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Volumn 44, Issue 6, 2008, Pages 787-796

Purification of inclusion body-forming peptides and proteins in soluble form by fusion to Escherichia coli thermostable proteins

Author keywords

[No Author keywords available]

Indexed keywords

HYBRID PROTEIN; PEPTIDE; PROTEIN;

EID: 45249105602     PISSN: 07366205     EISSN: None     Source Type: Journal    
DOI: 10.2144/000112728     Document Type: Article
Times cited : (33)

References (27)
  • 1
    • 0029828233 scopus 로고    scopus 로고
    • Strategies for achieving high-level expression of genes in Escherichia coli
    • Makrides, S.C. 1996. Strategies for achieving high-level expression of genes in Escherichia coli. Microbiol. Rev. 60:512-538.
    • (1996) Microbiol. Rev , vol.60 , pp. 512-538
    • Makrides, S.C.1
  • 2
    • 1942537173 scopus 로고    scopus 로고
    • An efficient system for high-level expression and easy purification of authentic recombinant proteins
    • Catanzariti, A.M., T.A. Soboleva, D.A. Jans, P.G. Bord, and R.T. Baker. 2004. An efficient system for high-level expression and easy purification of authentic recombinant proteins. Protein Sci. 13:1331-1339.
    • (2004) Protein Sci , vol.13 , pp. 1331-1339
    • Catanzariti, A.M.1    Soboleva, T.A.2    Jans, D.A.3    Bord, P.G.4    Baker, R.T.5
  • 3
    • 0032007853 scopus 로고    scopus 로고
    • Strategies for optimizing heterologous protein expression in Escherichia coli
    • Hannig, G. and S.C. Makrides. 1998. Strategies for optimizing heterologous protein expression in Escherichia coli. Trends Biotechnol. 16:54-60.
    • (1998) Trends Biotechnol , vol.16 , pp. 54-60
    • Hannig, G.1    Makrides, S.C.2
  • 4
    • 10644255526 scopus 로고    scopus 로고
    • Advanced genetic strategies for recombinant protein expression in Escherichia coli
    • Sorensen, H.P. and K.K. Mortensen. 2005. Advanced genetic strategies for recombinant protein expression in Escherichia coli. J. Biotechnol. 115:113-128.
    • (2005) J. Biotechnol , vol.115 , pp. 113-128
    • Sorensen, H.P.1    Mortensen, K.K.2
  • 5
    • 4444378435 scopus 로고    scopus 로고
    • The solubility and stability of recombinant proteins are increased by their fusion to NusA
    • De Marco, V., G. Stier, S. Blandin, and A. de Marco. 2004. The solubility and stability of recombinant proteins are increased by their fusion to NusA. Biochem. Biophys. Res. Commun. 322:766-771.
    • (2004) Biochem. Biophys. Res. Commun , vol.322 , pp. 766-771
    • De Marco, V.1    Stier, G.2    Blandin, S.3    de Marco, A.4
  • 6
    • 0032787876 scopus 로고    scopus 로고
    • Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused
    • Kapust, R.B. and D.S. Waugh. 1999. Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused. Protein Sci. 8:1668-1674.
    • (1999) Protein Sci , vol.8 , pp. 1668-1674
    • Kapust, R.B.1    Waugh, D.S.2
  • 7
    • 29344475982 scopus 로고    scopus 로고
    • Comparison of SUMO fusion technology with traditional gene fusion systems: Enhanced expression and solubility with SUMO
    • Marblestone, J.G., S.C. Edavettal, Y. Lim, P. Lim, X. Zuo, and T.R. Butt. 2006. Comparison of SUMO fusion technology with traditional gene fusion systems: enhanced expression and solubility with SUMO. Protein Sci. 15:182-189.
    • (2006) Protein Sci , vol.15 , pp. 182-189
    • Marblestone, J.G.1    Edavettal, S.C.2    Lim, Y.3    Lim, P.4    Zuo, X.5    Butt, T.R.6
  • 8
    • 0035104597 scopus 로고    scopus 로고
    • Single amino acid substitutions on the surface of Escherichia coli maltose-binding protein can have a profound impact on the solubility of fusion proteins
    • Fox, J.D., R.B. Kapust, and D.S. Waugh. 2001. Single amino acid substitutions on the surface of Escherichia coli maltose-binding protein can have a profound impact on the solubility of fusion proteins. Protein Sci. 10:622-630.
