메뉴 건너뛰기




Volumn 4, Issue 1, 2007, Pages 67-78

Optimization of protein expression systems for modern drug discovery

Author keywords

Automation; Baculovirus; Cell free transcription; Cell free translation; Escherichia coli; Mammalian; Recombinant protein expression

Indexed keywords

BACTERIAL PROTEIN; CELL PROTEIN; RECOMBINANT PROTEIN; VIRUS PROTEIN;

EID: 33846894709     PISSN: 14789450     EISSN: 17448387     Source Type: Journal    
DOI: 10.1586/14789450.4.1.67     Document Type: Review
Times cited : (21)

References (77)
  • 1
    • 3543140130 scopus 로고    scopus 로고
    • Protein crystallization in the structural genomics era
    • McPherson A. Protein crystallization in the structural genomics era. J. Struct. Funct. Genomics 5(1-2), 3-12 (2004).
    • (2004) J. Struct. Funct. Genomics , vol.5 , Issue.1-2 , pp. 3-12
    • McPherson, A.1
  • 2
    • 33744977069 scopus 로고    scopus 로고
    • Mayr LM. Tackling the chemo-genomic space by novel screening technologies: monograph of ESRF Workshop 58. In: Chemical Genomics: Small Molecule Probes to Study Cellular Function. Jaroch S, Weinmann H (Eds.), Springer Verlag, Weinheim, Germany, 111-173 (2006).
    • Mayr LM. Tackling the chemo-genomic space by novel screening technologies: monograph of ESRF Workshop 58. In: Chemical Genomics: Small Molecule Probes to Study Cellular Function. Jaroch S, Weinmann H (Eds.), Springer Verlag, Weinheim, Germany, 111-173 (2006).
  • 4
    • 13844281394 scopus 로고    scopus 로고
    • Directed evolution of proteins for heterologous expression and stability
    • Roodveldt C, Aharoni A, Tawfik DS. Directed evolution of proteins for heterologous expression and stability. Curr. Opin. Struct. Biol. 15, 50-56 (2005).
    • (2005) Curr. Opin. Struct. Biol , vol.15 , pp. 50-56
    • Roodveldt, C.1    Aharoni, A.2    Tawfik, D.S.3
  • 5
    • 0037255597 scopus 로고    scopus 로고
    • Overview of tag protein fusions: From molecular and biochemical fundamentals to commercial systems
    • Terpe K. Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems. Appl. Microbiol. Biotechnol. 60, 523-533 (2003).
    • (2003) Appl. Microbiol. Biotechnol , vol.60 , pp. 523-533
    • Terpe, K.1
  • 7
    • 0347911980 scopus 로고    scopus 로고
    • A favorable solubility partner for the recombinant expression of streptavidin
    • Sorensen HP, Sperling-Petersen HU, Mortensen KK. A favorable solubility partner for the recombinant expression of streptavidin. Protein Expr. Purif. 32, 252-259 (2003).
    • (2003) Protein Expr. Purif , vol.32 , pp. 252-259
    • Sorensen, H.P.1    Sperling-Petersen, H.U.2    Mortensen, K.K.3
  • 8
    • 0038395853 scopus 로고    scopus 로고
    • A rubredoxin based system for screening of protein expression conditions and on-line monitoring of the purification process
    • Kohli BM, Ostermeier C. A rubredoxin based system for screening of protein expression conditions and on-line monitoring of the purification process. Protein Expr. Purif. 28, 362-367 (2003).
    • (2003) Protein Expr. Purif , vol.28 , pp. 362-367
    • Kohli, B.M.1    Ostermeier, C.2
  • 9
    • 27644571313 scopus 로고    scopus 로고
    • Increase of soluble expression in Escherichia coli cytoplasm by a protein disulfide isomerase gene fusion system
    • Liu Y, Zhao TJ, Yan YB, Zhou HM. Increase of soluble expression in Escherichia coli cytoplasm by a protein disulfide isomerase gene fusion system. Protein Expr. Purif. 44, 155-161 (2005).
    • (2005) Protein Expr. Purif , vol.44 , pp. 155-161
    • Liu, Y.1    Zhao, T.J.2    Yan, Y.B.3    Zhou, H.M.4
  • 10
    • 32644478232 scopus 로고    scopus 로고
    • Chatterjee DK, Esposito D. Enhanced soluble protein expression using two new fusion tags. Protein Expr. Purif. 46, 122-129 (2006). • New fusion tags designed for improvement of soluble expression of recombinant proteins in Escherichia coli.
