus 로고    scopus 로고
    • Functional antibody production using cell-free translation: Effects of protein disulfide isomerase and chaperones
    • of special interest. The authors describe a thorough optimization of cell-free production of functional antibody fragments (scFvs). Protein disulfide isomerase and the molecular chaperones DnaJ and DnaK have the most prominent effect on the amount of functional and soluble scFv, respectively.
    • Ryabova LA, Desplancq D, Spirin AS, Plückthun A. Functional antibody production using cell-free translation: effects of protein disulfide isomerase and chaperones. of special interest Nat Biotechnol. 15:1997;79-84 The authors describe a thorough optimization of cell-free production of functional antibody fragments (scFvs). Protein disulfide isomerase and the molecular chaperones DnaJ and DnaK have the most prominent effect on the amount of functional and soluble scFv, respectively.
    • (1997) Nat Biotechnol , vol.15 , pp. 79-84
    • Ryabova, L.A.1    Desplancq, D.2    Spirin, A.S.3    Plückthun, A.4
  • 84
    • 0030048409 scopus 로고    scopus 로고
    • In vitro protein folding by ribosomes from Escherichia coli, wheat germ and rat liver: The role of 50S particle and its 23S RNA
    • Das B, Chattopadhyay S, Bega AK, Dasgupta C. In vitro protein folding by ribosomes from Escherichia coli, wheat germ and rat liver: the role of 50S particle and its 23S RNA. Eur J Biochem. 235:1996;613-621.
    • (1996) Eur J Biochem , vol.235 , pp. 613-621
    • Das, B.1    Chattopadhyay, S.2    Bega, A.K.3    Dasgupta, C.4
  • 85
    • 0030623528 scopus 로고    scopus 로고
    • Ribosomes and ribosomal RNA as chaperones for folding of proteins
    • Kudlicki W, Coffman A, Kramer G, Hardesty B. Ribosomes and ribosomal RNA as chaperones for folding of proteins. Fold Des. 2:1997;101-108.
    • (1997) Fold Des , vol.2 , pp. 101-108
    • Kudlicki, W.1    Coffman, A.2    Kramer, G.3    Hardesty, B.4
  • 86
    • 0029759715 scopus 로고    scopus 로고
    • Reactivation of denatured proteins by 23S ribosomal RNA: Role of domain V
    • Chattophadhyay A, Das B, Dasgupta C. Reactivation of denatured proteins by 23S ribosomal RNA: role of domain V. Proc Natl Acad Sci USA. 93:1996;8284-8287.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8284-8287
    • Chattophadhyay, A.1    Das, B.2    Dasgupta, C.3
  • 87
    • 0031448932 scopus 로고    scopus 로고
    • Renaturation of rhodanese by translational elongation factors (EF) Tu
    • Kudlicki W, Coffman A, Kramer G, Hardesty B. Renaturation of rhodanese by translational elongation factors (EF) Tu. J Biol Chem. 272:1997;32206-32210.
    • (1997) J Biol Chem , vol.272 , pp. 32206-32210
    • Kudlicki, W.1    Coffman, A.2    Kramer, G.3    Hardesty, B.4
  • 88
    • 0031895718 scopus 로고    scopus 로고
    • Preparation and application of chaperone-deficient Escherichia coli cell-free translation system
    • Kramer G, Zhang T, Kudliski W, Hardesty B. Preparation and application of chaperone-deficient Escherichia coli cell-free translation system. Methods Enzymol. 290:1998;18-26.
    • (1998) Methods Enzymol , vol.290 , pp. 18-26
    • Kramer, G.1    Zhang, T.2    Kudliski, W.3    Hardesty, B.4
  • 89
  • 90
    • 0030881723 scopus 로고    scopus 로고
    • Noncoded amino acid replacement probes of the aspartate aminotransferase mechanism
    • of outstanding interest. By incorporating unnatural amino acids into the enzyme using in vitro translation the authors could decipher key elements of the enzymatic mechanism.
