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Volumn 112, Issue 5, 2015, Pages 867-878

A versatile coupled cell-free transcription-translation system based on tobacco BY-2 cell lysates

Author keywords

BY 2 cell lysate; Cell free protein synthesis; Coupled transcription translation; High throughput screening; Protein expression

Indexed keywords

BIOLOGICAL MEMBRANES; BIOSYNTHESIS; CELL MEMBRANES; CELLS; COVALENT BONDS; CYTOLOGY; GLUCOSE OXIDASE; GLUCOSE SENSORS; RECOMBINANT PROTEINS; THROUGHPUT; TOBACCO; TRANSCRIPTION;

EID: 84925598713     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.25502     Document Type: Article
Times cited : (62)

References (58)
  • 1
    • 84878892281 scopus 로고    scopus 로고
    • Cell-free co-production of an orthogonal transfer RNA activates efficient site-specific non-natural amino acid incorporation
    • Albayrak C, Swartz JR. 2013. Cell-free co-production of an orthogonal transfer RNA activates efficient site-specific non-natural amino acid incorporation. Nucleic Acids Res 41(11):5949-5963.
    • (2013) Nucleic Acids Res , vol.41 , Issue.11 , pp. 5949-5963
    • Albayrak, C.1    Swartz, J.R.2
  • 2
    • 0026606239 scopus 로고
    • Advances in the Synthesis of Oligonucleotides by the Phosphoramidite Approach
    • Beaucage SL, Iyer RP. 1992. Advances in the Synthesis of Oligonucleotides by the Phosphoramidite Approach. Tetrahedron 48(12):2223-2311.
    • (1992) Tetrahedron , vol.48 , Issue.12 , pp. 2223-2311
    • Beaucage, S.L.1    Iyer, R.P.2
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 84888046697 scopus 로고    scopus 로고
    • Cell-free protein expression based on extracts from CHO cells
    • Brodel AK, Sonnabend A, Kubick S. 2014. Cell-free protein expression based on extracts from CHO cells. Biotechnol Bioeng 111(1):25-36.
    • (2014) Biotechnol Bioeng , vol.111 , Issue.1 , pp. 25-36
    • Brodel, A.K.1    Sonnabend, A.2    Kubick, S.3
  • 5
    • 84900311214 scopus 로고    scopus 로고
    • Tobacco BY-2 cell-free lysate: An alternative and highly-productive plant-based in vitro translation system
    • Buntru M, Vogel S, Spiegel H, Schillberg S. 2014. Tobacco BY-2 cell-free lysate: An alternative and highly-productive plant-based in vitro translation system. BMC Biotechnol 14:37.
    • (2014) BMC Biotechnol , vol.14 , pp. 37
    • Buntru, M.1    Vogel, S.2    Spiegel, H.3    Schillberg, S.4
  • 6
    • 84864953230 scopus 로고    scopus 로고
    • Cell-free protein synthesis: Applications come of age
    • Carlson ED, Gan R, Hodgman CE, Jewett MC. 2012. Cell-free protein synthesis: Applications come of age. Biotechnol Adv 30(5):1185-1194.
    • (2012) Biotechnol Adv , vol.30 , Issue.5 , pp. 1185-1194
    • Carlson, E.D.1    Gan, R.2    Hodgman, C.E.3    Jewett, M.C.4
  • 8
    • 84894033400 scopus 로고    scopus 로고
    • Synthesis of 2.3mg/ml of protein with an all Escherichia coli cell-free transcription-translation system
    • Caschera F, Noireaux V. 2014. Synthesis of 2.3mg/ml of protein with an all Escherichia coli cell-free transcription-translation system. Biochimie 99:162-168.
    • (2014) Biochimie , vol.99 , pp. 162-168
    • Caschera, F.1    Noireaux, V.2
  • 9
    • 25144498144 scopus 로고    scopus 로고
    • De novo folding of GFP fusion proteins: High efficiency in eukaryotes but not in bacteria
    • Chang HC, Kaiser CM, Hartl FU, Barral JM. 2005. De novo folding of GFP fusion proteins: High efficiency in eukaryotes but not in bacteria. J Mol Biol 353(2):397-409.
    • (2005) J Mol Biol , vol.353 , Issue.2 , pp. 397-409
    • Chang, H.C.1    Kaiser, C.M.2    Hartl, F.U.3    Barral, J.M.4
  • 11
    • 0033472598 scopus 로고    scopus 로고
    • One-factor-at-a-time versus designed experiments
    • Czitrom V. 1999. One-factor-at-a-time versus designed experiments. Am Statist 53(2):126-131.
    • (1999) Am Statist , vol.53 , Issue.2 , pp. 126-131
    • Czitrom, V.1
  • 12
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • Ellgaard L, Helenius A. 2003. Quality control in the endoplasmic reticulum. Nat Rev Mol Cell Biol 4(3):181-191.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , Issue.3 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2