    • Chatterjee DK, Esposito D. Enhanced soluble protein expression using two new fusion tags. Protein Expr. Purif. 46, 122-129 (2006). • New fusion tags designed for improvement of soluble expression of recombinant proteins in Escherichia coli.
  • 11
    • 0036145552 scopus 로고    scopus 로고
    • Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli
    • Hammarström M, Hellgren N, Van der Berg S et al. Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli. Prot. Sci. 11, 313-321 (2002).
    • (2002) Prot. Sci , vol.11 , pp. 313-321
    • Hammarström, M.1    Hellgren, N.2    Van der Berg, S.3
  • 12
    • 0036087525 scopus 로고    scopus 로고
    • High-throughput screening of soluble recombinant proteins
    • Shih YP, Kung WM, Chen JC et al. High-throughput screening of soluble recombinant proteins Prot. Sci. 11, 1714-1719 (2002).
    • (2002) Prot. Sci , vol.11 , pp. 1714-1719
    • Shih, Y.P.1    Kung, W.M.2    Chen, J.C.3
  • 13
    • 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. Biotech. Bioeng. 65, 382-388 (1999).
    • (1999) Biotech. Bioeng , vol.65 , pp. 382-388
    • Davis, G.D.1    Elisee, C.2    Newham, D.M.3    Harrison, R.G.4
  • 14
    • 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 PS, Vincent KJ et al. Production of soluble mammalian proteins in Escherichia coli: identification of protein features that correlate with successful expression. BMC Biotechnology 4, 32 (2004).
    • (2004) BMC Biotechnology , vol.4 , pp. 32
    • Dyson, M.R.1    Shadbolt, P.S.2    Vincent, K.J.3
  • 15
    • 28844481147 scopus 로고    scopus 로고
    • Solubility-enhancing protein MBP and NusA play a passive role in the folding of their fusion partner
    • Nallamsetty S, Waugh DS. Solubility-enhancing protein MBP and NusA play a passive role in the folding of their fusion partner. Protein Expr. Purif. 45, 175-182 (2006).
    • (2006) Protein Expr. Purif , vol.45 , pp. 175-182
    • Nallamsetty, S.1    Waugh, D.S.2
  • 16
    • 0035823143 scopus 로고    scopus 로고
    • Escherichia coli maltose binding protein as a molecular chaperone for recombinant intracellular single-chain antibodies
    • Bach H, Mazor Y, Shaky S et al. Escherichia coli maltose binding protein as a molecular chaperone for recombinant intracellular single-chain antibodies. J. Mol. Biol. 312, 79-93 (2001).
    • (2001) J. Mol. Biol , vol.312 , pp. 79-93
    • Bach, H.1    Mazor, Y.2    Shaky, S.3
  • 17
    • 33646857665 scopus 로고    scopus 로고
    • Current strategies for the use of affinity tags and tag removal for the purification of recombinant proteins
    • Arnau J, Lauritzen C, Petersen GE, Pedersen J. Current strategies for the use of affinity tags and tag removal for the purification of recombinant proteins. Protein Expr. Purif. 48, 1-13 (2006).
    • (2006) Protein Expr. Purif , vol.48 , pp. 1-13
    • Arnau, J.1    Lauritzen, C.2    Petersen, G.E.3    Pedersen, J.4
  • 18
    • 3042825336 scopus 로고    scopus 로고
    • Cold-shock induced high-yield expression protein production in Escherichia coli
    • Qing G, Ma L-C, Khorchid A et al. Cold-shock induced high-yield expression protein production in Escherichia coli. Nat. Biotechnol. 22, 877-882 (2004).
    • (2004) Nat. Biotechnol , vol.22 , pp. 877-882
    • Qing, G.1    Ma, L.-C.2    Khorchid, A.3
  • 19
    • 0031860811 scopus 로고    scopus 로고
    • Nishihiara K, Kanemori M, Kitagawa M et al. Chaperone coexpression plasmids: differential and synergistic roles of DnaK-DnaJ-GrpE and GroEL-GroES in assisted refolding of an allergen from Japanese cedar pollen, Cryi2, in Escherichia coli. Appl. Environ. Microbiol. 64, 1694-1699 (1999).