    • Park Y, Luo J, Schultz PG, Kirsch JF. Noncoded amino acid replacement probes of the aspartate aminotransferase mechanism. of outstanding interest Biochemistry. 36:1997;10517-10525 By incorporating unnatural amino acids into the enzyme using in vitro translation the authors could decipher key elements of the enzymatic mechanism.
    • (1997) Biochemistry , vol.36 , pp. 10517-10525
    • Park, Y.1    Luo, J.2    Schultz, P.G.3    Kirsch, J.F.4
  • 92
    • 0030776931 scopus 로고    scopus 로고
    • Synthesis of region-labelled proteins for NMR studies by in vitro translation of column-coupled mRNAs
    • Pavlov MY, Freistoffer DV, Ehrenberg M. Synthesis of region-labelled proteins for NMR studies by in vitro translation of column-coupled mRNAs. Biochimie. 79:1997;415-422.
    • (1997) Biochimie , vol.79 , pp. 415-422
    • Pavlov, M.Y.1    Freistoffer, D.V.2    Ehrenberg, M.3
  • 93
    • 0030711495 scopus 로고    scopus 로고
    • Protein synthesis by chemical ligation of unprotected peptides in aqueous solution
    • of outstanding interest. Review of the protocols for the chemical ligation reaction yielding a normal peptide bond, which makes the synthesis of large proteins possible. As the peptide segments are made by normal solid phase synthesis, unnatural amino acids can be encoded anywhere.
    • Muir TW, Dawson PE, Kent SB. Protein synthesis by chemical ligation of unprotected peptides in aqueous solution. of outstanding interest Methods Enzymol. 289:1997;266-298 Review of the protocols for the chemical ligation reaction yielding a normal peptide bond, which makes the synthesis of large proteins possible. As the peptide segments are made by normal solid phase synthesis, unnatural amino acids can be encoded anywhere.
    • (1997) Methods Enzymol , vol.289 , pp. 266-298
    • Muir, T.W.1    Dawson, P.E.2    Kent, S.B.3
  • 94
    • 0029116947 scopus 로고
    • Protein splicing: Self-splicing of genetically mobile elements at the protein level
    • Cooper AA, Stevens TH. Protein splicing: self-splicing of genetically mobile elements at the protein level. Trends Biochem Sci. 20:1995;351-356.
    • (1995) Trends Biochem Sci , vol.20 , pp. 351-356
    • Cooper, A.A.1    Stevens, T.H.2
  • 95
    • 0023046569 scopus 로고
    • Translation arrest by oligodeoxynucleotides complementary to mRNA coding sequences yields polypeptides of predetermined length
    • Haeuptle MT, Frank R, Dobberstein B. Translation arrest by oligodeoxynucleotides complementary to mRNA coding sequences yields polypeptides of predetermined length. Nucleic Acids Res. 14:1986;1427-1447.
    • (1986) Nucleic Acids Res , vol.14 , pp. 1427-1447
    • Haeuptle, M.T.1    Frank, R.2    Dobberstein, B.3
  • 97
    • 0020994721 scopus 로고
    • Preparation of microsomal membranes for cotranslational protein translocation
    • Walter P, Blobel G. Preparation of microsomal membranes for cotranslational protein translocation. Methods Enzymol. 96:1983;84-93.
    • (1983) Methods Enzymol , vol.96 , pp. 84-93
    • Walter, P.1    Blobel, G.2
  • 98
    • 0030909990 scopus 로고    scopus 로고
    • In vitro reconstitution of assembly of apolipoprotein B48-conatining lipoproteins
    • Rusinol AE, Jamil H, Vance JE. in vitro reconstitution of assembly of apolipoprotein B48-conatining lipoproteins. J Biol Chem. 272:1997;8019-8025.
    • (1997) J Biol Chem , vol.272 , pp. 8019-8025
    • Rusinol, A.E.1    Jamil, H.2    Vance, J.E.3
  • 99
    • 0030817962 scopus 로고    scopus 로고
    • In vitro translation and assembly of a complete T cell receptor-CD3 complex
    • of outstanding interest. A remarkable example of the complexity which can be reached with in vitro systems. The chains for the complete T-cell receptor-CD3 complex together with the chains for its corresponding MHC complex were simultaneously translated and assembled.
