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Volumn 20, Issue 5 SUPPL., 2007, Pages 6-14

Applying fusion protein technology to E. coli

Author keywords

[No Author keywords available]

Indexed keywords

BETA1A INTERFERON; ETANERCEPT; HYBRID PROTEIN; NOVEL ERYTHROPOIESIS STIMULATING PROTEIN; RECOMBINANT ERYTHROPOIETIN; RECOMBINANT GRANULOCYTE COLONY STIMULATING FACTOR; RECOMBINANT PROTEIN; RESIN;

EID: 34249021711     PISSN: 1542166X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (3)

References (61)
  • 1
    • 11144334098 scopus 로고    scopus 로고
    • Recombinant protein therapeutics-success rates, market trends and values to 2010
    • Panlou AK, Reichert JM. Recombinant protein therapeutics-success rates, market trends and values to 2010. Nature Biotechnol. 2004; 12:1513-9.
    • (2004) Nature Biotechnol , vol.12 , pp. 1513-1519
    • Panlou, A.K.1    Reichert, J.M.2
  • 3
    • 0035985128 scopus 로고    scopus 로고
    • Co-overexpression of folding modulators improves the solubility of the recombinant guinea pig liver transglutaminase in Escherichia coli
    • Ikura K, Kokubu T, Natsuka S, Ichikawa A, Adachi M, Nishihara K, et al. Co-overexpression of folding modulators improves the solubility of the recombinant guinea pig liver transglutaminase in Escherichia coli. Prep. Biochem. Biotechnol. 2002; 32:189-205.
    • (2002) Prep. Biochem. Biotechnol , vol.32 , pp. 189-205
    • Ikura, K.1    Kokubu, T.2    Natsuka, S.3    Ichikawa, A.4    Adachi, M.5    Nishihara, K.6
  • 4
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith DB, Johnson, KS. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene. 1988; 67:31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 5
    • 0023959219 scopus 로고
    • Production in Escherichia coli and one-step purification of bifunctional hybrid proteins which bind maltose. Export of the Klenow polymerase into the periplasmic space
    • Bedouelle H, Duplay P. Production in Escherichia coli and one-step purification of bifunctional hybrid proteins which bind maltose. Export of the Klenow polymerase into the periplasmic space. Eur. J. Biochem. 1988; 171:541-549.
    • (1988) Eur. J. Biochem , vol.171 , pp. 541-549
    • Bedouelle, H.1    Duplay, P.2
  • 6
    • 0023680201 scopus 로고
    • Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein
    • Di Guan C, Li P, Riggs PD, Inouye H. Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein. Gene. 1988; 67:21-30.
    • (1988) Gene , vol.67 , pp. 21-30
    • Di Guan, C.1    Li, P.2    Riggs, P.D.3    Inouye, H.4
  • 7
    • 0033589826 scopus 로고    scopus 로고
    • New fusion protein systems designed to give soluble expression in Escherichia coli
    • Davis GD, Elisee C, Newham DM, Harrison RG. New fusion protein systems designed to give soluble expression in Escherichia coli. Biotechnol. Bioeng. 1999; 65:382-388.
    • (1999) Biotechnol. Bioeng , vol.65 , pp. 382-388
    • Davis, G.D.1    Elisee, C.2    Newham, D.M.3    Harrison, R.G.4
  • 8
    • 14744292185 scopus 로고
    • A thioredoxin gene fusion expression system that circumvents inclusion body formation in the E. coli cytoplasm
    • LaVallie ER, DiBlasio EA, Kovacic S, Grant KL, Schendel PF, McCoy JM. A thioredoxin gene fusion expression system that circumvents inclusion body formation in the E. coli cytoplasm. Biotechnology. 1993; 11:187-193.