    • Nishihiara K, Kanemori M, Kitagawa M et al. Chaperone coexpression plasmids: differential and synergistic roles of DnaK-DnaJ-GrpE and GroEL-GroES in assisted refolding of an allergen from Japanese cedar pollen, Cryi2, in Escherichia coli. Appl. Environ. Microbiol. 64, 1694-1699 (1999).
  • 20
    • 26844560708 scopus 로고    scopus 로고
    • Chaperone-mediated folding and maturation of the penicillin acylase precursor in the cytoplasm of Escherichia coli
    • Xu Y, Weng CL, Narayanan N et al. Chaperone-mediated folding and maturation of the penicillin acylase precursor in the cytoplasm of Escherichia coli. Appl. Environ. Microbiol. 71, 6247-6253 (2005).
    • (2005) Appl. Environ. Microbiol , vol.71 , pp. 6247-6253
    • Xu, Y.1    Weng, C.L.2    Narayanan, N.3
  • 21
    • 18144376288 scopus 로고    scopus 로고
    • Coexpression of folding accessory proteins for production of active cyclodextrin glycosyltransferase of Bacillus macerans in recombinant Escherichia coli
    • Sung-Gun K, Dae-Hyuk K, Dae-Hee L et al. Coexpression of folding accessory proteins for production of active cyclodextrin glycosyltransferase of Bacillus macerans in recombinant Escherichia coli. Protein Expr. Purif. 41, 426-432 (2005).
    • (2005) Protein Expr. Purif , vol.41 , pp. 426-432
    • Sung-Gun, K.1    Dae-Hyuk, K.2    Dae-Hee, L.3
  • 22
    • 0242322575 scopus 로고    scopus 로고
    • Chaperonins govern growth of Escherichia coli at low temperatures
    • Ferrer M, Chernikova TN, Yakimov MM et al. Chaperonins govern growth of Escherichia coli at low temperatures. Nat. Biotechnol. 21, 1266-1267 (2003).
    • (2003) Nat. Biotechnol , vol.21 , pp. 1266-1267
    • Ferrer, M.1    Chernikova, T.N.2    Yakimov, M.M.3
  • 23
    • 31344476293 scopus 로고    scopus 로고
    • Strocchi M, Ferrer M, Timmis KN, Golyshin PN. Low temperature-induced systems failure in Escherichia coli: insights from rescue by cold-adapted chaperones. Proteomics 6, 193-206 (2006). • The crucial role of the cold-shock Cpn60/10 chaperone for successful growth of E. coli at low temperatures is elucidated.
    • Strocchi M, Ferrer M, Timmis KN, Golyshin PN. Low temperature-induced systems failure in Escherichia coli: insights from rescue by cold-adapted chaperones. Proteomics 6, 193-206 (2006). • The crucial role of the cold-shock Cpn60/10 chaperone for successful growth of E. coli at low temperatures is elucidated.
  • 24
    • 0037022657 scopus 로고    scopus 로고
    • Proteome-scale purification of human proteins from bacteria
    • Braun P, Ju Y, Halleck A et al. Proteome-scale purification of human proteins from bacteria. Proc. Natl Acad. Sci. USA 99, 2654-2659 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 2654-2659
    • Braun, P.1    Ju, Y.2    Halleck, A.3
  • 25
    • 0035477627 scopus 로고    scopus 로고
    • Screening for soluble expression of recombinant proteins in a 96-well format
    • Knaust RKC, Nordlund P. Screening for soluble expression of recombinant proteins in a 96-well format. Anal. Biochem. 297, 79-85 (2001).
    • (2001) Anal. Biochem , vol.297 , pp. 79-85
    • Knaust, R.K.C.1    Nordlund, P.2
  • 26
    • 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 et al. Fast identification of folded human protein domains expressed in E. coli suitable for structural analysis. BMC Struct. Biol. 4, 4 (2004).
    • (2004) BMC Struct. Biol , vol.4 , pp. 4
    • Scheich, C.1    Leitner, D.2    Sievert, V.3
  • 27
    • 33646112145 scopus 로고    scopus 로고
    • Automated purification of recombinant proteins: Combining high-throughput with high yield
    • Lin CT, Moore PA, Auberry DL et al. Automated purification of recombinant proteins: combining high-throughput with high yield. Protein Expr. Purif. 47, 16-24 (2006).