    • Huppa JB, Ploegh HL. In vitro translation and assembly of a complete T cell receptor-CD3 complex. of outstanding interest J Exp Med. 186:1997;393-403 A remarkable example of the complexity which can be reached with in vitro systems. The chains for the complete T-cell receptor-CD3 complex together with the chains for its corresponding MHC complex were simultaneously translated and assembled.
    • (1997) J Exp Med , vol.186 , pp. 393-403
    • Huppa, J.B.1    Ploegh, H.L.2
  • 100
    • 0031035737 scopus 로고    scopus 로고
    • Membrane insertion, glycosylation, and oligomerization of inositol triphosphate receptors in a cell-free translation system
    • Joseph SK, Boehning D, Pierson S, Niccitta CV. Membrane insertion, glycosylation, and oligomerization of inositol triphosphate receptors in a cell-free translation system. J Biol Chem. 272:1997;1579-1588.
    • (1997) J Biol Chem , vol.272 , pp. 1579-1588
    • Joseph, S.K.1    Boehning, D.2    Pierson, S.3    Niccitta, C.V.4
  • 101
    • 0031001091 scopus 로고    scopus 로고
    • Cell-free synthesis and assembly of connexins into functional gap junction membrane channels
    • of special interest. The authors describe the functional reconstitution of a multimeric membrane transporter in vitro. The membrane channels were reconstituted into synthetic lipid bilayers for functionality tests.
    • Falk MM, Buehler LK, Kumar NM, Gilula NB. Cell-free synthesis and assembly of connexins into functional gap junction membrane channels. of special interest EMBO J. 16:1997;2703-2716 The authors describe the functional reconstitution of a multimeric membrane transporter in vitro. The membrane channels were reconstituted into synthetic lipid bilayers for functionality tests.
    • (1997) EMBO J , vol.16 , pp. 2703-2716
    • Falk, M.M.1    Buehler, L.K.2    Kumar, N.M.3    Gilula, N.B.4
  • 102
    • 0026325508 scopus 로고
    • Cell-free, de novo synthesis of poliovirus
    • Molla A, Paul AV, Wimmer E. Cell-free, de novo synthesis of poliovirus. Science. 254:1991;1647-1651.
    • (1991) Science , vol.254 , pp. 1647-1651
    • Molla, A.1    Paul, A.V.2    Wimmer, E.3
  • 103
    • 0029821262 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 capsid formation in reticulocyte lysates
    • Spearman P, Ratner L. Human immunodeficiency virus type 1 capsid formation in reticulocyte lysates. J Virol. 70:1996;8187-8194.
    • (1996) J Virol , vol.70 , pp. 8187-8194
    • Spearman, P.1    Ratner, L.2
  • 104
    • 0031044374 scopus 로고    scopus 로고
    • A multistep, ATP-dependent pathway for assembly of human immunodeficiency virus capsids in a cell-free system
    • Lingappa JR, Hill RL, Wong ML, Ramanujan SH. A multistep, ATP-dependent pathway for assembly of human immunodeficiency virus capsids in a cell-free system. J Cell Biol. 136:1997;567-681.
    • (1997) J Cell Biol , vol.136 , pp. 567-681
    • Lingappa, J.R.1    Hill, R.L.2    Wong, M.L.3    Ramanujan, S.H.4
  • 105
    • 0030592812 scopus 로고    scopus 로고
    • Formation of bacteriophage MS2 infectious units in a cell-free translation system
    • Katanaev VL, Spirin AS, Reuss M, Siemann M. Formation of bacteriophage MS2 infectious units in a cell-free translation system. FEBS Lett. 397:1996;143-148.