  • 13
    • 33748366035 scopus 로고    scopus 로고
    • Effects of E. coli chaperones on the solubility of human receptors in an in vitro expression system
    • Endo S, Tomimoto Y, Shimizu H, Taniguchi Y, Onizuka T. 2006. Effects of E. coli chaperones on the solubility of human receptors in an in vitro expression system. Mol Biotechnol 33(3):199-209.
    • (2006) Mol Biotechnol , vol.33 , Issue.3 , pp. 199-209
    • Endo, S.1    Tomimoto, Y.2    Shimizu, H.3    Taniguchi, Y.4    Onizuka, T.5
  • 15
    • 0033213605 scopus 로고    scopus 로고
    • Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum
    • Frand AR, Kaiser CA. 1999. Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum. Mol Cell 4(4):469-477.
    • (1999) Mol Cell , vol.4 , Issue.4 , pp. 469-477
    • Frand, A.R.1    Kaiser, C.A.2
  • 16
    • 84899749136 scopus 로고    scopus 로고
    • A combined cell-free transcription-translation system from Saccharomyces cerevisiae for rapid and robust protein synthe
    • Gan R, Jewett MC. 2014. A combined cell-free transcription-translation system from Saccharomyces cerevisiae for rapid and robust protein synthe. Biotechnol J 9(5):641-651.
    • (2014) Biotechnol J , vol.9 , Issue.5 , pp. 641-651
    • Gan, R.1    Jewett, M.C.2
  • 17
    • 67649886956 scopus 로고    scopus 로고
    • Replication of Tomato bushy stunt virus RNA in a plant in vitro system
    • Gursinsky T, Schulz B, Behrens SE. 2009. Replication of Tomato bushy stunt virus RNA in a plant in vitro system. Virology 390(2):250-260.
    • (2009) Virology , vol.390 , Issue.2 , pp. 250-260
    • Gursinsky, T.1    Schulz, B.2    Behrens, S.E.3
  • 18
    • 84896415554 scopus 로고    scopus 로고
    • Optimized extract preparation methods and reaction conditions for improved yeast cell-free protein synthesis
    • Hodgman CE, Jewett MC. 2013. Optimized extract preparation methods and reaction conditions for improved yeast cell-free protein synthesis. Biotechnol Bioeng 110(10):2643-2654.
    • (2013) Biotechnol Bioeng , vol.110 , Issue.10 , pp. 2643-2654
    • Hodgman, C.E.1    Jewett, M.C.2
  • 19
    • 1542720448 scopus 로고    scopus 로고
    • Mimicking the Escherichia coli cytoplasmic environment activates long-lived and efficient cell-free protein synthesis
    • Jewett MC, Swartz JR. 2004. Mimicking the Escherichia coli cytoplasmic environment activates long-lived and efficient cell-free protein synthesis. Biotechnol Bioeng 86(1):19-26.
    • (2004) Biotechnol Bioeng , vol.86 , Issue.1 , pp. 19-26
    • Jewett, M.C.1    Swartz, J.R.2
  • 20
    • 0345256409 scopus 로고    scopus 로고
    • Efficient synthesis of a disulfide-containing protein through a batch cell-free system from wheat germ
    • Kawasaki T, Gouda MD, Sawasaki T, Takai K, Endo Y. 2003. Efficient synthesis of a disulfide-containing protein through a batch cell-free system from wheat germ. Eur J Biochem 270(23):4780-4786.
    • (2003) Eur J Biochem , vol.270 , Issue.23 , pp. 4780-4786
    • Kawasaki, T.1    Gouda, M.D.2    Sawasaki, T.3    Takai, K.4    Endo, Y.5
  • 21
    • 0942286940 scopus 로고    scopus 로고
    • Efficient production of a bioactive, multiple disulfide-bonded protein using modified extracts of Escherichia coli
    • Kim DM, Swartz JR. 2004. Efficient production of a bioactive, multiple disulfide-bonded protein using modified extracts of Escherichia coli. Biotechnol Bioeng 85(2):122-129.
    • (2004) Biotechnol Bioeng , vol.85 , Issue.2 , pp. 122-129
    • Kim, D.M.1    Swartz, J.R.2
  • 23
    • 1242274438 scopus 로고    scopus 로고
    • Replication of plant RNA virus genomes in a cell-free extract of evacuolated plant protoplasts
    • Komoda K, Naito S, Ishikawa M. 2004. Replication of plant RNA virus genomes in a cell-free extract of evacuolated plant protoplasts. Proc Natl Acad Sci U S A 101(7):1863-1873.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , Issue.7 , pp. 1863-1873
    • Komoda, K.1    Naito, S.2    Ishikawa, M.3
  • 24
    • 37749004225 scopus 로고    scopus 로고