    • (2006) Protein Expr. Purif , vol.47 , pp. 16-24
    • Lin, C.T.1    Moore, P.A.2    Auberry, D.L.3
  • 28
    • 0036518147 scopus 로고    scopus 로고
    • Identification of in vitro folding conditions for procathepsin S and cathepsin S using fractional factorial screens
    • Tobbell DA, Middleton BJ, Raines S et al. Identification of in vitro folding conditions for procathepsin S and cathepsin S using fractional factorial screens. Protein Expr. Purif. 24, 242-252 (2002).
    • (2002) Protein Expr. Purif , vol.24 , pp. 242-252
    • Tobbell, D.A.1    Middleton, B.J.2    Raines, S.3
  • 29
    • 4644322380 scopus 로고    scopus 로고
    • High-throughput automated refolding screening of inclusion bodies
    • Vincentelli R, Canaan S, Campanacci V et al. High-throughput automated refolding screening of inclusion bodies. Prot. Sci. 22, 2782-2792 (2004).
    • (2004) Prot. Sci , vol.22 , pp. 2782-2792
    • Vincentelli, R.1    Canaan, S.2    Campanacci, V.3
  • 30
    • 22244468386 scopus 로고    scopus 로고
    • Investigation of protein refolding using a fractional factorial screen: A study of reagent effects and interactions
    • Willis MS, Hogan JK, Prabhakar P et al. Investigation of protein refolding using a fractional factorial screen: a study of reagent effects and interactions. Prot. Sci. 14, 1818-1826 (2005).
    • (2005) Prot. Sci , vol.14 , pp. 1818-1826
    • Willis, M.S.1    Hogan, J.K.2    Prabhakar, P.3
  • 32
    • 0038119652 scopus 로고    scopus 로고
    • On-column refolding of recombinant human interferon-γ with an immobilized chaperone fragment
    • Gao YG, Guan YX, Yao SJ, Cho MG. On-column refolding of recombinant human interferon-γ with an immobilized chaperone fragment. Biotechn. Prog. 19, 915-920 (2003).
    • (2003) Biotechn. Prog , vol.19 , pp. 915-920
    • Gao, Y.G.1    Guan, Y.X.2    Yao, S.J.3    Cho, M.G.4
  • 33
    • 23044453734 scopus 로고    scopus 로고
    • Reconstitution of functional nuclear receptor proteins using high pressure refolding
    • Schoner BE, Bramlett KS, Guo H, Burris TP. Reconstitution of functional nuclear receptor proteins using high pressure refolding. Mol. Gen. Metabol. 84, 318-322 (2005).
    • (2005) Mol. Gen. Metabol , vol.84 , pp. 318-322
    • Schoner, B.E.1    Bramlett, K.S.2    Guo, H.3    Burris, T.P.4
  • 34
    • 31344467064 scopus 로고    scopus 로고
    • Effects of solutes on solubilization and refolding of proteins from inclusion bodies with high hydrostatic pressure
    • Lee SH, Carpenter JF, Chang BS et al. Effects of solutes on solubilization and refolding of proteins from inclusion bodies with high hydrostatic pressure. Prot. Sci. 15, 304-313 (2006).
    • (2006) Prot. Sci , vol.15 , pp. 304-313
    • Lee, S.H.1    Carpenter, J.F.2    Chang, B.S.3
  • 36
    • 0346655251 scopus 로고    scopus 로고
    • Baculovirus expression system for magnetic sorting of infected cells and enhanced titer determination
    • Philipps B, Forstner M, Mayr LM. Baculovirus expression system for magnetic sorting of infected cells and enhanced titer determination. Biotechniques 36, 80-83 (2004).
    • (2004) Biotechniques , vol.36 , pp. 80-83
    • Philipps, B.1    Forstner, M.2    Mayr, L.M.3
  • 37
    • 20444373770 scopus 로고    scopus 로고
    • Philipps B, Rotmann D, Wicki M et al. Time reduction and process optimization of the baculovirus expression system for more efficient recombinant protein production in insect cells. Protein Expr. Purif. 42, 211-218 (2005). •• Description of an optimized baculovirus vector and expression methodology that has changed the way recombinant proteins are produced at Novartis International AG (Basel, Switzerland).
    • Philipps B, Rotmann D, Wicki M et al. Time reduction and process optimization of the baculovirus expression system for more efficient recombinant protein production in insect cells. Protein Expr. Purif. 42, 211-218 (2005). •• Description of an optimized baculovirus vector and expression methodology that has changed the way recombinant proteins are produced at Novartis International AG (Basel, Switzerland).
