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Volumn 8, Issue 1, 2017, Pages

Phage-assisted continuous evolution of proteases with altered substrate specificity

Author keywords

[No Author keywords available]

Indexed keywords

INTERLEUKIN 23; INTERLEUKIN 23P19; PEPTIDE DERIVATIVE; PROLINE; PROTEINASE; RNA POLYMERASE; THREONINE; TEV PROTEASE;

EID: 85031807193     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/s41467-017-01055-9     Document Type: Article
Times cited : (83)

References (55)
  • 1
    • 84976878698 scopus 로고    scopus 로고
    • Twenty years of the MEROPS database of proteolytic enzymes, their substrates and inhibitors
    • Rawlings, N. D., Barrett, A. J., & Finn, R. Twenty years of the MEROPS database of proteolytic enzymes, their substrates and inhibitors. Nucleic Acids Res. 44, D343-D350 (2016
    • (2016) Nucleic Acids Res , vol.44 , pp. D343-D350
    • Rawlings, N.D.1    Barrett, A.J.2    Finn, R.3
  • 3
    • 0032973026 scopus 로고    scopus 로고
    • Directed evolution converts subtilisin e into a functional equivalent of thermitase
    • Zhao, H. M., & Arnold, F. H. Directed evolution converts subtilisin E into a functional equivalent of thermitase. Protein Eng. 12, 47-53 (1999
    • (1999) Protein Eng , vol.12 , pp. 47-53
    • Zhao, H.M.1    Arnold, F.H.2
  • 4
    • 0029969577 scopus 로고    scopus 로고
    • Directed evolution of subtilisin e in Bacillus subtilis to enhance total activity in aqueous dimethylformamide
    • You, L., & Arnold, F. H. Directed evolution of subtilisin E in Bacillus subtilis to enhance total activity in aqueous dimethylformamide. Protein Eng. 9, 77-83 (1996
    • (1996) Protein Eng , vol.9 , pp. 77-83
    • You, L.1    Arnold, F.H.2
  • 5
    • 0035923721 scopus 로고    scopus 로고
    • Rational design of coagulation factor VIIa variants with substantially increased intrinsic activity
    • Persson, E., Kjalke, M., & Olsen, O. H. Rational design of coagulation factor VIIa variants with substantially increased intrinsic activity. Proc. Natl Acad. Sci. USA 98, 13583-13588 (2001
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 13583-13588
    • Persson, E.1    Kjalke, M.2    Olsen, O.H.3
  • 6
  • 7
    • 33847054740 scopus 로고    scopus 로고
    • A variant of recombinant factor VIIa with enhanced procoagulant and antifibrinolytic activities in an in vitro model of hemophilia
    • Allen, G. A., et al. A variant of recombinant factor VIIa with enhanced procoagulant and antifibrinolytic activities in an in vitro model of hemophilia. Arterioscl. Thromb. Vasc. 27, 683-689 (2007
    • (2007) Arterioscl. Thromb. Vasc , vol.27 , pp. 683-689
    • Allen, G.A.1
  • 8
    • 77951586447 scopus 로고    scopus 로고
    • Strategies and challenges for the next generation of therapeutic antibodies
    • Beck, A., Wurch, T., Bailly, C., & Corvaia, N. Strategies and challenges for the next generation of therapeutic antibodies. Nat. Rev. Immunol. 10, 345-352 (2010
    • (2010) Nat. Rev. Immunol , vol.10 , pp. 345-352
    • Beck, A.1    Wurch, T.2    Bailly, C.3    Corvaia, N.4
  • 9
    • 0027965324 scopus 로고
    • Converting trypsin to chymotrypsin: Ground-state binding does not determine substrate specificity
    • Hedstrom, L., Farr-Jones, S., Kettner, C. A., & Rutter, W. J. Converting trypsin to chymotrypsin: ground-state binding does not determine substrate specificity. Biochemistry 33, 8764-8769 (1994
    • (1994) Biochemistry , vol.33 , pp. 8764-8769
    • Hedstrom, L.1    Farr-Jones, S.2    Kettner, C.A.3    Rutter, W.J.4
  • 10
    • 0030740225 scopus 로고    scopus 로고
    • Converting trypsin to chymotrypsin: Structural determinants of S1 specificity
    • Kurth, T., Ullmann, D., Jakubke, H. D., & Hedstrom, L. Converting trypsin to chymotrypsin: structural determinants of S1 specificity. Biochemistry 36, 10098-10104 (1997
