메뉴 건너뛰기




Volumn 75, Issue C, 2008, Pages 53-84

Chapter 2 Development of Key Technologies for High-Throughput Cell-Free Protein Production with the Extract from Wheat Embryos

Author keywords

[No Author keywords available]

Indexed keywords

PLANT EXTRACT; VEGETABLE PROTEIN;

EID: 76649137521     PISSN: 18761623     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0065-3233(07)75002-7     Document Type: Review
Times cited : (12)

References (84)
  • 2
    • 49249152943 scopus 로고
    • Fidelity of protein synthesis in vitro is increased in the presence of spermidine
    • Abraham A.K., Olsnes S., and Pihl A. Fidelity of protein synthesis in vitro is increased in the presence of spermidine. FEBS Lett. 101 (1979) 93-96
    • (1979) FEBS Lett. , vol.101 , pp. 93-96
    • Abraham, A.K.1    Olsnes, S.2    Pihl, A.3
  • 3
    • 27744523608 scopus 로고    scopus 로고
    • Cell-free synthesis of recombinant proteins from PCR-amplified genes at a comparable productivity to that of plasmid-based reactions
    • Ahn J., Chu H., Kim T., Oh I., Choi C., Hahn G., Park C., and Kim D. Cell-free synthesis of recombinant proteins from PCR-amplified genes at a comparable productivity to that of plasmid-based reactions. Biochem. Biophys. Res. Commun. 338 (2005) 1346-1352
    • (2005) Biochem. Biophys. Res. Commun. , vol.338 , pp. 1346-1352
    • Ahn, J.1    Chu, H.2    Kim, T.3    Oh, I.4    Choi, C.5    Hahn, G.6    Park, C.7    Kim, D.8
  • 4
    • 36148982267 scopus 로고    scopus 로고
    • Translation of non-capped mRNAs in a eukaryotic cell-free system: Acceleration of initiation rate in the course of polysome formation
    • Alekhina O.M., Vassilenko K.S., and Spirin A.S. Translation of non-capped mRNAs in a eukaryotic cell-free system: Acceleration of initiation rate in the course of polysome formation. Nucleic Acids Res. 35 (2007) 6547-6559
    • (2007) Nucleic Acids Res. , vol.35 , pp. 6547-6559
    • Alekhina, O.M.1    Vassilenko, K.S.2    Spirin, A.S.3
  • 5
    • 33744993160 scopus 로고    scopus 로고
    • In vitro reconstitution of eukaryotic translation reveals cooperativity between release factors eRF1 and eRF3
    • Alkalaeva E.Z., Pisarev A.V., Frolova L.Y., Kisselev L.L., and Pestova T.V. In vitro reconstitution of eukaryotic translation reveals cooperativity between release factors eRF1 and eRF3. Cell 125 (2006) 1125-1136
    • (2006) Cell , vol.125 , pp. 1125-1136
    • Alkalaeva, E.Z.1    Pisarev, A.V.2    Frolova, L.Y.3    Kisselev, L.L.4    Pestova, T.V.5
  • 6
    • 0019889101 scopus 로고
    • Factor requirements for the tritin inactivation of animal cell ribosomes
    • Coleman W.H., and Roberts W.K. Factor requirements for the tritin inactivation of animal cell ribosomes. Biochim. Biophys. Acta 654 (1981) 57-66
    • (1981) Biochim. Biophys. Acta , vol.654 , pp. 57-66
    • Coleman, W.H.1    Roberts, W.K.2
  • 7
    • 33746695331 scopus 로고    scopus 로고
    • Cell-free expression systems for eukaryotic protein production
    • Endo Y., and Sawasaki T. Cell-free expression systems for eukaryotic protein production. Curr. Opin. Biotechnol. 17 (2006) 373-380
    • (2006) Curr. Opin. Biotechnol. , vol.17 , pp. 373-380
    • Endo, Y.1    Sawasaki, T.2
  • 8
    • 0023219950 scopus 로고
    • RNA N-glycosidase activity of ricin A-chain. Mechanism of action of the toxic lectin ricin on eukaryotic ribosomes
    • Endo Y., and Tsurugi K. RNA N-glycosidase activity of ricin A-chain. Mechanism of action of the toxic lectin ricin on eukaryotic ribosomes. J. Biol. Chem. 262 (1987) 8128-8130
    • (1987) J. Biol. Chem. , vol.262 , pp. 8128-8130
    • Endo, Y.1    Tsurugi, K.2
  • 9
    • 0023664263 scopus 로고
    • The mechanism of action of ricin and related toxic lectins on eukaryotic ribosomes. The site and the characteristics of the modification in 28 S ribosomal RNA caused by the toxins