  • 38
    • 23744461088 scopus 로고    scopus 로고
    • Development of a bicistronic baculovirus expression vector by the Rhopalosiphum padi virus 5′ internal ribosome entry site
    • Chen YJ, Chen WS, Wu TY. Development of a bicistronic baculovirus expression vector by the Rhopalosiphum padi virus 5′ internal ribosome entry site. Biochem. Biophys. Res. Commun. 335, 616-623 (2005).
    • (2005) Biochem. Biophys. Res. Commun , vol.335 , pp. 616-623
    • Chen, Y.J.1    Chen, W.S.2    Wu, T.Y.3
  • 39
    • 11144340226 scopus 로고    scopus 로고
    • Baculovirus expression system for heterologous multiprotein complexes
    • Berger I, Fitzgerald DJ, Richmond TJ. Baculovirus expression system for heterologous multiprotein complexes. Nat. Biotechnol. 22, 1583-1587 (2004).
    • (2004) Nat. Biotechnol , vol.22 , pp. 1583-1587
    • Berger, I.1    Fitzgerald, D.J.2    Richmond, T.J.3
  • 40
    • 0038544334 scopus 로고    scopus 로고
    • Developing baculovirus-insect cell expression systems for humanized recombinant glycoprotein production
    • Jarvis DL. Developing baculovirus-insect cell expression systems for humanized recombinant glycoprotein production. Virology 310, 1-7 (2003).
    • (2003) Virology , vol.310 , pp. 1-7
    • Jarvis, D.L.1
  • 41
    • 20144378872 scopus 로고    scopus 로고
    • A baculovirus expression vector system for simultaneous protein expression in insect and mammalian cells
    • Philipps B, Forstner M, Mayr LM. A baculovirus expression vector system for simultaneous protein expression in insect and mammalian cells. Biotechnol. Prog. 21, 708-711 (2005).
    • (2005) Biotechnol. Prog , vol.21 , pp. 708-711
    • Philipps, B.1    Forstner, M.2    Mayr, L.M.3
  • 42
    • 22844450442 scopus 로고    scopus 로고
    • Kost TA, Condreay JP, Jarvis DL. Baculovirus as versatile vectors for protein expression in insect and mammalian cells. Nat. Biotechnol. 23, 567-575 (2005). •• Excellent paper illustrating the capabilities of baculovirus transduction of mammalian cells.
    • Kost TA, Condreay JP, Jarvis DL. Baculovirus as versatile vectors for protein expression in insect and mammalian cells. Nat. Biotechnol. 23, 567-575 (2005). •• Excellent paper illustrating the capabilities of baculovirus transduction of mammalian cells.
  • 43
    • 20444400646 scopus 로고    scopus 로고
    • Improvements to the throughput of recombinant protein expression in the baculovirus/insect cell system
    • McCall EJ, Danielsson A, Hardern IM et al. Improvements to the throughput of recombinant protein expression in the baculovirus/insect cell system. Protein Expr. Purif. 42, 29-36 (2005).
    • (2005) Protein Expr. Purif , vol.42 , pp. 29-36
    • McCall, E.J.1    Danielsson, A.2    Hardern, I.M.3
  • 44
    • 13844271129 scopus 로고    scopus 로고
    • Hunt I. From gene to protein: a review of new and enabling technologies for multi-parallel protein expression. Protein Expr. Purif. 40, 1-22 (2005). • Very good overview of technological developments.
    • Hunt I. From gene to protein: a review of new and enabling technologies for multi-parallel protein expression. Protein Expr. Purif. 40, 1-22 (2005). • Very good overview of technological developments.
  • 45
    • 10644230292 scopus 로고    scopus 로고
    • Optimisation of insect cell growth in deep-well blocks: Development of a high-throughput insect cell expression screen
    • Bahia D, Cheung R, Buchs M et al. Optimisation of insect cell growth in deep-well blocks: development of a high-throughput insect cell expression screen. Protein Expr. Purif. 39, 61-70 (2005).
    • (2005) Protein Expr. Purif , vol.39 , pp. 61-70
    • Bahia, D.1    Cheung, R.2    Buchs, M.3
  • 46
    • 0029043955 scopus 로고
    • Improved adenovirus vector provides herpes simplex virus ribonucleotide reductase R1 and R2 subunits very efficiently
    • Massie B, Dionne J, Lamarche N et al. Improved adenovirus vector provides herpes simplex virus ribonucleotide reductase R1 and R2 subunits very efficiently. Biotechnology (NY) 13, 602-608 (1995).