    • (1997) Biochemistry , vol.36 , pp. 10098-10104
    • Kurth, T.1    Ullmann, D.2    Jakubke, H.D.3    Hedstrom, L.4
  • 11
    • 0026520387 scopus 로고
    • Converting trypsin to chymotrypsin: The role of surface loops
    • Hedstrom, L., Szilagyi, L., & Rutter, W. J. Converting trypsin to chymotrypsin: the role of surface loops. Science 255, 1249-1253 (1992
    • (1992) Science , vol.255 , pp. 1249-1253
    • Hedstrom, L.1    Szilagyi, L.2    Rutter, W.J.3
  • 12
    • 0028133496 scopus 로고
    • Converting trypsin to chymotrypsin: Residue 172 is a substrate specificity determinant
    • Hedstrom, L., Perona, J. J., & Rutter, W. J. Converting trypsin to chymotrypsin: residue 172 is a substrate specificity determinant. Biochemistry 33, 8757-8763 (1994
    • (1994) Biochemistry , vol.33 , pp. 8757-8763
    • Hedstrom, L.1    Perona, J.J.2    Rutter, W.J.3
  • 13
    • 17544378583 scopus 로고    scopus 로고
    • Programming the Rous sarcoma virus protease to cleave new substrate sequences
    • Ridky, T. W., et al. Programming the Rous sarcoma virus protease to cleave new substrate sequences. J. Biol. Chem. 271, 10538-10544 (1996
    • (1996) J. Biol. Chem , vol.271 , pp. 10538-10544
    • Ridky, T.W.1
  • 14
    • 0033998380 scopus 로고    scopus 로고
    • Alteration of substrate and inhibitor specificity of feline immunodeficiency virus protease
    • Lin, Y. C., et al. Alteration of substrate and inhibitor specificity of feline immunodeficiency virus protease. J. Virol. 74, 4710-4720 (2000
    • (2000) J. Virol , vol.74 , pp. 4710-4720
    • Lin, Y.C.1
  • 15
    • 84953257367 scopus 로고    scopus 로고
    • Simultaneous selection and counter-selection for the directed evolution of proteases in e coli using a cytoplasmic anchoring strategy
    • Carrico, Z. M., Strobel, K. L., Atreya, M. E., Clark, D. S., & Francis, M. B. Simultaneous selection and counter-selection for the directed evolution of proteases in E. coli using a cytoplasmic anchoring strategy. Biotechnol. Bioeng. 113, 1187-1193 (2016
    • (2016) Biotechnol. Bioeng , vol.113 , pp. 1187-1193
    • Carrico, Z.M.1    Strobel, K.L.2    Atreya, M.E.3    Clark, D.S.4    Francis, M.B.5
  • 16
    • 84879471277 scopus 로고    scopus 로고
    • A tobacco etch virus protease with increased substrate tolerance at the P1 position
    • Renicke, C., Spadaccini, R., & Taxis, C. A tobacco etch virus protease with increased substrate tolerance at the P1 position. PLoS ONE 8, e67915 (2013
    • (2013) Plos One , vol.8 , pp. e67915
    • Renicke, C.1    Spadaccini, R.2    Taxis, C.3
  • 17
    • 18744388856 scopus 로고    scopus 로고
    • Engineering of protease variants exhibiting high catalytic activity and exquisite substrate selectivity
    • Varadarajan, N., Gam, J., Olsen, M. J., Georgiou, G., & Iverson, B. L. Engineering of protease variants exhibiting high catalytic activity and exquisite substrate selectivity. Proc. Natl Acad. Sci. USA 102, 6855-6860 (2005
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 6855-6860
    • Varadarajan, N.1    Gam, J.2    Olsen, M.J.3    Georgiou, G.4    Iverson, B.L.5
  • 18
    • 84858650282 scopus 로고    scopus 로고
    • Intracellular detection and evolution of site-specific proteases using a genetic selection system
    • Verhoeven, K. D., Altstadt, O. C., & Savinov, S. N. Intracellular detection and evolution of site-specific proteases using a genetic selection system. Appl. Biochem. Biotechnol. 166, 1340-1354 (2012
    • (2012) Appl. Biochem. Biotechnol , vol.166 , pp. 1340-1354
    • Verhoeven, K.D.1    Altstadt, O.C.2    Savinov, S.N.3
  • 19
    • 84876919211 scopus 로고    scopus 로고