    • Endo Y., Mitsui K., Motizuki M., and Tsurugi K. The mechanism of action of ricin and related toxic lectins on eukaryotic ribosomes. The site and the characteristics of the modification in 28 S ribosomal RNA caused by the toxins. J. Biol. Chem. 262 (1987) 5908-5912
    • (1987) J. Biol. Chem. , vol.262 , pp. 5908-5912
    • Endo, Y.1    Mitsui, K.2    Motizuki, M.3    Tsurugi, K.4
  • 10
    • 0026658323 scopus 로고
    • Production of an enzymatic active protein using a continuous flow cell-free translation system
    • Endo Y., Otsuzuki S., Ito K., and Miura K. Production of an enzymatic active protein using a continuous flow cell-free translation system. J. Biotechnol. 25 (1992) 221-230
    • (1992) J. Biotechnol. , vol.25 , pp. 221-230
    • Endo, Y.1    Otsuzuki, S.2    Ito, K.3    Miura, K.4
  • 11
    • 0020997221 scopus 로고
    • Cell-free translation of messenger RNA in a wheat germ system
    • Erickson A.H., and Blobel G. Cell-free translation of messenger RNA in a wheat germ system. Methods Enzymol. 96 (1983) 38-50
    • (1983) Methods Enzymol. , vol.96 , pp. 38-50
    • Erickson, A.H.1    Blobel, G.2
  • 12
    • 0032541485 scopus 로고    scopus 로고
    • A tale of two termini: A functional interaction between the termini of an mRNA is a prerequisite for efficient translation initiation
    • Gallie D.R. A tale of two termini: A functional interaction between the termini of an mRNA is a prerequisite for efficient translation initiation. Gene 216 (1998) 1-11
    • (1998) Gene , vol.216 , pp. 1-11
    • Gallie, D.R.1
  • 13
    • 0026783938 scopus 로고
    • Identification of the motifs within the tobacco mosaic virus 5′-leader responsible for enhancing translation
    • Gallie D.R., and Walbot V. Identification of the motifs within the tobacco mosaic virus 5′-leader responsible for enhancing translation. Nucleic Acids Res. 20 (1992) 4631-4638
    • (1992) Nucleic Acids Res. , vol.20 , pp. 4631-4638
    • Gallie, D.R.1    Walbot, V.2
  • 14
    • 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 D.R., Sleat D.E., Watts J.W., Turner P.C., and Wilson T.M. 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.5
  • 15
    • 33745591913 scopus 로고    scopus 로고
    • Tolerance for random recombination of domains in prokaryotic and eukaryotic translation systems: Limited interdomain misfolding in a eukaryotic translation system
    • Hirano N., Sawasaki T., Tozawa Y., Endo Y., and Takai K. Tolerance for random recombination of domains in prokaryotic and eukaryotic translation systems: Limited interdomain misfolding in a eukaryotic translation system. Proteins 64 (2006) 343-354
    • (2006) Proteins , vol.64 , pp. 343-354
    • Hirano, N.1    Sawasaki, T.2    Tozawa, Y.3    Endo, Y.4    Takai, K.5
  • 16
    • 0020395723 scopus 로고
    • Increase of fidelity of polypeptide synthesis by spermidine in eukaryotic cell-free systems
    • Igarashi K., Hashimoto S., Miyake A., Kashiwagi K., and Hirose S. Increase of fidelity of polypeptide synthesis by spermidine in eukaryotic cell-free systems. Eur. J. Biochem. 128 (1982) 597-604
    • (1982) Eur. J. Biochem. , vol.128 , pp. 597-604
    • Igarashi, K.1    Hashimoto, S.2    Miyake, A.3    Kashiwagi, K.4    Hirose, S.5
  • 17
    • 15744391469 scopus 로고    scopus 로고
    • Expression of G protein coupled receptors in a cell-free translational system using detergents and thioredoxin-fusion vectors
    • Ishihara G., Goto M., Saeki M., Ito K., Hori T., Kigawa T., Shirouzu M., and Yokoyama S. Expression of G protein coupled receptors in a cell-free translational system using detergents and thioredoxin-fusion vectors. Protein Expr. Purif. 41 (2005) 27-37
    • (2005) Protein Expr. Purif. , vol.41 , pp. 27-37
    • Ishihara, G.1    Goto, M.2    Saeki, M.3    Ito, K.4    Hori, T.5    Kigawa, T.6    Shirouzu, M.7    Yokoyama, S.8
  • 18
    • 27144543021 scopus 로고    scopus 로고
    • Discovery of a novel restriction endonuclease by genome comparison and application of a wheat-germ-based cell-free translation assay: PabI (5′-GTA/C) from the hyperthermophilic archaeon Pyrococcus abyssi