    • (1995) Biotechnology (NY) , vol.13 , pp. 602-608
    • Massie, B.1    Dionne, J.2    Lamarche, N.3
  • 47
    • 0028696562 scopus 로고
    • Scale up of the adenovirus expression system for the production of recombinant protein in human 293S cells
    • Garnier A, Cote J, Nadeau I et al. Scale up of the adenovirus expression system for the production of recombinant protein in human 293S cells. Cytotechnology 15, 145-155 (1994).
    • (1994) Cytotechnology , vol.15 , pp. 145-155
    • Garnier, A.1    Cote, J.2    Nadeau, I.3
  • 48
    • 0028986509 scopus 로고
    • A prime-boost approach to HIV preventive vaccine using a recombinant canarypox virus expressing glycoprotein 160 (MN) followed by a recombinant glycoprotein 160 (MN/LAI)
    • Pialoux G, Excler JL, Riviere Y et al. A prime-boost approach to HIV preventive vaccine using a recombinant canarypox virus expressing glycoprotein 160 (MN) followed by a recombinant glycoprotein 160 (MN/LAI). AIDS Res. Hum. Retroviruses 11, 373-381 (1995).
    • (1995) AIDS Res. Hum. Retroviruses , vol.11 , pp. 373-381
    • Pialoux, G.1    Excler, J.L.2    Riviere, Y.3
  • 49
    • 0026753413 scopus 로고
    • High level expression of active human prothrombin in a vaccinia virus expression system
    • Falkner FG, Turecek PL, MacGillivray RT et al. High level expression of active human prothrombin in a vaccinia virus expression system. Thromb. Haemost. 68, 119-124 (1992).
    • (1992) Thromb. Haemost , vol.68 , pp. 119-124
    • Falkner, F.G.1    Turecek, P.L.2    MacGillivray, R.T.3
  • 50
    • 14744304517 scopus 로고
    • A new generation of animal cell expression vectors based on the Semliki Forest virus replicon
    • Liljestrom P, Garoff H. A new generation of animal cell expression vectors based on the Semliki Forest virus replicon. Biotechnology (NY) 9, 1356-1361 (1991).
    • (1991) Biotechnology (NY) , vol.9 , pp. 1356-1361
    • Liljestrom, P.1    Garoff, H.2
  • 51
    • 0037450521 scopus 로고    scopus 로고
    • Semliki Forest virus vectors for rapid and high-level expression of integral membrane proteins
    • Lundstrom K. Semliki Forest virus vectors for rapid and high-level expression of integral membrane proteins. Biochim. Biophys. Acta 1610, 90-96 (2003).
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 90-96
    • Lundstrom, K.1
  • 52
    • 31044446490 scopus 로고    scopus 로고
    • Semliki Forest virus vectors for overexpression of 101 G protein-coupled receptors in mammalian host cells
    • Hassaine G, Wagner R, Kempf J et al. Semliki Forest virus vectors for overexpression of 101 G protein-coupled receptors in mammalian host cells. Protein Expr. Purif. 45, 343-351 (2006).
    • (2006) Protein Expr. Purif , vol.45 , pp. 343-351
    • Hassaine, G.1    Wagner, R.2    Kempf, J.3
  • 53
    • 0037264224 scopus 로고    scopus 로고
    • Semliki Forest virus vectors for large-scale production of recombinant proteins
    • Lundstrom K. Semliki Forest virus vectors for large-scale production of recombinant proteins. Methods Mol. Med. 76, 525-543 (2003).
    • (2003) Methods Mol. Med , vol.76 , pp. 525-543
    • Lundstrom, K.1
  • 54
    • 26444612689 scopus 로고    scopus 로고
    • Large-scale transient transfection of mammalian cells: A newly emerging attractive option for recombinant protein production
    • Geisse S, Henke M. Large-scale transient transfection of mammalian cells: a newly emerging attractive option for recombinant protein production. J. Struct. Funct. Genomics 6, 165-170 (2005).