    • Engineering of TEV protease variants by yeast ER sequestration screening (YESS) of combinatorial libraries
    • Yi, L., et al. Engineering of TEV protease variants by yeast ER sequestration screening (YESS) of combinatorial libraries. Proc. Natl Acad. Sci. USA 110, 7229-7234 (2013
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 7229-7234
    • Yi, L.1
  • 20
    • 42249107490 scopus 로고    scopus 로고
    • Highly active and selective endopeptidases with programmed substrate specificities
    • Varadarajan, N., Rodriguez, S., Hwang, B. Y., Georgiou, G., & Iverson, B. L. Highly active and selective endopeptidases with programmed substrate specificities. Nat. Chem. Biol. 4, 290-294 (2008
    • (2008) Nat. Chem. Biol , vol.4 , pp. 290-294
    • Varadarajan, N.1    Rodriguez, S.2    Hwang, B.Y.3    Georgiou, G.4    Iverson, B.L.5
  • 21
    • 84949115623 scopus 로고    scopus 로고
    • In vivo continuous directed evolution
    • Badran, A. H., & Liu, D. R. In vivo continuous directed evolution. Curr. Opin. Chem. Biol. 24C, 1-10 (2015
    • (2015) Curr. Opin. Chem. Biol , vol.24 C , pp. 1-10
    • Badran, A.H.1    Liu, D.R.2
  • 22
    • 79955534060 scopus 로고    scopus 로고
    • A system for the continuous directed evolution of biomolecules
    • Esvelt, K. M., Carlson, J. C., & Liu, D. R. A system for the continuous directed evolution of biomolecules. Nature 472, 499-503 (2011
    • (2011) Nature , vol.472 , pp. 499-503
    • Esvelt, K.M.1    Carlson, J.C.2    Liu, D.R.3
  • 23
    • 84943777049 scopus 로고    scopus 로고
    • Development of potent in vivo mutagenesis plasmids with broad mutational spectra
    • Badran, A. H., & Liu, D. R. Development of potent in vivo mutagenesis plasmids with broad mutational spectra. Nat. Commun. 6, 8425 (2015
    • (2015) Nat. Commun , vol.6 , pp. 8425
    • Badran, A.H.1    Liu, D.R.2
  • 24
    • 0024708229 scopus 로고
    • Molecular genetic analysis of a plant virus polyprotein cleavage site: A model
    • Dougherty, W. G., Cary, S. M., & Parks, T. D. Molecular genetic analysis of a plant virus polyprotein cleavage site: a model. Virology 171, 356-364 (1989
    • (1989) Virology , vol.171 , pp. 356-364
    • Dougherty, W.G.1    Cary, S.M.2    Parks, T.D.3
  • 25
    • 0037184981 scopus 로고    scopus 로고
    • Structural basis for the substrate specificity of tobacco etch virus protease
    • Phan, J., et al. Structural basis for the substrate specificity of tobacco etch virus protease. J. Biol. Chem. 277, 50564-50572 (2002
    • (2002) J. Biol. Chem , vol.277 , pp. 50564-50572
    • Phan, J.1
  • 26
    • 84906535154 scopus 로고    scopus 로고
    • The IL-23-IL-17 immune axis: From mechanisms to therapeutic testing
    • Gaffen, S. L., Jain, R., Garg, A. V., & Cua, D. J. The IL-23-IL-17 immune axis: from mechanisms to therapeutic testing. Nat. Rev. Immunol. 14, 585-600 (2014
    • (2014) Nat. Rev. Immunol , vol.14 , pp. 585-600
    • Gaffen, S.L.1    Jain, R.2    Garg, A.V.3    Cua, D.J.4
  • 27
    • 13244283212 scopus 로고    scopus 로고
    • IL-23 drives a pathogenic T cell population that induces autoimmune inflammation
    • Langrish, C. L., et al. IL-23 drives a pathogenic T cell population that induces autoimmune inflammation. J. Exp. Med. 201, 233-240 (2005
    • (2005) J. Exp. Med , vol.201 , pp. 233-240
    • Langrish, C.L.1
  • 28
    • 84936891385 scopus 로고    scopus 로고
    • IL-12 and IL-23 cytokines: From discovery to targeted therapies for immune-mediated inflammatory diseases
    • Teng, M. W., et al. IL-12 and IL-23 cytokines: from discovery to targeted therapies for immune-mediated inflammatory diseases. Nat. Med. 21, 719-729 (2015
    • (2015) Nat. Med , vol.21 , pp. 719-729
    • Teng, M.W.1
  • 29
    • 84969786561 scopus 로고    scopus 로고
    • Continuous evolution of Bacillus thuringiensis toxins overcomes insect resistance