    • (2001) Protein Sci , vol.10 , pp. 622-630
    • Fox, J.D.1    Kapust, R.B.2    Waugh, D.S.3
  • 9
    • 0347985703 scopus 로고    scopus 로고
    • Recombinant proteins fused to thermostable partners can be purified by heat incubation
    • de Marco, A., E. Casatta, S. Savaresi, and A. Geerlof. 2004. Recombinant proteins fused to thermostable partners can be purified by heat incubation. J. Biotechnol. 107:125-133.
    • (2004) J. Biotechnol , vol.107 , pp. 125-133
    • de Marco, A.1    Casatta, E.2    Savaresi, S.3    Geerlof, A.4
  • 10
    • 34250206336 scopus 로고    scopus 로고
    • Stable activity of a deubiquitylating enzyme (Usp2-cc) in the presence of high concentrations of urea and its application to purify aggregation-prone peptides
    • Shahnawaz, M., A. Thapa, and I.S. Park. 2007. Stable activity of a deubiquitylating enzyme (Usp2-cc) in the presence of high concentrations of urea and its application to purify aggregation-prone peptides. Biochem. Biophys. Res. Commun. 359:801-805.
    • (2007) Biochem. Biophys. Res. Commun , vol.359 , pp. 801-805
    • Shahnawaz, M.1    Thapa, A.2    Park, I.S.3
  • 11
    • 6944241283 scopus 로고    scopus 로고
    • High-yield, solid-phase synthesis of humanin, an Alzheimer's disease associated, novel 24-mer peptide which contains a difficult sequence
    • Evangelou, A., C. Zikos, E. Livaniou, and G.P. Evangelatos. 2004. High-yield, solid-phase synthesis of humanin, an Alzheimer's disease associated, novel 24-mer peptide which contains a difficult sequence. J. Pept. Sci. 10:631-635.
    • (2004) J. Pept. Sci , vol.10 , pp. 631-635
    • Evangelou, A.1    Zikos, C.2    Livaniou, E.3    Evangelatos, G.P.4
  • 12
    • 0038136890 scopus 로고    scopus 로고
    • Role of prodomain in importin-mediated nuclear localization and activation of caspase-2
    • Baliga, B.C., P.A. Colussi, S.H. Read, M.M. Dias, D.A. Jans, and S. Kumar. 2003. Role of prodomain in importin-mediated nuclear localization and activation of caspase-2. J. Biol. Chem. 278:4899-4905.
    • (2003) J. Biol. Chem , vol.278 , pp. 4899-4905
    • Baliga, B.C.1    Colussi, P.A.2    Read, S.H.3    Dias, M.M.4    Jans, D.A.5    Kumar, S.6
  • 13
    • 27644595172 scopus 로고    scopus 로고
    • Baker, R.T., A.M. Catanzariti, Y. Karunasekara, T.A. Soboleva, R. Sharwood, S. Whitney, and P.G. Board. 2005. Using deubiquitylating enzymes as research tools. Methods Enzymol. 398:540-554.
    • Baker, R.T., A.M. Catanzariti, Y. Karunasekara, T.A. Soboleva, R. Sharwood, S. Whitney, and P.G. Board. 2005. Using deubiquitylating enzymes as research tools. Methods Enzymol. 398:540-554.
  • 14
    • 0030030956 scopus 로고    scopus 로고
    • First-order kinetic model of Alzheimer's beta-amyloid fibril extension in vitro
    • Naiki, H. and K. Nakakuki. 1996. First-order kinetic model of Alzheimer's beta-amyloid fibril extension in vitro. Lab. Invest. 74:374-383.
    • (1996) Lab. Invest , vol.74 , pp. 374-383
    • Naiki, H.1    Nakakuki, K.2
  • 15
    • 0035812658 scopus 로고    scopus 로고
    • Identification and characterization of key kinetic intermediates in amyloid beta-protein fibrillogenesis
    • Kirkitadze, M.D., M.M. Condron, and D.B. Teplow. 2001. Identification and characterization of key kinetic intermediates in amyloid beta-protein fibrillogenesis. J. Mol. Biol. 312:1103-1119.
    • (2001) J. Mol. Biol , vol.312 , pp. 1103-1119
    • Kirkitadze, M.D.1    Condron, M.M.2    Teplow, D.B.3
  • 16
    • 10644275363 scopus 로고    scopus 로고
    • Optimized expression of soluble cyclomaltodextrinase of thermophilic origin in Escherichia coli by using a soluble fusiontag and by tuning of inducer concentration