    • (1996) FEBS Lett , vol.397 , pp. 143-148
    • Katanaev, V.L.1    Spirin, A.S.2    Reuss, M.3    Siemann, M.4
  • 106
    • 0030924255 scopus 로고    scopus 로고
    • Poliovirus RNA recombination in cell-free extracts
    • Tang RS, Barton DJ, Flanegan JB, Kirkegaard K. Poliovirus RNA recombination in cell-free extracts. RNA. 3:1997;624-633.
    • (1997) RNA , vol.3 , pp. 624-633
    • Tang, R.S.1    Barton, D.J.2    Flanegan, J.B.3    Kirkegaard, K.4
  • 108
    • 0027082582 scopus 로고
    • Duck hepatitis B virus polymerase produced by in vitro transcription and translation possesses DNA polymerase and reverse transcriptase activities
    • Howe AY, Elliott JF, Tyrrell DL. Duck hepatitis B virus polymerase produced by in vitro transcription and translation possesses DNA polymerase and reverse transcriptase activities. Biochem Biophys Res Commun. 189:1992;1170-1176.
    • (1992) Biochem Biophys Res Commun , vol.189 , pp. 1170-1176
    • Howe, A.Y.1    Elliott, J.F.2    Tyrrell, D.L.3
  • 109
    • 0026493753 scopus 로고
    • The reverse transcriptase of hepatitis B virus acts as a protein primer for viral DNA synthesis
    • Wang GH, Seeger C. The reverse transcriptase of hepatitis B virus acts as a protein primer for viral DNA synthesis. Cell. 71:1992;663-670.
    • (1992) Cell , vol.71 , pp. 663-670
    • Wang, G.H.1    Seeger, C.2
  • 110
    • 2642608675 scopus 로고    scopus 로고
    • Type D retrovirus capsid assembly and release are active events requiring ATP
    • Weldon RA, Parker WB, Sakalian M, Hunter E. Type D retrovirus capsid assembly and release are active events requiring ATP. J Virol. 72:1998;3098-3106.
    • (1998) J Virol , vol.72 , pp. 3098-3106
    • Weldon, R.A.1    Parker, W.B.2    Sakalian, M.3    Hunter, E.4
  • 111
    • 0028926048 scopus 로고
    • Protein-protein interactions: Methods for detection and analysis
    • Phizicky EM, Fields S. Protein-protein interactions: methods for detection and analysis. Microbiol Rev. 59:1995;94-123.
    • (1995) Microbiol Rev , vol.59 , pp. 94-123
    • Phizicky, E.M.1    Fields, S.2
  • 112
    • 0028592703 scopus 로고
    • An in vitro polysome display system for identifying ligands from very large peptide libraries
    • Mattheakis LC, Bhatt RR, Dower WJ. An in vitro polysome display system for identifying ligands from very large peptide libraries. Proc Natl Acad Sci USA. 91:1994;9022-9026.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 9022-9026
    • Mattheakis, L.C.1    Bhatt, R.R.2    Dower, W.J.3
  • 113
    • 0029693534 scopus 로고    scopus 로고
    • Cell-free synthesis of peptide libraries displayed on polysomes
    • Mattheakis LC, Dias JM, Dower WJ. Cell-free synthesis of peptide libraries displayed on polysomes. Methods Enzymol. 267:1996;195-207.
    • (1996) Methods Enzymol , vol.267 , pp. 195-207
    • Mattheakis, L.C.1    Dias, J.M.2    Dower, W.J.3
  • 114
    • 0015890357 scopus 로고
    • Biologically and chemically pure mRNA coding for a mouse immunoglobulin L-chain prepared with the aid of antibodies and immobilized oligothymidine
    • Schechter I. Biologically and chemically pure mRNA coding for a mouse immunoglobulin L-chain prepared with the aid of antibodies and immobilized oligothymidine. Proc Natl Acad Sci USA. 70:1973;2256-2260.
    • (1973) Proc Natl Acad Sci USA , vol.70 , pp. 2256-2260
    • Schechter, I.1
  • 115
    • 0018537103 scopus 로고
    • Improvements in immunoprecipitation of specific messenger RNA
    • Payvar F, Schimke RT. Improvements in immunoprecipitation of specific messenger RNA. Eur J Biochem. 101:1979;271-282.