    • Badran, A. H., et al. Continuous evolution of Bacillus thuringiensis toxins overcomes insect resistance. Nature 533, 58-63 (2016
    • (2016) Nature , vol.533 , pp. 58-63
    • Badran, A.H.1
  • 30
    • 84894101033 scopus 로고    scopus 로고
    • Negative selection and stringency modulation in phage-assisted continuous evolution
    • Carlson, J. C., Badran, A. H., Guggiana-Nilo, D. A., & Liu, D. R. Negative selection and stringency modulation in phage-assisted continuous evolution. Nat. Chem. Biol. 10, 216-222 (2014
    • (2014) Nat. Chem. Biol , vol.10 , pp. 216-222
    • Carlson, J.C.1    Badran, A.H.2    Guggiana-Nilo, D.A.3    Liu, D.R.4
  • 31
    • 84878427504 scopus 로고    scopus 로고
    • Experimental interrogation of the path dependence and stochasticity of protein evolution using phage-assisted continuous evolution
    • Dickinson, B. C., Leconte, A. M., Allen, B., Esvelt, K. M., & Liu, D. R. Experimental interrogation of the path dependence and stochasticity of protein evolution using phage-assisted continuous evolution. Proc. Natl Acad. Sci. USA 110, 9007-9012 (2013
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 9007-9012
    • Dickinson, B.C.1    Leconte, A.M.2    Allen, B.3    Esvelt, K.M.4    Liu, D.R.5
  • 32
    • 84923266286 scopus 로고    scopus 로고
    • A system for the continuous directed evolution of proteases rapidly reveals drug-resistance mutations
    • Dickinson, B. C., Packer, M. S., Badran, A. H., & Liu, D. R. A system for the continuous directed evolution of proteases rapidly reveals drug-resistance mutations. Nat. Commun. 5, 5352 (2014
    • (2014) Nat. Commun , vol.5 , pp. 5352
    • Dickinson, B.C.1    Packer, M.S.2    Badran, A.H.3    Liu, D.R.4
  • 33
    • 84959102577 scopus 로고    scopus 로고
    • Continuous directed evolution of DNA-binding proteins to improve TALEN specificity
    • Hubbard, B. P., et al. Continuous directed evolution of DNA-binding proteins to improve TALEN specificity. Nat. Methods 12, 939-942 (2015
    • (2015) Nat. Methods , vol.12 , pp. 939-942
    • Hubbard, B.P.1
  • 34
    • 79951565301 scopus 로고    scopus 로고
    • Design construction and characterization of a set of insulated bacterial promoters
    • Davis, J. H., Rubin, A. J., & Sauer, R. T. Design, construction and characterization of a set of insulated bacterial promoters. Nucleic Acids Res. 39, 1131-1141 (2011
    • (2011) Nucleic Acids Res , vol.39 , pp. 1131-1141
    • Davis, J.H.1    Rubin, A.J.2    Sauer, R.T.3
  • 35
    • 0029558248 scopus 로고
    • Transcribing of Escherichia coli genes with mutant T7 RNA polymerases: Stability of lacZ mRNA inversely correlates with polymerase speed
    • Makarova, O. V., Makarov, E. M., Sousa, R., & Dreyfus, M. Transcribing of Escherichia coli genes with mutant T7 RNA polymerases: stability of lacZ mRNA inversely correlates with polymerase speed. Proc. Natl Acad. Sci. USA 92, 12250-12254 (1995
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 12250-12254
    • Makarova, O.V.1    Makarov, E.M.2    Sousa, R.3    Dreyfus, M.4
  • 36
    • 77957021680 scopus 로고    scopus 로고
    • High throughput substrate phage display for protease profiling
    • Ratnikov, B., Cieplak, P., & Smith, J. W. High throughput substrate phage display for protease profiling. Methods Mol. Biol. 539, 93-114 (2009
    • (2009) Methods Mol. Biol , vol.539 , pp. 93-114
    • Ratnikov, B.1    Cieplak, P.2    Smith, J.W.3
  • 37
    • 33646797435 scopus 로고    scopus 로고
    • Mapping protease substrates by using a biotinylated phage substrate library
    • Scholle, M. D., et al. Mapping protease substrates by using a biotinylated phage substrate library. Chem. Bio. Chem. 7, 834-838 (2006
    • (2006) Chem. Bio. Chem , vol.7 , pp. 834-838