    • Ishikawa K., Watanabe M., Kuroita T., Uchiyama I., Bujnicki J.M., Kawakami B., Tanokura M., and Kobayashi I. Discovery of a novel restriction endonuclease by genome comparison and application of a wheat-germ-based cell-free translation assay: PabI (5′-GTA/C) from the hyperthermophilic archaeon Pyrococcus abyssi. Nucleic Acids Res. 33 (2005) e112
    • (2005) Nucleic Acids Res. , vol.33
    • Ishikawa, K.1    Watanabe, M.2    Kuroita, T.3    Uchiyama, I.4    Bujnicki, J.M.5    Kawakami, B.6    Tanokura, M.7    Kobayashi, I.8
  • 19
    • 0023040107 scopus 로고
    • The increase by spermidine of fidelity of protamine synthesis in a wheat-germ cell-free system
    • Ito K., and Igarashi K. The increase by spermidine of fidelity of protamine synthesis in a wheat-germ cell-free system. Eur. J. Biochem. 156 (1986) 505-510
    • (1986) Eur. J. Biochem. , vol.156 , pp. 505-510
    • Ito, K.1    Igarashi, K.2
  • 20
    • 0021103090 scopus 로고
    • Enhanced polypeptide synthesis programmed by linear DNA fragments in cell-free extracts lacking exonuclease V
    • Jackson M., Pratt J.M., and Holland I.B. Enhanced polypeptide synthesis programmed by linear DNA fragments in cell-free extracts lacking exonuclease V. FEBS Lett. 163 (1983) 221-224
    • (1983) FEBS Lett. , vol.163 , pp. 221-224
    • Jackson, M.1    Pratt, J.M.2    Holland, I.B.3
  • 21
    • 0018498843 scopus 로고
    • Nucleoside triphosphate regeneration decreases the frequency of translation errors
    • Jelenc P.C., and Kurland C.G. Nucleoside triphosphate regeneration decreases the frequency of translation errors. Proc. Natl Acad. Sci. USA 76 (1979) 3174-3178
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 3174-3178
    • Jelenc, P.C.1    Kurland, C.G.2
  • 22
    • 41849151162 scopus 로고    scopus 로고
    • Continuous-exchange cell-free protein synthesis using PCR-generated DNA and an RNase E-deficient extract
    • Jun S.Y., Kang S.H., and Lee K. Continuous-exchange cell-free protein synthesis using PCR-generated DNA and an RNase E-deficient extract. BioTechniques 44 (2008) 387-391
    • (2008) BioTechniques , vol.44 , pp. 387-391
    • Jun, S.Y.1    Kang, S.H.2    Lee, K.3
  • 24
    • 27644468401 scopus 로고    scopus 로고
    • Selection of 5′-untranslated sequences that enhance initiation of translation in a cell-free protein synthesis system from wheat embryos
    • Kamura N., Sawasaki T., Kasahara Y., Takai K., and Endo Y. Selection of 5′-untranslated sequences that enhance initiation of translation in a cell-free protein synthesis system from wheat embryos. Bioorg. Med. Chem. Lett. 15 (2005) 5402-5406
    • (2005) Bioorg. Med. Chem. Lett. , vol.15 , pp. 5402-5406
    • Kamura, N.1    Sawasaki, T.2    Kasahara, Y.3    Takai, K.4    Endo, Y.5
  • 25
    • 3442888896 scopus 로고    scopus 로고
    • In vitro reconstitution of rice anthranilate synthase: Distinct functional properties of the alpha subunits OASA1 and OASA2
    • Kanno T., Kasai K., Ikejiri-Kanno Y., Wakasa K., and Tozawa Y. In vitro reconstitution of rice anthranilate synthase: Distinct functional properties of the alpha subunits OASA1 and OASA2. Plant Mol. Biol. 54 (2004) 11-22
    • (2004) Plant Mol. Biol. , vol.54 , pp. 11-22
    • Kanno, T.1    Kasai, K.2    Ikejiri-Kanno, Y.3    Wakasa, K.4    Tozawa, Y.5
  • 26
    • 33644674170 scopus 로고    scopus 로고
    • Structure-based in vitro engineering of the anthranilate synthase, a metabolic key enzyme in the plant tryptophan pathway
    • Kanno T., Komatsu A., Kasai K., Dubouzet J.G., Sakurai M., Ikejiri-Kanno Y., Wakasa K., and Tozawa Y. Structure-based in vitro engineering of the anthranilate synthase, a metabolic key enzyme in the plant tryptophan pathway. Plant Physiol. 138 (2005) 2260-2268
    • (2005) Plant Physiol. , vol.138 , pp. 2260-2268
    • Kanno, T.1    Komatsu, A.2    Kasai, K.3    Dubouzet, J.G.4    Sakurai, M.5    Ikejiri-Kanno, Y.6    Wakasa, K.7    Tozawa, Y.8
  • 27