    • (1993) Biotechnology , vol.11 , pp. 187-193
    • LaVallie, E.R.1    DiBlasio, E.A.2    Kovacic, S.3    Grant, K.L.4    Schendel, P.F.5    McCoy, J.M.6
  • 9
    • 0023747768 scopus 로고
    • Major surface antigen p190 of Plasmodium falciparum: Detection of common epitopes present in a variety of plasmodia isolates
    • Gentz R, Certa U, Takacs B, Matile H, Döbeli H, Pink R, et al. Major surface antigen p190 of Plasmodium falciparum: Detection of common epitopes present in a variety of plasmodia isolates. EMBO J. 1988; 7:225-230.
    • (1988) EMBO J , vol.7 , pp. 225-230
    • Gentz, R.1    Certa, U.2    Takacs, B.3    Matile, H.4    Döbeli, H.5    Pink, R.6
  • 10
    • 0023781763 scopus 로고
    • Genetic approach to facilitate purifaction of recombinant proteins with a novel metal chelate adsorbent
    • Hochuli E, Bannwarth W, Döbeli H, Gentz R, Stüber D. Genetic approach to facilitate purifaction of recombinant proteins with a novel metal chelate adsorbent. Biotechnol. 1988; 6:1321-1325.
    • (1988) Biotechnol , vol.6 , pp. 1321-1325
    • Hochuli, E.1    Bannwarth, W.2    Döbeli, H.3    Gentz, R.4    Stüber, D.5
  • 11
    • 0024296676 scopus 로고
    • Chelating peptide-immobilized metal ion affinity chromatography. A new concept in affinity chromatography for recombinant proteins
    • Smith MC, Furman TC, Ingolia TD, Pidgeon C. Chelating peptide-immobilized metal ion affinity chromatography. A new concept in affinity chromatography for recombinant proteins. J. Biol. Chem. 1988; 263:7211-7215.
    • (1988) J. Biol. Chem , vol.263 , pp. 7211-7215
    • Smith, M.C.1    Furman, T.C.2    Ingolia, T.D.3    Pidgeon, C.4
  • 13
    • 20444419709 scopus 로고    scopus 로고
    • Enhanced expression and purification of membrane proteins by SUMO fusion in E. coli
    • Zuo X, Li S, Hall J, Mattern MR, Tran H, Shoo J, et al. Enhanced expression and purification of membrane proteins by SUMO fusion in E. coli. J. Struct. Funct. Genomics. 2005; 6:103-111.
    • (2005) J. Struct. Funct. Genomics , vol.6 , pp. 103-111
    • Zuo, X.1    Li, S.2    Hall, J.3    Mattern, M.R.4    Tran, H.5    Shoo, J.6
  • 14
    • 20444400305 scopus 로고    scopus 로고
    • Expression and purification of SARS Coronavirus proteins using SUMO fusions
    • Zuo X, Mattern MR, Tan R, Li S, Hall J, Sterner DE, et al. Expression and purification of SARS Coronavirus proteins using SUMO fusions. Protein Express Purif. 2005; 42:100-110.
    • (2005) Protein Express Purif , vol.42 , pp. 100-110
    • Zuo, X.1    Mattern, M.R.2    Tan, R.3    Li, S.4    Hall, J.5    Sterner, D.E.6
  • 16
    • 29344475982 scopus 로고    scopus 로고
    • Comparison of SUMO fusion technology with traditional gene fusion systems: Enhanced expression and solubility with SUMO
    • Marblestone JG, Edavettal SC, Lim. Y, Lim P, Zuo X, Butt TR. Comparison of SUMO fusion technology with traditional gene fusion systems: Enhanced expression and solubility with SUMO. Protein Sci. 2006; 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
  • 17
    • 0036145552 scopus 로고    scopus 로고
    • Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli
    • Hammarstrom M, Hellgren N, van Den Berg S, Berglund H, Hard T. Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli. Protein Sci. 2002; 11(2):313-321.
    • (2002) Protein Sci , vol.11 , Issue.2 , pp. 313-321
    • Hammarstrom, M.1    Hellgren, N.2    van Den Berg, S.3    Berglund, H.4    Hard, T.5
  • 20
    • 13244265563 scopus 로고    scopus 로고
    • Production of soluble mammalian proteins in Escherichia coli: Identification of protein features that correlate with successful expression
    • Dyson MR, Shadbolt SP, Vincent KJ, Perera RL, McCafferty J. Production of soluble mammalian proteins in Escherichia coli: identification of protein features that correlate with successful expression. BMC Biotechnol. 2004; 4:32.