    • Scholle, M.D.1
  • 38
    • 0027316004 scopus 로고
    • Substrate phage: Selection of protease substrates by monovalent phage display
    • Matthews, D. J., & Wells, J. A. Substrate phage: selection of protease substrates by monovalent phage display. Science 260, 1113-1117 (1993
    • (1993) Science , vol.260 , pp. 1113-1117
    • Matthews, D.J.1    Wells, J.A.2
  • 39
    • 84864463147 scopus 로고    scopus 로고
    • A method for construction and visualization of amino acid binding motifs and sequence profiles including sequence weighting, pseudo counts and two-sided representation of amino acid enrichment and depletion
    • Seq2Logo
    • Thomsen, M. C., & Nielsen, M. Seq2Logo: a method for construction and visualization of amino acid binding motifs and sequence profiles including sequence weighting, pseudo counts and two-sided representation of amino acid enrichment and depletion. Nucleic Acids Res. 40, W281-W287 (2012
    • (2012) Nucleic Acids Res , vol.40 , pp. W281-W287
    • Thomsen, M.C.1    Nielsen, M.2
  • 40
    • 84876935490 scopus 로고    scopus 로고
    • Cleavage entropy as quantitative measure of protease specificity
    • Fuchs, J. E., et al. Cleavage entropy as quantitative measure of protease specificity. PLoS Comput. Biol. 9, e1003007 (2013
    • (2013) PLoS Comput. Biol , vol.9 , pp. e1003007
    • Fuchs, J.E.1
  • 41
    • 69249100500 scopus 로고    scopus 로고
    • Human caspases: Activation, specificity, and regulation
    • Pop, C., & Salvesen, G. S. Human caspases: activation, specificity, and regulation. J. Biol. Chem. 284, 21777-21781 (2009
    • (2009) J. Biol. Chem , vol.284 , pp. 21777-21781
    • Pop, C.1    Salvesen, G.S.2
  • 42
    • 84870484133 scopus 로고    scopus 로고
    • PROSPER: An integrated feature-based tool for predicting protease substrate cleavage sites
    • Song, J., et al. PROSPER: an integrated feature-based tool for predicting protease substrate cleavage sites. PLoS ONE 7, e50300 (2012
    • (2012) Plos One , vol.7 , pp. e50300
    • Song, J.1
  • 43
    • 16644392080 scopus 로고    scopus 로고
    • A substrate-phage approach for investigating caspase specificity
    • Lien, S., Pastor, R., Sutherlin, D., & Lowman, H. B. A substrate-phage approach for investigating caspase specificity. Protein J. 23, 413-425 (2004
    • (2004) Protein J. , vol.23 , pp. 413-425
    • Lien, S.1    Pastor, R.2    Sutherlin, D.3    Lowman, H.B.4
  • 44
    • 35648952843 scopus 로고    scopus 로고
    • Enhancing the stability and solubility of TEV protease using in silico design
    • Cabrita, L. D., et al. Enhancing the stability and solubility of TEV protease using in silico design. Protein Sci. 16, 2360-2367 (2007
    • (2007) Protein Sci , vol.16 , pp. 2360-2367
    • Cabrita, L.D.1
  • 45
    • 30944459888 scopus 로고    scopus 로고
    • Improved solubility of TEV protease by directed evolution
    • van den Berg, S., Lofdahl, P. A., Hard, T., & Berglund, H. Improved solubility of TEV protease by directed evolution. J. Biotechnol. 121, 291-298 (2006
    • (2006) J. Biotechnol , vol.121 , pp. 291-298
    • Van Den Berg, S.1    Lofdahl, P.A.2    Hard, T.3    Berglund, H.4
  • 46
    • 84859914061 scopus 로고    scopus 로고
    • In vivo and in vitro characterization of TEV protease mutants
    • Wei, L., et al. In vivo and in vitro characterization of TEV protease mutants. Protein Expr. Purif. 83, 157-163 (2012
    • (2012) Protein Expr. Purif , vol.83 , pp. 157-163
    • Wei, L.1
  • 47
    • 84923238605 scopus 로고    scopus 로고
    • Structural basis of IL-23 antagonism by an Alphabody protein scaffold
    • Desmet, J., et al. Structural basis of IL-23 antagonism by an Alphabody protein scaffold. Nat. Commun. 5, 5237 (2014
    • (2014) Nat. Commun , vol.5 , pp. 5237