    • (1979) Eur J Biochem , vol.101 , pp. 271-282
    • Payvar, F.1    Schimke, R.T.2
  • 116
    • 0020315469 scopus 로고
    • CDNA clones for the heavy chain of HLA-DR antigens obtained after immunoprecipitation of polysomes by monoclonal antibody
    • Korman AJ, Knudsen PJ, Kaufman JF, Strominger JL. cDNA clones for the heavy chain of HLA-DR antigens obtained after immunoprecipitation of polysomes by monoclonal antibody. Proc Natl Acad Sci USA. 79:1982;1844-1848.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 1844-1848
    • Korman, A.J.1    Knudsen, P.J.2    Kaufman, J.F.3    Strominger, J.L.4
  • 117
    • 0020164157 scopus 로고
    • Purification of low-abundance messenger RNAs from rat liver by polysome immunoadsorption
    • Kraus JP, Rosenberg LE. Purification of low-abundance messenger RNAs from rat liver by polysome immunoadsorption. Proc Natl Acad Sci USA. 79:1982;4015-4019.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 4015-4019
    • Kraus, J.P.1    Rosenberg, L.E.2
  • 118
    • 85030343406 scopus 로고    scopus 로고
    • Ribosome display selects and evolves high-affinity binding antibodies from murine libraries
    • of special interest in" affinity maturation occuring simultaneously to the selection.
    • Hanes J, Jermutus L, Bornhauser-Weber S, Bosshard HR, Plückthun A. Ribosome display selects and evolves high-affinity binding antibodies from murine libraries. of special interest Proc Natl Acad Sci USA. 1998; The first demonstration that a diverse protein library can be screened with ribosome display. The authors observed a "built-in" affinity maturation occuring simultaneously to the selection.
    • (1998) Proc Natl Acad Sci USA
    • Hanes, J.1    Jermutus, L.2    Bornhauser-Weber, S.3    Bosshard, H.R.4    Plückthun, A.5
  • 119
    • 0031559943 scopus 로고    scopus 로고
    • In vitro virus: Bonding of mRNA bearing puromycin at the 3′-terminal end to the C-terminal end of its encoded protein on ribosome in vitro
    • of special interest. A protocol for the puroymycin-mediated fusion of mRNA to its encoding protein
    • Nemoto N, Miyamoto-Sato E, Husimi Y, Yanagawa H. in vitro virus: bonding of mRNA bearing puromycin at the 3′-terminal end to the C-terminal end of its encoded protein on ribosome in vitro. of special interest FEBS Lett. 414:1997;405-408 A protocol for the puroymycin-mediated fusion of mRNA to its encoding protein.
    • (1997) FEBS Lett , vol.414 , pp. 405-408
    • Nemoto, N.1    Miyamoto-Sato, E.2    Husimi, Y.3    Yanagawa, H.4
  • 120
    • 0030817279 scopus 로고    scopus 로고
    • RNA-peptide fusions for the in vitro selection of peptides and proteins
    • of outstanding interest. The authors demonstrate in a model system that the puromycin-based in vitro selection technique is able to enrich binding ligands out of a doped peptide library.
    • Roberts RW, Szostak JW. RNA-peptide fusions for the in vitro selection of peptides and proteins. of outstanding interest Proc Natl Acad Sci USA. 94:1997;12297-12302 The authors demonstrate in a model system that the puromycin-based in vitro selection technique is able to enrich binding ligands out of a doped peptide library.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12297-12302
    • Roberts, R.W.1    Szostak, J.W.2
  • 121
    • 85030342462 scopus 로고    scopus 로고
    • Kawasaki G: Screening randomized peptides and proteins with polysomes. PCT International Application 1991, WO 91/05058.
    • Kawasaki G: Screening randomized peptides and proteins with polysomes. PCT International Application 1991, WO 91/05058.


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