    • 33845963089 scopus 로고    scopus 로고
    • Sequence specificity and efficiency of protein N-terminal methionine elimination in wheat-embryo cell-free system
    • Kanno T., Kitano M., Kato R., Omori A., Endo Y., and Tozawa Y. Sequence specificity and efficiency of protein N-terminal methionine elimination in wheat-embryo cell-free system. Protein Expr. Purif. 52 (2007) 59-65
    • (2007) Protein Expr. Purif. , vol.52 , pp. 59-65
    • Kanno, T.1    Kitano, M.2    Kato, R.3    Omori, A.4    Endo, Y.5    Tozawa, Y.6
  • 28
    • 0345256409 scopus 로고    scopus 로고
    • Efficient synthesis of a disulfide-containing protein through a batch cell-free system from wheat germ
    • Kawasaki T., Gouda M.D., Sawasaki T., Takai K., and Endo Y. Efficient synthesis of a disulfide-containing protein through a batch cell-free system from wheat germ. Eur. J. Biochem. 270 (2003) 4780-4786
    • (2003) Eur. J. Biochem. , vol.270 , pp. 4780-4786
    • Kawasaki, T.1    Gouda, M.D.2    Sawasaki, T.3    Takai, K.4    Endo, Y.5
  • 29
    • 0025787535 scopus 로고
    • A continuous cell-free protein synthesis system for coupled transcription-translation
    • Kigawa T., and 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
  • 30
    • 0032923295 scopus 로고    scopus 로고
    • Cell-free production and stable-isotope labeling of milligram quantities of proteins
    • Kigawa T., Yabuki T., Yoshida Y., Tsutsui M., Ito Y., Shibata T., and Yokoyama S. Cell-free production and stable-isotope labeling of milligram quantities of proteins. FEBS Lett. 442 (1999) 15-19
    • (1999) FEBS Lett. , vol.442 , pp. 15-19
    • Kigawa, T.1    Yabuki, T.2    Yoshida, Y.3    Tsutsui, M.4    Ito, Y.5    Shibata, T.6    Yokoyama, S.7
  • 31
    • 0029956987 scopus 로고    scopus 로고
    • A highly efficient cell-free protein synthesis system from Escherichia coli
    • Kim D.-M., Kigawa T., Choi C.-Y., and 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    Choi, C.-Y.3    Yokoyama, S.4
  • 33
    • 28244458078 scopus 로고    scopus 로고
    • Evaluation of detergents for the soluble expression of alpha-helical and beta-barrel-type integral membrane proteins by a preparative scale individual cell-free expression system
    • Klammt C., Schwarz D., Fendler K., Haase W., Dötsch V., and Bernhard F. Evaluation of detergents for the soluble expression of alpha-helical and beta-barrel-type integral membrane proteins by a preparative scale individual cell-free expression system. FEBS J. 272 (2005) 6024-6038
    • (2005) FEBS J. , vol.272 , pp. 6024-6038
    • Klammt, C.1    Schwarz, D.2    Fendler, K.3    Haase, W.4    Dötsch, V.5    Bernhard, F.6
  • 34
    • 33748307399 scopus 로고    scopus 로고
    • Cell-free expression as an emerging technique for the large scale production of integral membrane protein
    • Klammt C., Schwarz D., Löhr F., Schneider B., Dötsch V., and Bernhard F. Cell-free expression as an emerging technique for the large scale production of integral membrane protein. FEBS J. 273 (2006) 4141-4153
    • (2006) FEBS J. , vol.273 , pp. 4141-4153
    • Klammt, C.1    Schwarz, D.2    Löhr, F.3    Schneider, B.4    Dötsch, V.5    Bernhard, F.6
  • 36
    • 47849106554 scopus 로고    scopus 로고
    • DNA-binding profiling of human hormone nuclear receptors via fluorescence correlation spectroscopy in a cell-free system
    • Kobayashi T., Kodani Y., Nozawa A., Endo Y., and Sawasaki T. DNA-binding profiling of human hormone nuclear receptors via fluorescence correlation spectroscopy in a cell-free system. FEBS Lett. 582 (2008) 2737-2744
    • (2008) FEBS Lett. , vol.582 , pp. 2737-2744
    • Kobayashi, T.1    Kodani, Y.2    Nozawa, A.3    Endo, Y.4    Sawasaki, T.5
  • 37
    • 33644793335 scopus 로고    scopus 로고
    • Production of proteins for NMR studies using the wheat germ cell-free system
    • Kohno T. Production of proteins for NMR studies using the wheat germ cell-free system. Methods Mol. Biol. 310 (2005) 169-185