    • (2004) BMC Biotechnol , vol.4 , pp. 32
    • Dyson, M.R.1    Shadbolt, S.P.2    Vincent, K.J.3    Perera, R.L.4    McCafferty, J.5
  • 21
    • 4444378435 scopus 로고    scopus 로고
    • The solubility and stability of recombinant proteins are increased by their fusion to NusA
    • De Marco V, Stier G, Blandin S, de Marco A. The solubility and stability of recombinant proteins are increased by their fusion to NusA. Biochem. Biophys. Res. Commun. 2004; 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
  • 22
    • 0026211940 scopus 로고
    • Metal affinity chromatography of recombinant HIV-1 reverse transcriptase containing a human renin cleavable metal binding domain
    • Sharma SK, Evans DB, Vosters AF, McQuade TJ, Tarpley WG. Metal affinity chromatography of recombinant HIV-1 reverse transcriptase containing a human renin cleavable metal binding domain. Biotechnol. Appl. Biochem. 1991; 14:69-81.
    • (1991) Biotechnol. Appl. Biochem , vol.14 , pp. 69-81
    • Sharma, S.K.1    Evans, D.B.2    Vosters, A.F.3    McQuade, T.J.4    Tarpley, W.G.5
  • 23
    • 0023680201 scopus 로고
    • Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein
    • Di Guan C, Li P, Riggs PD, Inouye H. Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein. Gene. 1988; 67:21-30.
    • (1988) Gene , vol.67 , pp. 21-30
    • Di Guan, C.1    Li, P.2    Riggs, P.D.3    Inouye, H.4
  • 24
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione-S-transferase
    • Smith DB, Johnson KS. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione-S-transferase. Gene. 1988; 67:31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 25
    • 0029828233 scopus 로고    scopus 로고
    • Strategies for achieving high-level expression of genes in Escherichia coli
    • Makrides AC. Strategies for achieving high-level expression of genes in Escherichia coli. Microbiol. Reviews. 1996; 60:512-538.
    • (1996) Microbiol. Reviews , vol.60 , pp. 512-538
    • Makrides, A.C.1
  • 26
    • 0035190397 scopus 로고    scopus 로고
    • Codon optimization of gene fragments encoding Plasmodium falciparum merzoite proteins enhances DNA vaccine protein expression and immunogenicity in mice
    • Narum DL, Kumar S, Rogers WO, Fuhrmann SR, Liang H, Oakley M, et al. Codon optimization of gene fragments encoding Plasmodium falciparum merzoite proteins enhances DNA vaccine protein expression and immunogenicity in mice. Infect. Immun. 2001; 69:7250-3.
    • (2001) Infect. Immun , vol.69 , pp. 7250-7253
    • Narum, D.L.1    Kumar, S.2    Rogers, W.O.3    Fuhrmann, S.R.4    Liang, H.5    Oakley, M.6
  • 27
    • 0024825088 scopus 로고
    • High-level expression of recombinant genes in Escherichia coli is dependent on the availability of the dnaY gene product
    • Brinkmann U, Mattes RE, Buckel P. High-level expression of recombinant genes in Escherichia coli is dependent on the availability of the dnaY gene product. Gene. 1989; 85:109-114.
    • (1989) Gene , vol.85 , pp. 109-114
    • Brinkmann, U.1    Mattes, R.E.2    Buckel, P.3
  • 29
    • 0026305697 scopus 로고
    • Controlling basal expression in an inducible T7 expression system by blocking the target T7 promoter with the lac repressor
    • Dubendorff JW, Studier FW. Controlling basal expression in an inducible T7 expression system by blocking the target T7 promoter with the lac repressor. J. Mol. Biol. 1991; 219:45-59.