    • (2005) J. Struct. Funct. Genomics , vol.6 , pp. 165-170
    • Geisse, S.1    Henke, M.2
  • 55
    • 33646066296 scopus 로고    scopus 로고
    • The cold-shock response in cultured mammalian cells: Harnessing the response for the improvement of recombinant protein production
    • Al-Fageeh MB, Marchant RJ, Carden MJ, Smales CM. The cold-shock response in cultured mammalian cells: harnessing the response for the improvement of recombinant protein production. Biotechnol. Bioeng. 93, 829-835 (2006).
    • (2006) Biotechnol. Bioeng , vol.93 , pp. 829-835
    • Al-Fageeh, M.B.1    Marchant, R.J.2    Carden, M.J.3    Smales, C.M.4
  • 56
    • 0038496837 scopus 로고    scopus 로고
    • Gene expression analysis of murine cells producing amphotropic mouse leukaemia virus at a cultivation temperature of 32 and 37 degrees C
    • Beer C, Buhr P, Hahn H et al. Gene expression analysis of murine cells producing amphotropic mouse leukaemia virus at a cultivation temperature of 32 and 37 degrees C. J. Gen. Virol. 84, 1677-1686 (2003).
    • (2003) J. Gen. Virol , vol.84 , pp. 1677-1686
    • Beer, C.1    Buhr, P.2    Hahn, H.3
  • 57
    • 25644455246 scopus 로고    scopus 로고
    • Ivanova L, Brandli J, Saudan P, Bachmann MF. Hybrid Sindbis/Epstein-Barr virus episomal expression vector for inducible production of proteins. Biotechniques 39, 209-212 (2005). •• Development of a cold-inducible mammalian expression vector - exciting!
    • Ivanova L, Brandli J, Saudan P, Bachmann MF. Hybrid Sindbis/Epstein-Barr virus episomal expression vector for inducible production of proteins. Biotechniques 39, 209-212 (2005). •• Development of a cold-inducible mammalian expression vector - exciting!
  • 58
    • 0032923295 scopus 로고    scopus 로고
    • Cell-free production and stable-isotope labeling of milligram quantities of proteins
    • Kigawa T, Yabuki T, Yoshida Y et al. Cell-free production and stable-isotope labeling of milligram quantities of proteins. FEBS Lett. 442, 15-19 (1999).
    • (1999) FEBS Lett , vol.442 , pp. 15-19
    • Kigawa, T.1    Yabuki, T.2    Yoshida, Y.3
  • 59
    • 0037305599 scopus 로고    scopus 로고
    • Protein expression systems for structural genomics and proteomics
    • Yokoyama S. Protein expression systems for structural genomics and proteomics. Curr. Opin. Chem. Biol. 7, 39-43 (2003).
    • (2003) Curr. Opin. Chem. Biol , vol.7 , pp. 39-43
    • Yokoyama, S.1
  • 61
    • 0037205759 scopus 로고    scopus 로고
    • NMR analysis of in vitro-synthesized proteins without purification: A high-throughput approach
    • Guignard L, Ozawa K, Pursglove SE et al. NMR analysis of in vitro-synthesized proteins without purification: a high-throughput approach. FEBS Lett. 524, 159-162 (2002).
    • (2002) FEBS Lett , vol.524 , pp. 159-162
    • Guignard, L.1    Ozawa, K.2    Pursglove, S.E.3
  • 62
    • 1242319564 scopus 로고    scopus 로고
    • In vitro synthesis of fully functional EmrE, a multidrug transporter, and study of its oligomeric state
    • Elbaz Y, Steiner-Mordoch S, Danieli T, Schuldiner S. In vitro synthesis of fully functional EmrE, a multidrug transporter, and study of its oligomeric state. Proc. Natl Acad. Sci. USA 101, 1519-1524 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 1519-1524
    • Elbaz, Y.1    Steiner-Mordoch, S.2    Danieli, T.3    Schuldiner, S.4
  • 63
    • 0025262173 scopus 로고
    • Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure
    • Hendrickson WA, Horton JR, LeMaster DM. Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structure. EMBO J. 9, 1665-1672 (1990).
    • (1990) EMBO J , vol.9 , pp. 1665-1672
    • Hendrickson, W.A.1    Horton, J.R.2    LeMaster, D.M.3
  • 65
    • 0034904102 scopus 로고    scopus 로고
    • Cell-free translation reconstituted with purified components
    • Shimizu Y, Inoue A, Tomari Y et al. Cell-free translation reconstituted with purified components. Nat. Biotechnol. 19, 751-755 (2001).