    • (2005) Methods Mol. Biol. , vol.310 , pp. 169-185
    • Kohno, T.1
  • 38
    • 34547683964 scopus 로고    scopus 로고
    • Production of protein for nuclear magnetic resonance study using the wheat germ cell-free system
    • Kohno T., and Endo Y. Production of protein for nuclear magnetic resonance study using the wheat germ cell-free system. Methods Mol. Biol. 375 (2007) 257-272
    • (2007) Methods Mol. Biol. , vol.375 , pp. 257-272
    • Kohno, T.1    Endo, Y.2
  • 40
    • 0020058545 scopus 로고
    • Translational accuracy in vitro
    • Kurland C.G. Translational accuracy in vitro. Cell 28 (1982) 201-202
    • (1982) Cell , vol.28 , pp. 201-202
    • Kurland, C.G.1
  • 41
    • 0031044374 scopus 로고    scopus 로고
    • A multistep, ATP-dependent pathway for assembly of human immunodeficiency virus capsids in a cell-free system
    • Lingappa J.R., Hill R.L., Wong M.L., and Hegde R.S. A multistep, ATP-dependent pathway for assembly of human immunodeficiency virus capsids in a cell-free system. J. Cell Biol. 136 (1997) 567-581
    • (1997) J. Cell Biol. , vol.136 , pp. 567-581
    • Lingappa, J.R.1    Hill, R.L.2    Wong, M.L.3    Hegde, R.S.4
  • 42
    • 13544270914 scopus 로고    scopus 로고
    • Comparing capsid assembly of primate lentiviruses and hepatitis B virus using cell-free systems
    • Lingappa J.R., Newman M.A., Klein K.C., and Dooher J.E. Comparing capsid assembly of primate lentiviruses and hepatitis B virus using cell-free systems. Virology 333 (2005) 114-123
    • (2005) Virology , vol.333 , pp. 114-123
    • Lingappa, J.R.1    Newman, M.A.2    Klein, K.C.3    Dooher, J.E.4
  • 43
    • 0034681174 scopus 로고    scopus 로고
    • A highly efficient and robust cell-free protein synthesis system prepared from wheat embryos: Plants apparently contain a suicide system directed at ribosomes
    • Madin K., Sawasaki T., Ogasawara T., and Endo Y. A highly efficient and robust cell-free protein synthesis system prepared from wheat embryos: Plants apparently contain a suicide system directed at ribosomes. Proc. Natl Acad. Sci. USA 97 (2000) 559-564
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 559-564
    • Madin, K.1    Sawasaki, T.2    Ogasawara, T.3    Endo, Y.4
  • 44
    • 0038487811 scopus 로고    scopus 로고
    • Poly(A)-binding proteins: Multifunctional scaffolds for the post-transcriptional control of gene expression
    • Mangus D.A., Evans M.C., and Jacobson A. Poly(A)-binding proteins: Multifunctional scaffolds for the post-transcriptional control of gene expression. Genome Biol. 4 (2003) 223
    • (2003) Genome Biol. , vol.4 , pp. 223
    • Mangus, D.A.1    Evans, M.C.2    Jacobson, A.3
  • 45
    • 0346765387 scopus 로고
    • Activation of protein synthesis in the imbibitions phase of seed germination
    • Marcus A., and Feeley J. Activation of protein synthesis in the imbibitions phase of seed germination. Proc. Natl Acad. Sci. USA 51 (1964) 1075-1079
    • (1964) Proc. Natl Acad. Sci. USA , vol.51 , pp. 1075-1079
    • Marcus, A.1    Feeley, J.2
  • 46
    • 0031559892 scopus 로고    scopus 로고
    • Direct expression of PCR products in a cell-free transcription/translation system: Synthesis of antibacterial peptide cecropin
    • Martemyanov K.A., Spirin A.S., and Gudkov A.T. 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
  • 47
    • 44449172019 scopus 로고    scopus 로고
    • The wheat germ cell-free based screening of protein substrates of calcium/calmodulin-dependent protein kinase II delta
    • Masaoka T., Nishi M., Ryo A., Endo Y., and Sawasaki T. The wheat germ cell-free based screening of protein substrates of calcium/calmodulin-dependent protein kinase II delta. FEBS Lett. 582 (2008) 1795-1801
    • (2008) FEBS Lett. , vol.582 , pp. 1795-1801
    • Masaoka, T.1    Nishi, M.2    Ryo, A.3    Endo, Y.4    Sawasaki, T.5
  • 48
    • 0029199332 scopus 로고
    • Wheat ribosome-inactivating proteins: Seed and leaf forms with different specificities and cofactor requirements