    • (1991) J. Mol. Biol , vol.219 , pp. 45-59
    • Dubendorff, J.W.1    Studier, F.W.2
  • 30
    • 0025144364 scopus 로고
    • Differential gene expression mediated by late, very late and hybrid baculovirus promoters
    • Thiem SM, Miller LK. Differential gene expression mediated by late, very late and hybrid baculovirus promoters. Gene. 1980; 91:87-94.
    • (1980) Gene , vol.91 , pp. 87-94
    • Thiem, S.M.1    Miller, L.K.2
  • 31
    • 0033809233 scopus 로고    scopus 로고
    • Fusions to maltose-binding protein: Control of folding and solubility in protein purification
    • Sachdev D, Chirgwin JM. Fusions to maltose-binding protein: Control of folding and solubility in protein purification. Methods Enzymol. 2000; 326:321-321.
    • (2000) Methods Enzymol , vol.326 , pp. 321-321
    • Sachdev, D.1    Chirgwin, J.M.2
  • 32
    • 0038643751 scopus 로고    scopus 로고
    • Over-expression of Escherichia coli F1F(o)-ATPase subunit a is inhibited by instability of the uncB gene transcript
    • Arechaga I, Miroux B, Runswick MJ, Walker JE. Over-expression of Escherichia coli F1F(o)-ATPase subunit a is inhibited by instability of the uncB gene transcript. FEBS Lett. 2003; 547;97-100.
    • (2003) FEBS Lett , vol.547 , pp. 97-100
    • Arechaga, I.1    Miroux, B.2    Runswick, M.J.3    Walker, J.E.4
  • 33
    • 0030941829 scopus 로고    scopus 로고
    • The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm
    • Prinz A, Aslund F, Holmgren A, Beckwith J. The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm. J. Biol. Chem. 1997; 272:15661-7.
    • (1997) J. Biol. Chem , vol.272 , pp. 15661-15667
    • Prinz, A.1    Aslund, F.2    Holmgren, A.3    Beckwith, J.4
  • 34
    • 0035985128 scopus 로고    scopus 로고
    • Co-overexpression of folding modulators improves the solubility of the recombinant guinea pig liver transglutaminase in Escherichia coli
    • Ikura K, Kokubu T, Natsuka S, Ichikawa A, Adachi M, Nishihara K, et al. Co-overexpression of folding modulators improves the solubility of the recombinant guinea pig liver transglutaminase in Escherichia coli. Prep. Biochem. Biotechnol. 2002; 32:189-205.
    • (2002) Prep. Biochem. Biotechnol , vol.32 , pp. 189-205
    • Ikura, K.1    Kokubu, T.2    Natsuka, S.3    Ichikawa, A.4    Adachi, M.5    Nishihara, K.6
  • 35
    • 0027997012 scopus 로고
    • Correctly folded T-cell receptor fragments In the periplasm of Escherichia coli. Influence of folding catalysts
    • Wulfing C, Pluckthun A. Correctly folded T-cell receptor fragments In the periplasm of Escherichia coli. Influence of folding catalysts. J. Mol. Biol. 1994; 242:655-669.
    • (1994) J. Mol. Biol , vol.242 , pp. 655-669
    • Wulfing, C.1    Pluckthun, A.2
  • 36
    • 13544264496 scopus 로고    scopus 로고
    • Improved secretory production of recombinant proteins by random mutagenesis of hlyB, an a-hemolysin transporter from Escherichia coli
    • Sugamata Y, Shiba T. Improved secretory production of recombinant proteins by random mutagenesis of hlyB, an a-hemolysin transporter from Escherichia coli. Appl. Environ. Microbiol. 2005; 71:656-662.
    • (2005) Appl. Environ. Microbiol , vol.71 , pp. 656-662
    • Sugamata, Y.1    Shiba, T.2
  • 37
    • 0028303849 scopus 로고
    • Improved synthesis of Salmonella typhimurium enterotoxin using gene fusion expression systems
    • Chopra AK, Brasier AR, Das M, Xu XJ, Peterson JW. Improved synthesis of Salmonella typhimurium enterotoxin using gene fusion expression systems. Gene. 1994; 144:81-85.