    • (2001) Nat. Biotechnol , vol.19 , pp. 751-755
    • Shimizu, Y.1    Inoue, A.2    Tomari, Y.3
  • 66
    • 0037332583 scopus 로고    scopus 로고
    • DiscernArray technology: A cell-free method for the generation of protein arrays from PCR DNA
    • He M, Taussig MJ. DiscernArray technology: a cell-free method for the generation of protein arrays from PCR DNA. J. Immunol. Methods 274, 265-270 (2003).
    • (2003) J. Immunol. Methods , vol.274 , pp. 265-270
    • He, M.1    Taussig, M.J.2
  • 67
    • 0037070555 scopus 로고    scopus 로고
    • Expression of Fab fragment of catalytic antibody 6D9 in an Escherichia coli in vitro coupled transcription/translation system
    • Jiang X, Ookubo Y, Fujii I et al. Expression of Fab fragment of catalytic antibody 6D9 in an Escherichia coli in vitro coupled transcription/translation system. FEBS Lett. 514, 290-294 (2002).
    • (2002) FEBS Lett , vol.514 , pp. 290-294
    • Jiang, X.1    Ookubo, Y.2    Fujii, I.3
  • 69
    • 17444399053 scopus 로고
    • In vitro transcription and translation protocols
    • Tymms MJ Ed, Humana Press, NJ, USA
    • Tymms MJ (Ed.) In vitro transcription and translation protocols. In: Methods in Molecular Biology. Vol. 37. Humana Press, NJ, USA (1995).
    • (1995) Methods in Molecular Biology , vol.37
  • 70
    • 3543116722 scopus 로고    scopus 로고
    • High-throughput, genome-scale protein production method based on the wheat germ cell-free expression system
    • Endo Y, Sawasaki T. High-throughput, genome-scale protein production method based on the wheat germ cell-free expression system. J. Struct. Funct. Genomics 5, 45-57 (2004).
    • (2004) J. Struct. Funct. Genomics , vol.5 , pp. 45-57
    • Endo, Y.1    Sawasaki, T.2
  • 71
    • 0035014494 scopus 로고    scopus 로고
    • Establishment and characterization of cell-free translation/glycosylation in insect cell (Spodoptera frugiperda 21) extract prepared with high pressure treatment
    • Tarui H, Murata M, Tani I et al. Establishment and characterization of cell-free translation/glycosylation in insect cell (Spodoptera frugiperda 21) extract prepared with high pressure treatment. Appl. Microbiol. Biotechnol. 55, 446-453 (2001).
    • (2001) Appl. Microbiol. Biotechnol , vol.55 , pp. 446-453
    • Tarui, H.1    Murata, M.2    Tani, I.3
  • 73
    • 1642434197 scopus 로고    scopus 로고
    • Mimicking posttranslational modifications of proteins
    • Davis BG. Biochemistry. Mimicking posttranslational modifications of proteins. Science 303, 480-482 (2004).
    • (2004) Science , vol.303 , pp. 480-482
    • Biochemistry, D.B.G.1
  • 74
    • 13944274948 scopus 로고    scopus 로고
    • Katzen F, Chang G, Kudlicki W. The past, present and future of cell-free protein synthesis. Trends Biotechnol. 23, 150-156 (2005). • Excellent overview of cell-free transcription/translation.
    • Katzen F, Chang G, Kudlicki W. The past, present and future of cell-free protein synthesis. Trends Biotechnol. 23, 150-156 (2005). • Excellent overview of cell-free transcription/translation.
  • 75
    • 20144387833 scopus 로고    scopus 로고
    • Robotic cloning and Protein Production Platform of the Northeast Structural Genomics Consortium
    • Acton TB, Gunsalus KC, Xiao R et al. Robotic cloning and Protein Production Platform of the Northeast Structural Genomics Consortium. Methods Enzymol. 394, 210-243 (2005).
    • (2005) Methods Enzymol , vol.394 , pp. 210-243
    • Acton, T.B.1    Gunsalus, K.C.2    Xiao, R.3
  • 76
    • 33846921695 scopus 로고    scopus 로고
    • Invitrogen Corp
    • Invitrogen Corp. www.invitrogen.com
  • 77
    • 33846919498 scopus 로고    scopus 로고
    • EMD Biosciences, Inc. www.emdbiosciences.com
    • EMD Biosciences, Inc. www.emdbiosciences.com


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.