    • Massiah A.J., and Hartley M.R. Wheat ribosome-inactivating proteins: Seed and leaf forms with different specificities and cofactor requirements. Planta 197 (1995) 633-640
    • (1995) Planta , vol.197 , pp. 633-640
    • Massiah, A.J.1    Hartley, M.R.2
  • 50
    • 27544487569 scopus 로고    scopus 로고
    • Increasing PCR fragment stability and protein yields in a cell-free system with genetically modified Escherichia coli extracts
    • Michel-Reydellet N., Woodrow K., and Swartz J. Increasing PCR fragment stability and protein yields in a cell-free system with genetically modified Escherichia coli extracts. J. Mol. Microbiol. Biotechnol. 9 (2005) 26-34
    • (2005) J. Mol. Microbiol. Biotechnol. , vol.9 , pp. 26-34
    • Michel-Reydellet, N.1    Woodrow, K.2    Swartz, J.3
  • 52
    • 0038583721 scopus 로고    scopus 로고
    • A wheat germ cell-free system is a novel way to screen protein folding and function
    • Morita E.H., Sawasaki T., Tanaka R., Endo Y., and Kohno T. A wheat germ cell-free system is a novel way to screen protein folding and function. Protein Sci. 12 (2003) 1216-1221
    • (2003) Protein Sci. , vol.12 , pp. 1216-1221
    • Morita, E.H.1    Sawasaki, T.2    Tanaka, R.3    Endo, Y.4    Kohno, T.5
  • 54
    • 0030844281 scopus 로고    scopus 로고
    • Recombination of protein domains facilitated by co-translational folding in eukaryotes
    • Netzer W.J., and Hartl F.U. Recombination of protein domains facilitated by co-translational folding in eukaryotes. Nature 388 (1997) 343-349
    • (1997) Nature , vol.388 , pp. 343-349
    • Netzer, W.J.1    Hartl, F.U.2
  • 55
    • 0024968835 scopus 로고
    • A general method for site-specific incorporation of unnatural amino acids into proteins
    • Noren C.J., Anthony-Cahill S.J., Griffith M.C., and Schultz P.G. A general method for site-specific incorporation of unnatural amino acids into proteins. Science 244 (1989) 182-188
    • (1989) Science , vol.244 , pp. 182-188
    • Noren, C.J.1    Anthony-Cahill, S.J.2    Griffith, M.C.3    Schultz, P.G.4
  • 56
    • 37149014145 scopus 로고    scopus 로고
    • A cell-free translation and proteoliposome reconstitution system for functional analysis of plant solute transporters
    • Nozawa A., Nanamiya H., Miyata T., Linka N., Endo Y., Weber A.P.M., and Tozawa Y. A cell-free translation and proteoliposome reconstitution system for functional analysis of plant solute transporters. Plant Cell Physiol. 48 (2007) 1815-1820
    • (2007) Plant Cell Physiol. , vol.48 , pp. 1815-1820
    • Nozawa, A.1    Nanamiya, H.2    Miyata, T.3    Linka, N.4    Endo, Y.5    Weber, A.P.M.6    Tozawa, Y.7
  • 57
    • 0033570907 scopus 로고    scopus 로고
    • A new class of enzyme acting on damaged ribosomes: Ribosomal RNA apurinic site specific lyase found in wheat germ
    • Ogasawara T., Sawasaki T., Morishita R., Ozawa A., Madin K., and Endo Y. A new class of enzyme acting on damaged ribosomes: Ribosomal RNA apurinic site specific lyase found in wheat germ. EMBO J. 18 (1999) 6522-6531
    • (1999) EMBO J. , vol.18 , pp. 6522-6531
    • Ogasawara, T.1    Sawasaki, T.2    Morishita, R.3    Ozawa, A.4    Madin, K.5    Endo, Y.6
  • 58
    • 0346996710 scopus 로고    scopus 로고
    • RALyase; a terminator of elongation function of depurinated ribosomes
    • Ozawa A., Sawasaki T., Takai K., Uchiumi T., Hori H., and Endo Y. RALyase; a terminator of elongation function of depurinated ribosomes. FEBS Lett. 555 (2003) 455-458
    • (2003) FEBS Lett. , vol.555 , pp. 455-458
    • Ozawa, A.1    Sawasaki, T.2    Takai, K.3    Uchiumi, T.4    Hori, H.5    Endo, Y.6
  • 59
    • 7044241070 scopus 로고    scopus 로고
    • Ribosome-inactivating proteins in plant biology
    • Park S.W., Vepachedu R., Sharma N., and Vivanco J.M. Ribosome-inactivating proteins in plant biology. Planta 219 (2004) 1093-1096
    • (2004) Planta , vol.219 , pp. 1093-1096
    • Park, S.W.1    Vepachedu, R.2    Sharma, N.3    Vivanco, J.M.4