    • (1994) Gene , vol.144 , pp. 81-85
    • Chopra, A.K.1    Brasier, A.R.2    Das, M.3    Xu, X.J.4    Peterson, J.W.5
  • 38
    • 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 JD, Kapust RB, Waugh DS. 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. 2001; 10:622-630.
    • (2001) Protein Sci , vol.10 , pp. 622-630
    • Fox, J.D.1    Kapust, R.B.2    Waugh, D.S.3
  • 39
    • 0033871781 scopus 로고    scopus 로고
    • Protein folding intermediates and pathways studied by hydrogen exchange
    • Englander SW. Protein folding intermediates and pathways studied by hydrogen exchange. Annu. Rev. Biophys. Biomol. Struct. 2000; 29:213-38.
    • (2000) Annu. Rev. Biophys. Biomol. Struct , vol.29 , pp. 213-238
    • Englander, S.W.1
  • 40
    • 0031026007 scopus 로고    scopus 로고
    • How important is the molten globule for correct protein folding?
    • Creighton TE. How important is the molten globule for correct protein folding? Trends Biochem. Sci. 1997; 22:6-10.
    • (1997) Trends Biochem. Sci , vol.22 , pp. 6-10
    • Creighton, T.E.1
  • 41
    • 0035823143 scopus 로고    scopus 로고
    • Escherichia coli maltose-binding protein as a molecular chaperone for recombinant intracellular cytoplasmic single-chain antibodies
    • Bach H, Mazor Y, Shaky S, Shoham-Lev A, Berdichevsky Y, Gutnick DL, Benhar I. Escherichia coli maltose-binding protein as a molecular chaperone for recombinant intracellular cytoplasmic single-chain antibodies. J. Mol. Biol. 2001; 312(1):79-93.
    • (2001) J. Mol. Biol , vol.312 , Issue.1 , pp. 79-93
    • Bach, H.1    Mazor, Y.2    Shaky, S.3    Shoham-Lev, A.4    Berdichevsky, Y.5    Gutnick, D.L.6    Benhar, I.7
  • 42
    • 0034956228 scopus 로고    scopus 로고
    • A strategy for optimizing the monodispersity of fusion proteins: Application to purification of recombinant HPV E6 oncoprotein
    • Nomine Y, Ristriani T, Laurent C, Lefevre J-F, Weiss E, Trave G. A strategy for optimizing the monodispersity of fusion proteins: application to purification of recombinant HPV E6 oncoprotein. Protein Eng. 2001; 14(4):297-305.
    • (2001) Protein Eng , vol.14 , Issue.4 , pp. 297-305
    • Nomine, Y.1    Ristriani, T.2    Laurent, C.3    Lefevre, J.-F.4    Weiss, E.5    Trave, G.6
  • 43
    • 53149124391 scopus 로고    scopus 로고
    • Properties of soluble fusions between mammalian aspartic proteinases and bacterial maltose-binding protein
    • Sachdev D, Chirgwin JM. Properties of soluble fusions between mammalian aspartic proteinases and bacterial maltose-binding protein. J. Protein Chem. 1999; 18(1):127-136.
    • (1999) J. Protein Chem , vol.18 , Issue.1 , pp. 127-136
    • Sachdev, D.1    Chirgwin, J.M.2
  • 44
    • 2942609001 scopus 로고    scopus 로고
    • Fast identification of folded human protein domains expressed in E. coli suitable for structural analysis
    • Scheich C, Leitner D, Sievert V, Leidert M, Schlegel B, Simon B, et al. Fast identification of folded human protein domains expressed in E. coli suitable for structural analysis. BMC Struct. Biol. 2004, 4(1):4.
