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Volumn 195, Issue , 2015, Pages 1-7

Gateway-compatible vectors for high-throughput protein expression in pro- and eukaryotic cell-free systems

Author keywords

Cell free protein expression; Gateway cloning; Rolling Circle DNA Amplification; Species Independent Translation Initiation Sequence

Indexed keywords

PLASMID DNA; RECOMBINANT PROTEIN;

EID: 84919903411     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2014.12.006     Document Type: Article
Times cited : (33)

References (25)
  • 1
    • 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.H., Chu H.S., Kim T.W., Oh I.S., Choi C.Y., Hahn G.H., Park C.G., Kim D.M. Cell-free synthesis of recombinant proteins from PCR-amplified genes at a comparable productivity to that of plasmid-based reactions. Biochem. Biophys. Res. Commun. 2005, 338:1346-1352.
    • (2005) Biochem. Biophys. Res. Commun. , vol.338 , pp. 1346-1352
    • Ahn, J.H.1    Chu, H.S.2    Kim, T.W.3    Oh, I.S.4    Choi, C.Y.5    Hahn, G.H.6    Park, C.G.7    Kim, D.M.8
  • 2
    • 84878892281 scopus 로고    scopus 로고
    • Cell-free co-production of an orthogonal transfer RNA activates efficient site-specific non-natural amino acid incorporation
    • Albayrak C., Swartz J.R. Cell-free co-production of an orthogonal transfer RNA activates efficient site-specific non-natural amino acid incorporation. Nucleic Acids Res. 2013, 41:5949-5963.
    • (2013) Nucleic Acids Res. , vol.41 , pp. 5949-5963
    • Albayrak, C.1    Swartz, J.R.2
  • 4
    • 0034830935 scopus 로고    scopus 로고
    • Rapid amplification of plasmid and phage DNA using Phi 29 DNA polymerase and multiply-primed rolling circle amplification
    • Dean F.B., Nelson J.R., Giesler T.L., Lasken R.S. Rapid amplification of plasmid and phage DNA using Phi 29 DNA polymerase and multiply-primed rolling circle amplification. Genome Res. 2001, 11:1095-1099.
    • (2001) Genome Res. , vol.11 , pp. 1095-1099
    • Dean, F.B.1    Nelson, J.R.2    Giesler, T.L.3    Lasken, R.S.4
  • 7
    • 84857429666 scopus 로고    scopus 로고
    • A systematic approach to increase the efficiency of membrane protein production in cell-free expression systems
    • Haberstock S., Roos C., Hoevels Y., Dotsch V., Schnapp G., Pautsch A., Bernhard F. A systematic approach to increase the efficiency of membrane protein production in cell-free expression systems. Protein Expr. Purif. 2012, 82:308-316.
    • (2012) Protein Expr. Purif. , vol.82 , pp. 308-316
    • Haberstock, S.1    Roos, C.2    Hoevels, Y.3    Dotsch, V.4    Schnapp, G.5    Pautsch, A.6    Bernhard, F.7
  • 8
    • 60349130597 scopus 로고    scopus 로고
    • Production of protein arrays by cell-free systems
    • He M., Taussig M.J. Production of protein arrays by cell-free systems. Methods Mol. Biol. 2008, 484:207-215.
    • (2008) Methods Mol. Biol. , vol.484 , pp. 207-215
    • He, M.1    Taussig, M.J.2
  • 9
    • 0032191388 scopus 로고    scopus 로고
    • Recent advances in producing and selecting functional proteins by using cell-free translation
    • Jermutus L., Ryabova L.A., Pluckthun A. Recent advances in producing and selecting functional proteins by using cell-free translation. Curr. Opin. Biotechnol. 1998, 9:534-548.
    • (1998) Curr. Opin. Biotechnol. , vol.9 , pp. 534-548
    • Jermutus, L.1    Ryabova, L.A.2    Pluckthun, A.3
  • 10
    • 84934441259 scopus 로고    scopus 로고
    • Production of eukaryotic cell-free lysate from Leishmania tarentolae
    • Johnston W.A., Alexandrov K. Production of eukaryotic cell-free lysate from Leishmania tarentolae. Methods Mol. Biol. 2014, 1118:1-15.
    • (2014) Methods Mol. Biol. , vol.1118 , pp. 1-15