  • 60
    • 0029873397 scopus 로고    scopus 로고
    • Rate of translation of natural mRNAs in an optimized in vitro system
    • Pavlov M.Y., and Ehrenberg M. Rate of translation of natural mRNAs in an optimized in vitro system. Arch. Biochem. Biophys. 328 (1996) 9-16
    • (1996) Arch. Biochem. Biophys. , vol.328 , pp. 9-16
    • Pavlov, M.Y.1    Ehrenberg, M.2
  • 61
    • 35348815020 scopus 로고    scopus 로고
    • Recycling of eukaryotic posttermination ribosomal complexes
    • Pisarev A.V., Hellen C.U.T., and Pestova T.V. Recycling of eukaryotic posttermination ribosomal complexes. Cell 131 (2007) 286-299
    • (2007) Cell , vol.131 , pp. 286-299
    • Pisarev, A.V.1    Hellen, C.U.T.2    Pestova, T.V.3
  • 62
    • 33750799914 scopus 로고    scopus 로고
    • The highly conserved LepA is a ribosomal elongation factor that back-translocates the ribosome
    • Qin Y., Polacek N., Vesper O., Staub E., Einfeldt E., Wilson D.N., and Nierhaus K.H. The highly conserved LepA is a ribosomal elongation factor that back-translocates the ribosome. Cell 127 (2006) 721-733
    • (2006) Cell , vol.127 , pp. 721-733
    • Qin, Y.1    Polacek, N.2    Vesper, O.3    Staub, E.4    Einfeldt, E.5    Wilson, D.N.6    Nierhaus, K.H.7
  • 63
    • 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 B.E., and Paterson B.M. Efficient translation of tobacco mosaic virus RNA and rabbit globin 9S RNA in a cell-free system from commercial wheat germ. Proc. Natl Acad. Sci. USA 70 (1973) 2330-2334
    • (1973) Proc. Natl Acad. Sci. USA , vol.70 , pp. 2330-2334
    • Roberts, B.E.1    Paterson, B.M.2
  • 64
    • 76649104598 scopus 로고    scopus 로고
    • Protein expression in the wheat-germ cell-free system
    • Expression Systems. Dyson M.R., and Durocher Y. (Eds), Scion Publishing Ltd, Bloxham, Oxfordshire, UK
    • Sawasaki T., and Endo Y. Protein expression in the wheat-germ cell-free system. In: Dyson M.R., and Durocher Y. (Eds). Expression Systems. The METHODS EXPRESS series (2007), Scion Publishing Ltd, Bloxham, Oxfordshire, UK 87-108
    • (2007) The METHODS EXPRESS series , pp. 87-108
    • Sawasaki, T.1    Endo, Y.2
  • 65
    • 0037069324 scopus 로고    scopus 로고
    • A cell-free protein synthesis system for high-throughput proteomics
    • Sawasaki T., Ogasawara T., Morishita R., and Endo Y. A cell-free protein synthesis system for high-throughput proteomics. Proc. Natl Acad. Sci. USA 99 (2002) 14652-14657
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 14652-14657
    • Sawasaki, T.1    Ogasawara, T.2    Morishita, R.3    Endo, Y.4
  • 67
    • 3242767781 scopus 로고    scopus 로고
    • Genome-scale, biochemical annotation method based on the wheat germ cell-free protein synthesis system
    • Sawasaki T., Hasegawa Y., Morishita R., Seki M., Shinozaki K., and Endo Y. Genome-scale, biochemical annotation method based on the wheat germ cell-free protein synthesis system. Phytochemistry 65 (2004) 1549-1555
    • (2004) Phytochemistry , vol.65 , pp. 1549-1555
    • Sawasaki, T.1    Hasegawa, Y.2    Morishita, R.3    Seki, M.4    Shinozaki, K.5    Endo, Y.6
  • 68
    • 38049057933 scopus 로고    scopus 로고
    • Arabidopsis HY5 protein functions as a DNA-binding tag for purification and functional immobilization of proteins on agarose/DNA microplate
    • Sawasaki T., Kamura N., Matsunaga S., Saeki M., Tsuchimochi M., Morishita R., and Endo Y. Arabidopsis HY5 protein functions as a DNA-binding tag for purification and functional immobilization of proteins on agarose/DNA microplate. FEBS Lett. 582 (2008) 221-228
    • (2008) FEBS Lett. , vol.582 , pp. 221-228
    • Sawasaki, T.1    Kamura, N.2    Matsunaga, S.3    Saeki, M.4    Tsuchimochi, M.5    Morishita, R.6    Endo, Y.7
  • 69
    • 43049120195 scopus 로고    scopus 로고
    • RIP and RALyase cleave the sarcin/ricin domain, a critical domain for ribosome function, during senescence of wheat coleoptiles