    • (2004) BMC Struct. Biol , vol.4 , Issue.1 , pp. 4
    • Scheich, C.1    Leitner, D.2    Sievert, V.3    Leidert, M.4    Schlegel, B.5    Simon, B.6
  • 45
    • 3142689876 scopus 로고    scopus 로고
    • Analysis and control of proteolysis of recombinant proteins in Escherichia coli
    • Rozkov A, Enfors SO. Analysis and control of proteolysis of recombinant proteins in Escherichia coli. Adv. Biochem. Engin./Biotechnol. 2004; 89:163-195.
    • (2004) Adv. Biochem. Engin./Biotechnol , vol.89 , pp. 163-195
    • Rozkov, A.1    Enfors, S.O.2
  • 46
    • 0015523019 scopus 로고
    • Efffects of protease inhibitors on protein breakdown in Escherichia coli
    • Prouty W, Goldberg A. Efffects of protease inhibitors on protein breakdown in Escherichia coli. J. Biol. Chem. 1972; 247:3341-3352.
    • (1972) J. Biol. Chem , vol.247 , pp. 3341-3352
    • Prouty, W.1    Goldberg, A.2
  • 47
    • 0013564318 scopus 로고
    • Cellular location affects protein stability in Escherichia coli
    • Talmadge K, Gilbert W. Cellular location affects protein stability in Escherichia coli. Proc. Natl. Acad. Sci. 1982; 79:1830-1833.
    • (1982) Proc. Natl. Acad. Sci , vol.79 , pp. 1830-1833
    • Talmadge, K.1    Gilbert, W.2
  • 48
    • 0025327105 scopus 로고
    • Expression and characterization of a recombinant human parathyroid hormone secreted by Escherichia coli employing the staphylocccal protein A promoter and signal sequence
    • Hogset A, Blingsom OR, Saether O, Gautvik VT, Holmgren E, Hartmanis M, et al. Expression and characterization of a recombinant human parathyroid hormone secreted by Escherichia coli employing the staphylocccal protein A promoter and signal sequence. J. Biol. Chem. 1990; 265:7338-7344.
    • (1990) J. Biol. Chem , vol.265 , pp. 7338-7344
    • Hogset, A.1    Blingsom, O.R.2    Saether, O.3    Gautvik, V.T.4    Holmgren, E.5    Hartmanis, M.6
  • 49
    • 0030110770 scopus 로고    scopus 로고
    • Upstream strategies to minimize proteolytic degradation upon recombinant production in Escherichia coli
    • Murby M, Uhlen M, Stahl S. Upstream strategies to minimize proteolytic degradation upon recombinant production in Escherichia coli. Protein Express. Purif. 1996; 7:129-36.
    • (1996) Protein Express. Purif , vol.7 , pp. 129-136
    • Murby, M.1    Uhlen, M.2    Stahl, S.3
  • 50
    • 0028901398 scopus 로고
    • Expression of recombinant human phenylalanine hydroxylase as fusion protein in Escherichia coli circumvents proteolytic degradation by host cell proteases. Isolation and characterization of the wild-type enzyme
    • Martinez A, Knappskog PM, Olafsdottir S, Doskeland AP, Eiken HG, Svebak RM, et al. Expression of recombinant human phenylalanine hydroxylase as fusion protein in Escherichia coli circumvents proteolytic degradation by host cell proteases. Isolation and characterization of the wild-type enzyme. Biochem. J. 1995; 306:589-97.
    • (1995) Biochem. J , vol.306 , pp. 589-597
    • Martinez, A.1    Knappskog, P.M.2    Olafsdottir, S.3    Doskeland, A.P.4    Eiken, H.G.5    Svebak, R.M.6
  • 51
    • 0027202203 scopus 로고
    • Augmentation of protein production by a combination of the T7 RNA polymerase system and ubiquitin fusion: Overproduction of the human DNA repair protein, ERCC1, as an ubiquitin fusion protein in Escherichia coli
    • Koken MH, Odijk HH, van Duin M, Fornerod M, Hoeijmakers JH. Augmentation of protein production by a combination of the T7 RNA polymerase system and ubiquitin fusion: overproduction of the human DNA repair protein, ERCC1, as an ubiquitin fusion protein in Escherichia coli. Biochem. Biophys. Res. Commun. 1993; 195:643-653.