    • Johnston, W.A.1    Alexandrov, K.2
  • 11
    • 13944274948 scopus 로고    scopus 로고
    • The past, present and future of cell-free protein synthesis
    • Katzen F., Chang G., Kudlicki W. The past, present and future of cell-free protein synthesis. Trends Biotechnol. 2005, 23:150-156.
    • (2005) Trends Biotechnol. , vol.23 , pp. 150-156
    • Katzen, F.1    Chang, G.2    Kudlicki, W.3
  • 12
    • 70350720040 scopus 로고    scopus 로고
    • Cell-free protein synthesis using multiply-primed rolling circle amplification products
    • Kumar G., Chernaya G. Cell-free protein synthesis using multiply-primed rolling circle amplification products. Biotechniques 2009, 47:637-639.
    • (2009) Biotechniques , vol.47 , pp. 637-639
    • Kumar, G.1    Chernaya, G.2
  • 13
    • 77952765484 scopus 로고    scopus 로고
    • Production of multi-subunit complexes on liposome through an E. coli cell-free expression system
    • Kuruma Y., Suzuki T., Ueda T. Production of multi-subunit complexes on liposome through an E. coli cell-free expression system. Methods Mol. Biol. 2010, 607:161-171.
    • (2010) Methods Mol. Biol. , vol.607 , pp. 161-171
    • Kuruma, Y.1    Suzuki, T.2    Ueda, T.3
  • 15
    • 68449097384 scopus 로고    scopus 로고
    • Species-independent translational leaders facilitate cell-free expression
    • Mureev S., Kovtun O., Nguyen U.T., Alexandrov K. Species-independent translational leaders facilitate cell-free expression. Nat. Biotechnol. 2009, 27:747-752.
    • (2009) Nat. Biotechnol. , vol.27 , pp. 747-752
    • Mureev, S.1    Kovtun, O.2    Nguyen, U.T.3    Alexandrov, K.4
  • 20
    • 84934435922 scopus 로고    scopus 로고
    • High-throughput protein expression using cell-free system
    • Sitaraman K., Chatterjee D.K. High-throughput protein expression using cell-free system. Methods Mol. Biol. 2009, 498:229-244.
    • (2009) Methods Mol. Biol. , vol.498 , pp. 229-244
    • Sitaraman, K.1    Chatterjee, D.K.2
  • 21
    • 84871221001 scopus 로고    scopus 로고
    • Generation of a genome scale lentiviral vector library for EF1alpha promoter-driven expression of human ORFs and identification of human genes affecting viral titer
    • Skalamera D., Dahmer M., Purdon A.S., Wilson B.M., Ranall M.V., Blumenthal A., Gabrielli B., Gonda T.J. Generation of a genome scale lentiviral vector library for EF1alpha promoter-driven expression of human ORFs and identification of human genes affecting viral titer. PLoS ONE 2012, 7:e51733.
    • (2012) PLoS ONE , vol.7 , pp. e51733
    • Skalamera, D.1    Dahmer, M.2    Purdon, A.S.3    Wilson, B.M.4    Ranall, M.V.5    Blumenthal, A.6    Gabrielli, B.7    Gonda, T.J.8
  • 23
    • 84860833500 scopus 로고    scopus 로고
    • Reorganizing the protein space at the Universal Protein Resource (UniProt)
    • UniProt C. Reorganizing the protein space at the Universal Protein Resource (UniProt). Nucleic Acids Res. 2012, 40:D71-D75.
    • (2012) Nucleic Acids Res. , vol.40 , pp. D71-D75
    • UniProt, C.1
  • 24
    • 84872807174 scopus 로고    scopus 로고
    • Cell-free protein synthesis: the state of the art
    • Whittaker J.W. Cell-free protein synthesis: the state of the art. Biotechnol. Lett. 2013, 35:143-152.
    • (2013) Biotechnol. Lett. , vol.35 , pp. 143-152
    • Whittaker, J.W.1
  • 25
    • 84934436713 scopus 로고    scopus 로고
    • A cell-free expression platform for production of protein microarrays
    • Zarate X., Galbraith D.W. A cell-free expression platform for production of protein microarrays. Methods Mol. Biol. 2014, 1118:297-307.
    • (2014) Methods Mol. Biol. , vol.1118 , pp. 297-307
    • Zarate, X.1    Galbraith, D.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.