    • Sawasaki T., Nishihara M., and Endo Y. RIP and RALyase cleave the sarcin/ricin domain, a critical domain for ribosome function, during senescence of wheat coleoptiles. Biochem. Biophys. Res. Commun. 370 (2008) 561-565
    • (2008) Biochem. Biophys. Res. Commun. , vol.370 , pp. 561-565
    • Sawasaki, T.1    Nishihara, M.2    Endo, Y.3
  • 70
    • 0039310043 scopus 로고
    • Use of peptide libraries to map the substrate specificity of a peptide-modifying enzyme: A 13 residue consensus peptide specifies biotinylation in Escherichia coli
    • Schatz P.J. Use of peptide libraries to map the substrate specificity of a peptide-modifying enzyme: A 13 residue consensus peptide specifies biotinylation in Escherichia coli. Biotechnology (N.Y.) 11 (1993) 1138-1143
    • (1993) Biotechnology (N.Y.) , vol.11 , pp. 1138-1143
    • Schatz, P.J.1
  • 72
    • 0024297305 scopus 로고
    • A continuous cell-free translation system capable of producing polypeptides in high yield
    • Spirin A.S., Baranov V.I., Ryabova L.A., Ovodov S.Y., and Alakhov Y.B. 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
  • 73
    • 0017738739 scopus 로고
    • An ATP-dependent inhibition of protein synthesis in ascites cell extracts by wheat germ protein
    • Stewart T.S., Hruby D.E., Sharma O.K., and Roberts W.K. An ATP-dependent inhibition of protein synthesis in ascites cell extracts by wheat germ protein. Biochim. Biophys. Acta 479 (1977) 31-38
    • (1977) Biochim. Biophys. Acta , vol.479 , pp. 31-38
    • Stewart, T.S.1    Hruby, D.E.2    Sharma, O.K.3    Roberts, W.K.4
  • 74
    • 4043133131 scopus 로고    scopus 로고
    • Ribosome-inactivating proteins
    • Stirpe F. Ribosome-inactivating proteins. Toxicon 44 (2004) 371-383
    • (2004) Toxicon , vol.44 , pp. 371-383
    • Stirpe, F.1
  • 75
    • 0029982484 scopus 로고    scopus 로고
    • Isolation and characterization of the 102-kilodalton RNA-binding protein that binds to the 5′ and 3′ translational enhancers of tobacco mosaic virus RNA
    • Tanguay R.L., and Gallie D.R. Isolation and characterization of the 102-kilodalton RNA-binding protein that binds to the 5′ and 3′ translational enhancers of tobacco mosaic virus RNA. J. Biol. Chem. 271 (1996) 14316-14322
    • (1996) J. Biol. Chem. , vol.271 , pp. 14316-14322
    • Tanguay, R.L.1    Gallie, D.R.2
  • 76
    • 0025187932 scopus 로고
    • Depurination of plant ribosomes by pokeweed antiviral protein
    • Taylor B.E., and Irvin J.D. Depurination of plant ribosomes by pokeweed antiviral protein. FEBS Lett. 273 (1990) 144-146
    • (1990) FEBS Lett. , vol.273 , pp. 144-146
    • Taylor, B.E.1    Irvin, J.D.2
  • 80
    • 33748289981 scopus 로고    scopus 로고
    • Wheat germ cell-free platform for eukaryotic protein production
    • Vinarov D.A., Loushin Newman C.L., and Markley J.L. Wheat germ cell-free platform for eukaryotic protein production. FEBS J. 273 (2006) 4160-4169
    • (2006) FEBS J. , vol.273 , pp. 4160-4169
    • Vinarov, D.A.1    Loushin Newman, C.L.2    Markley, J.L.3
  • 82
    • 0032532127 scopus 로고    scopus 로고
    • HSP101 functions as a specific translational regulatory protein whose activity is regulated by nutrient status
    • Wells D.R., Tanguay R.L., Le H., and Gallie D.R. HSP101 functions as a specific translational regulatory protein whose activity is regulated by nutrient status. Genes Dev. 12 (1998) 3236-3251
    • (1998) Genes Dev. , vol.12 , pp. 3236-3251
    • Wells, D.R.1    Tanguay, R.L.2    Le, H.3    Gallie, D.R.4
  • 84
    • 0009907706 scopus 로고
    • Cell-free coupled transcription-translation system for investigation of linear DNA segments
    • Yang H.L., Ivashkiv L., Chen H.Z., Zubay G., and Cashel M. Cell-free coupled transcription-translation system for investigation of linear DNA segments. Proc. Natl Acad. Sci. USA 77 (1980) 7029-7033
    • (1980) Proc. Natl Acad. Sci. USA , vol.77 , pp. 7029-7033
    • Yang, H.L.1    Ivashkiv, L.2    Chen, H.Z.3    Zubay, G.4    Cashel, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.