    • Desmet, J.1
  • 48
    • 0037449737 scopus 로고    scopus 로고
    • Interleukin-23 promotes a distinct CD4 T cell activation state characterized by the production of interleukin-17
    • Aggarwal, S., Ghilardi, N., Xie, M. H., de Sauvage, F. J., & Gurney, A. L. Interleukin-23 promotes a distinct CD4 T cell activation state characterized by the production of interleukin-17. J. Biol. Chem. 278, 1910-1914 (2003
    • (2003) J. Biol. Chem , vol.278 , pp. 1910-1914
    • Aggarwal, S.1    Ghilardi, N.2    Xie, M.H.3    De Sauvage, F.J.4    Gurney, A.L.5
  • 49
    • 0025730616 scopus 로고
    • At the crossroads of chemistry and immunology -catalytic antibodies
    • Lerner, R. A., Benkovic, S. J., & Schultz, P. G. At the crossroads of chemistry and immunology -catalytic antibodies. Science 252, 659-667 (1991
    • (1991) Science , vol.252 , pp. 659-667
    • Lerner, R.A.1    Benkovic, S.J.2    Schultz, P.G.3
  • 50
    • 84966293690 scopus 로고    scopus 로고
    • Intracellular FRET-based screen for redesigning the specificity of secreted proteases
    • Guerrero, J. L., O Malley, M. A., & Daugherty, P. S. Intracellular FRET-based screen for redesigning the specificity of secreted proteases. ACS. Chem. Biol. 11, 961-970 (2016
    • (2016) ACS. Chem. Biol , vol.11 , pp. 961-970
    • Guerrero, J.L.1    O'Malley, M.A.2    Daugherty, P.S.3
  • 51
    • 0033598777 scopus 로고    scopus 로고
    • Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm
    • Bessette, P. H., Aslund, F., Beckwith, J., & Georgiou, G. Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm. Proc. Natl Acad. Sci. USA 96, 13703-13708 (1999
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 13703-13708
    • Bessette, P.H.1    Aslund, F.2    Beckwith, J.3    Georgiou, G.4
  • 52
    • 78651484550 scopus 로고    scopus 로고
    • Disruption of reducing pathways is not essential for efficient disulfide bond formation in the cytoplasm of e coli
    • Hatahet, F., Nguyen, V. D., Salo, K. E., & Ruddock, L. W. Disruption of reducing pathways is not essential for efficient disulfide bond formation in the cytoplasm of E. coli. Microb. Cell Fact. 9, 67 (2010
    • (2010) Microb. Cell Fact , vol.9 , pp. 67
    • Hatahet, F.1    Nguyen, V.D.2    Salo, K.E.3    Ruddock, L.W.4
  • 53
    • 78650965365 scopus 로고    scopus 로고
    • Pre-expression of a sulfhydryl oxidase significantly increases the yields of eukaryotic disulfide bond containing proteins expressed in the cytoplasm of e coli
    • Nguyen, V. D., et al. Pre-expression of a sulfhydryl oxidase significantly increases the yields of eukaryotic disulfide bond containing proteins expressed in the cytoplasm of E. coli. Microb. Cell Fact. 10, 1 (2011
    • (2011) Microb. Cell Fact , vol.10 , pp. 1
    • Nguyen, V.D.1
  • 54
    • 0032189925 scopus 로고    scopus 로고
    • Disulfide bond formation in the Escherichia coli cytoplasm: An in vivo role reversal for the thioredoxins
    • Stewart, E. J., Aslund, F., & Beckwith, J. Disulfide bond formation in the Escherichia coli cytoplasm: an in vivo role reversal for the thioredoxins. EMBO J. 17, 5543-5550 (1998
    • (1998) EMBO J. , vol.17 , pp. 5543-5550
    • Stewart, E.J.1    Aslund, F.2    Beckwith, J.3
  • 55
    • 77956941760 scopus 로고    scopus 로고
    • USER cloning and USER fusion: The ideal cloning techniques for small and big laboratories
    • Nour-Eldin, H. H., Geu-Flores, F., & Halkier, B. A. USER cloning and USER fusion: the ideal cloning techniques for small and big laboratories. Plant Second. Metab. Eng. Methods Appl. 643, 185-200 (2010
    • (2010) Plant Second. Metab. Eng. Methods Appl , vol.643 , pp. 185-200
    • Nour-Eldin, H.H.1    Geu-Flores, F.2    Halkier, B.A.3


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