    • Turner, P., O. Hoist, and E.N. Karlsson. 2005. Optimized expression of soluble cyclomaltodextrinase of thermophilic origin in Escherichia coli by using a soluble fusiontag and by tuning of inducer concentration. Protein Expr. Purif. 39:54-60.
    • (2005) Protein Expr. Purif , vol.39 , pp. 54-60
    • Turner, P.1    Hoist, O.2    Karlsson, E.N.3
  • 17
    • 25644459395 scopus 로고    scopus 로고
    • Fusion tags and chaperone co-expression modulate both the solubility and the inclusion body features of the recombinant CLIPB14 serine protease
    • Schrodel, A., J. Volz, and A. de Marco. 2005. Fusion tags and chaperone co-expression modulate both the solubility and the inclusion body features of the recombinant CLIPB14 serine protease. J. Biotechnol. 120:2-10.
    • (2005) J. Biotechnol , vol.120 , pp. 2-10
    • Schrodel, A.1    Volz, J.2    de Marco, A.3
  • 18
    • 28844481147 scopus 로고    scopus 로고
    • Solubility-enhancing proteins MBP and NusA play a passive role in the folding of their fusion partners
    • Nallamsetty, S. and D.S. Waugh. 2006. Solubility-enhancing proteins MBP and NusA play a passive role in the folding of their fusion partners. Protein Expr. Purif. 45:175-182.
    • (2006) Protein Expr. Purif , vol.45 , pp. 175-182
    • Nallamsetty, S.1    Waugh, D.S.2
  • 20
    • 0036308719 scopus 로고    scopus 로고
    • Mutations that reduce aggregation of the Alzheimer's Abeta42 peptide: An unbiased search for the sequence determinants of Abeta amyloidogenesis
    • Wurth, C., N.K. Guimard, and M.H. Hecht. 2002. Mutations that reduce aggregation of the Alzheimer's Abeta42 peptide: an unbiased search for the sequence determinants of Abeta amyloidogenesis. J. Mol. Biol. 319:1279-1290.
    • (2002) J. Mol. Biol , vol.319 , pp. 1279-1290
    • Wurth, C.1    Guimard, N.K.2    Hecht, M.H.3
  • 21
    • 13844256497 scopus 로고    scopus 로고
    • Production of recombinant amyloid-beta peptide 42 as an ubiquitin extension
    • Lee, E.K., J.H. Hwang, D.Y. Shin, D.I. Kim, and Y.J. Yoo. 2005. Production of recombinant amyloid-beta peptide 42 as an ubiquitin extension. Protein Expr. Purif. 40:183-189.
    • (2005) Protein Expr. Purif , vol.40 , pp. 183-189
    • Lee, E.K.1    Hwang, J.H.2    Shin, D.Y.3    Kim, D.I.4    Yoo, Y.J.5
  • 23
  • 24
    • 0029160765 scopus 로고
    • A biotechnological method provides access to aggregation competent monomeric Alzheimer's 1-42 residue amyloid peptide
    • Dobeli, H., N. Draeger, G. Huber, P. Jakob, D. Schmidt, B. Seilheimer, D. Stuber, B. Wipf, et al. 1995. A biotechnological method provides access to aggregation competent monomeric Alzheimer's 1-42 residue amyloid peptide. Biotechnology (NY) 75:988-993.
    • (1995) Biotechnology (NY) , vol.75 , pp. 988-993
    • Dobeli, H.1    Draeger, N.2    Huber, G.3    Jakob, P.4    Schmidt, D.5    Seilheimer, B.6    Stuber, D.7    Wipf, B.8
  • 25
    • 0026756887 scopus 로고
    • Methodological variables in the assessment of beta amyloid neurotoxicity
    • Busciglio, J., A. Lorenzo, and B.A. Yankner. 1992. Methodological variables in the assessment of beta amyloid neurotoxicity. Neurobiol. Aging 13:609-612.
    • (1992) Neurobiol. Aging , vol.13 , pp. 609-612
    • Busciglio, J.1    Lorenzo, A.2    Yankner, B.A.3
  • 27
    • 0038623056 scopus 로고    scopus 로고
    • Trigger factor-mediated prolyl isomerization influences maturation of the Streptococcus pyogenes cysteine protease
    • Lyon, W.R. and M.G. Caparon. 2003. Trigger factor-mediated prolyl isomerization influences maturation of the Streptococcus pyogenes cysteine protease. J. Bacteriol. 185:3661-3667.
    • (2003) J. Bacteriol , vol.185 , pp. 3661-3667
    • Lyon, W.R.1    Caparon, M.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.