    • (1993) Biochem. Biophys. Res. Commun , vol.195 , pp. 643-653
    • Koken, M.H.1    Odijk, H.H.2    van Duin, M.3    Fornerod, M.4    Hoeijmakers, J.H.5
  • 52
    • 0026284951 scopus 로고
    • Stabilization of recombinant proteins from proteolytic degradation in Escherichia coli using a dual affinity fusion strategy
    • Murby M, Cedergren L, Nilsson J, Nygren PA, Hammarberg B, Nilsson B, et al. Stabilization of recombinant proteins from proteolytic degradation in Escherichia coli using a dual affinity fusion strategy. Biotechnol. Appl. Biochem. 1991; 14:336-346.
    • (1991) Biotechnol. Appl. Biochem , vol.14 , pp. 336-346
    • Murby, M.1    Cedergren, L.2    Nilsson, J.3    Nygren, P.A.4    Hammarberg, B.5    Nilsson, B.6
  • 53
    • 0345665954 scopus 로고
    • Multiple joined genes prevent product degradation in Escherichia coli
    • Shen SH. Multiple joined genes prevent product degradation in Escherichia coli. Proc. Natl. Acad. Sci. 1984; 81:4627-31.
    • (1984) Proc. Natl. Acad. Sci , vol.81 , pp. 4627-4631
    • Shen, S.H.1
  • 54
    • 0029861143 scopus 로고    scopus 로고
    • The N-end rule: Functions, mysteries, uses
    • Varshavsky A. The N-end rule: functions, mysteries, uses. Proc. Natl. Acad. Sci. 1996; 93:12142-9.
    • (1996) Proc. Natl. Acad. Sci , vol.93 , pp. 12142-12149
    • Varshavsky, A.1
  • 56
    • 0028337332 scopus 로고
    • Maltose transport system of Escherichia coli: An ABC-type transporter
    • Nikaido H. Maltose transport system of Escherichia coli: an ABC-type transporter. FEBS Lett. 1994; 346:55-8.
    • (1994) FEBS Lett , vol.346 , pp. 55-58
    • Nikaido, H.1
  • 57
    • 0035169206 scopus 로고    scopus 로고
    • Understanding the art of producing protein and nonprotein molecules in Escherichia coli
    • Balbas P. Understanding the art of producing protein and nonprotein molecules in Escherichia coli. Mol. Biotech. 2001; 19:251-267.
    • (2001) Mol. Biotech , vol.19 , pp. 251-267
    • Balbas, P.1
  • 58
    • 17744415288 scopus 로고    scopus 로고
    • Single-column purification of free recombinant proteins using a self-cleavable affinity tag derived from a protein splicing element
    • Chong S, Mersha FB, Comb DG, Scott ME, Landry D, Vence LM, et al. Single-column purification of free recombinant proteins using a self-cleavable affinity tag derived from a protein splicing element. Gene. 1997; 192:277-281.
    • (1997) Gene , vol.192 , pp. 277-281
    • Chong, S.1    Mersha, F.B.2    Comb, D.G.3    Scott, M.E.4    Landry, D.5    Vence, L.M.6
  • 59
    • 0141539517 scopus 로고    scopus 로고
    • A critical review of the methods for cleavage of fusion proteins with thrombin and factor Xa
    • Jenny RJ, Mann KG, Lundblad RL. A critical review of the methods for cleavage of fusion proteins with thrombin and factor Xa. Protein Express. Purif. 2003; 31:1-11.
    • (2003) Protein Express. Purif , vol.31 , pp. 1-11
    • Jenny, R.J.1    Mann, K.G.2    Lundblad, R.L.3
  • 61
    • 0032884573 scopus 로고    scopus 로고
    • Baneyx F. Recombinant protein expression in Escherichia coli. Opin. Biotech. 10: 411-421.
    • Baneyx F. Recombinant protein expression in Escherichia coli. Opin. Biotech. 10: 411-421.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.