메뉴 건너뛰기




Volumn 29, Issue 2, 2003, Pages 311-320

A less laborious approach to the high-throughput production of recombinant proteins in Escherichia coli using 2-liter plastic bottles

Author keywords

Functional genomics; Heterologous expression; High throughput; Structural genomics

Indexed keywords

ESCHERICHIA COLI;

EID: 0037790957     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/s1046-5928(03)00063-9     Document Type: Article
Times cited : (43)

References (21)
  • 1
    • 0033757870 scopus 로고    scopus 로고
    • Structural genomics in North America
    • T.C. Terwilliger, Structural genomics in North America, Nat. Struct. Biol. 7 (Suppl.) (2000) 935-939.
    • (2000) Nat. Struct. Biol. , vol.7 , Issue.SUPPL. , pp. 935-939
    • Terwilliger, T.C.1
  • 2
    • 0035919686 scopus 로고    scopus 로고
    • Tech. Sight. Industrializing structural biology
    • R.C. Stevens, I.A. Wilson, Tech. Sight. Industrializing structural biology, Science 293 (2001) 519-520.
    • (2001) Science , vol.293 , pp. 519-520
    • Stevens, R.C.1    Wilson, I.A.2
  • 3
    • 0033767363 scopus 로고    scopus 로고
    • Structural genomics for science and society
    • W.G. Hol, Structural genomics for science and society, Nat. Struct. Biol. 7 (Suppl.) (2000) 964-966.
    • (2000) Nat. Struct. Biol. , vol.7 , Issue.SUPPL. , pp. 964-966
    • Hol, W.G.1
  • 4
    • 0034957669 scopus 로고    scopus 로고
    • High-throughput proteomics: Protein expression and purification in the postgenomic world
    • S.A. Lesley, High-throughput proteomics: protein expression and purification in the postgenomic world, Protein Expr. Purif. 22 (2001) 159-164.
    • (2001) Protein Expr. Purif. , vol.22 , pp. 159-164
    • Lesley, S.A.1
  • 6
    • 0026658323 scopus 로고
    • Production of an enzymatic active protein using a continuous flow cell-free translation system
    • Y. Endo, S. Otsuzuki, K. Ito, K. Miura, 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
  • 8
  • 9
    • 0024297305 scopus 로고
    • A continuous cell-free translation system capable of producing polypeptides in high yield
    • A.S. Spirin, V.I. Baranov, L.A. Ryabova, S.Y. Ovodov, Y.B. Alakhov, 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
  • 10
    • 0002752973 scopus 로고
    • Improved media for growing plasmid and cosmid clones
    • K. Tartof, C. Hobbs, Improved media for growing plasmid and cosmid clones, Bethesda Res. Lab Focus 9 (1987) 12.
    • (1987) Bethesda Res. Lab Focus , vol.9 , pp. 12
    • Tartof, K.1    Hobbs, C.2
  • 12
    • 0036926615 scopus 로고    scopus 로고
    • A new vector for high-throughput, ligation-independent cloning encoding a tobacco etch virus protease cleavage site
    • L. Stols, M. Gu, L. Dieckman, R. Raffen, F.R. Collart, M.I. Donnelly, A new vector for high-throughput, ligation-independent cloning encoding a tobacco etch virus protease cleavage site, Protein Expr. Purif. 25 (2002) 8-15.
    • (2002) Protein Expr. Purif. , vol.25 , pp. 8-15
    • Stols, L.1    Gu, M.2    Dieckman, L.3    Raffen, R.4    Collart, F.R.5    Donnelly, M.I.6
  • 13
    • 0033939135 scopus 로고    scopus 로고
    • Controlled intracellular processing of fusion proteins by TEV protease
    • R.B. Kapust, D.S. Waugh, Controlled intracellular processing of fusion proteins by TEV protease, Protein Expr. Purif. 19 (2000) 312-318.
    • (2000) Protein Expr. Purif. , vol.19 , pp. 312-318
    • Kapust, R.B.1    Waugh, D.S.2
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli, Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227 (1970) 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0013158654 scopus 로고
    • Glycerokinase
    • S. Colowick, N. Kaplan (Eds.), Academic Press, New York
    • C. Bublitz, O. Weiland, Glycerokinase, in: S. Colowick, N. Kaplan (Eds.), Methods in Enzymology, vol. 5, Academic Press, New York, 1962, pp. 354-361.
    • (1962) Methods in Enzymology , vol.5 , pp. 354-361
    • Bublitz, C.1    Weiland, O.2
  • 16
    • 0020641705 scopus 로고
    • Periplasmic glycerophosphodiester phosphodiesterase of Escherichia coli, a new enzyme of the glp regulon
    • T.J. Larson, M. Ehrmann, W. Boos, Periplasmic glycerophosphodiester phosphodiesterase of Escherichia coli, a new enzyme of the glp regulon, J. Biol. Chem. 258 (1983) 5428-5432.
    • (1983) J. Biol. Chem. , vol.258 , pp. 5428-5432
    • Larson, T.J.1    Ehrmann, M.2    Boos, W.3
  • 17
    • 0023953461 scopus 로고
    • Purification and characterization of glpQ-encoded glycerophosphodiester phosphodiesterase from Escherichia coli K-12
    • T.J. Larson, A.T. van Loo-Bhattacharya, Purification and characterization of glpQ-encoded glycerophosphodiester phosphodiesterase from Escherichia coli K-12, Arch. Biochem. Biophys. 260 (1988) 577-584.
    • (1988) Arch. Biochem. Biophys. , vol.260 , pp. 577-584
    • Larson, T.J.1    Van Loo-Bhattacharya, A.T.2
  • 18
    • 0029196090 scopus 로고
    • A novel method for selective isotope labeling of bacterially expressed proteins
    • K.M. Lee, E.J. Androphy, J.D. Baleja, A novel method for selective isotope labeling of bacterially expressed proteins, J. Biomol. NMR 5 (1995) 93-96.
    • (1995) J. Biomol. NMR , vol.5 , pp. 93-96
    • Lee, K.M.1    Androphy, E.J.2    Baleja, J.D.3
  • 19
    • 0033152987 scopus 로고    scopus 로고
    • Application of fed-batch fermentation to the preparation of isotopically labeled or selenomethionyl-labeled proteins
    • J.M. Studts, B.G. Fox, Application of fed-batch fermentation to the preparation of isotopically labeled or selenomethionyl-labeled proteins, Protein Expr. Purif. 16 (1999) 109-119.
    • (1999) Protein Expr. Purif. , vol.16 , pp. 109-119
    • Studts, J.M.1    Fox, B.G.2
  • 20
    • 0025262173 scopus 로고
    • Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure
    • W.A. Hendrickson, J.R. Horton, D.M. LeMaster, Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structure, EMBO J. 9 (1990) 1665-1672.
    • (1990) EMBO J. , vol.9 , pp. 1665-1672
    • Hendrickson, W.A.1    Horton, J.R.2    LeMaster, D.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.