    • Protein therapeutics: A summary and pharmacological classification
    • Leader B, Baca QJ, Golan DE. 2008. Protein therapeutics: A summary and pharmacological classification. Nat Rev Drug Discov 7(1):21-39.
    • (2008) Nat Rev Drug Discov , vol.7 , Issue.1 , pp. 21-39
    • Leader, B.1    Baca, Q.J.2    Golan, D.E.3
  • 26
    • 84866386252 scopus 로고    scopus 로고
    • Cell-free synthesis of functional and endotoxin-free antibody Fab fragments by translocation into microsomes
    • Merk H, Gless C, Maertens B, Gerrits M, Stiege W. 2012. Cell-free synthesis of functional and endotoxin-free antibody Fab fragments by translocation into microsomes. Biotechniques 53(3):153-1560.
    • (2012) Biotechniques , vol.53 , Issue.3 , pp. 153-1560
    • Merk, H.1    Gless, C.2    Maertens, B.3    Gerrits, M.4    Stiege, W.5
  • 27
    • 68449097384 scopus 로고    scopus 로고
    • Species-independent translational leaders facilitate cell-free expression
    • Mureev S, Kovtun O, Nguyen UT, Alexandrov K. 2009. Species-independent translational leaders facilitate cell-free expression. Nat Biotechnol 27(8):747-752.
    • (2009) Nat Biotechnol , vol.27 , Issue.8 , pp. 747-752
    • Mureev, S.1    Kovtun, O.2    Nguyen, U.T.3    Alexandrov, K.4
  • 28
    • 0015504251 scopus 로고
    • Subunit structure of glucose oxidase from Aspergillus niger
    • O'Malley JJ, Weaver JL. 1972. Subunit structure of glucose oxidase from Aspergillus niger. Biochemistry 11(19):3527-3532.
    • (1972) Biochemistry , vol.11 , Issue.19 , pp. 3527-3532
    • O'Malley, J.J.1    Weaver, J.L.2
  • 29
    • 33747199320 scopus 로고    scopus 로고
    • Providing an oxidizing environment for the cell-free expression of disulfide-containing proteins by exhausting the reducing activity of Escherichia coli S30 extract
    • Oh IS, Kim DM, Kim TW, Park CG, Choi CY. 2006. Providing an oxidizing environment for the cell-free expression of disulfide-containing proteins by exhausting the reducing activity of Escherichia coli S30 extract. Biotechnol Prog 22(4):1225-1228.
    • (2006) Biotechnol Prog , vol.22 , Issue.4 , pp. 1225-1228
    • Oh, I.S.1    Kim, D.M.2    Kim, T.W.3    Park, C.G.4    Choi, C.Y.5
  • 30
    • 24344470555 scopus 로고    scopus 로고
    • Cell-free protein synthesis in an autoinduction system for NMR studies of protein-protein interactions
    • Ozawa K, Jergic S, Crowther JA, Thompson PR, Wijffels G, Otting G, Dixon NA. 2005. Cell-free protein synthesis in an autoinduction system for NMR studies of protein-protein interactions. J Biomol NMR 32(3):235-241.
    • (2005) J Biomol NMR , vol.32 , Issue.3 , pp. 235-241
    • Ozawa, K.1    Jergic, S.2    Crowther, J.A.3    Thompson, P.R.4    Wijffels, G.5    Otting, G.6    Dixon, N.A.7
  • 32
    • 0037069324 scopus 로고    scopus 로고
    • A cell-free protein synthesis system for high-throughput proteomics
    • Sawasaki T, Ogasawara T, Morishita R, Endo Y. 2002. A cell-free protein synthesis system for high-throughput proteomics. Proc Natl Acad Sci U S A 99(23):14652-14657.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , Issue.23 , pp. 14652-14657
    • Sawasaki, T.1    Ogasawara, T.2    Morishita, R.3    Endo, Y.4
  • 33
    • 84899922092 scopus 로고    scopus 로고
    • Substrate replenishment and byproduct removal improve yeast cell-free protein synthesis
    • Schoborg JA, Hodgman CE, Anderson MJ, Jewett MC. 2014. Substrate replenishment and byproduct removal improve yeast cell-free protein synthesis. Biotechnol J 9(5):630-640.
    • (2014) Biotechnol J , vol.9 , Issue.5 , pp. 630-640
    • Schoborg, J.A.1    Hodgman, C.E.2    Anderson, M.J.3    Jewett, M.C.4
  • 34
    • 55749110716 scopus 로고    scopus 로고
    • Production of membrane proteins using cell-free expression systems
    • Schwarz D, Dotsch V, Bernhard F. 2008. Production of membrane proteins using cell-free expression systems. Proteomics 8(19):3933-3946.
    • (2008) Proteomics , vol.8 , Issue.19 , pp. 3933-3946
    • Schwarz, D.1    Dotsch, V.2    Bernhard, F.3
  • 35
    • 78649788244 scopus 로고    scopus 로고
    • Efficient cell-free expression with the endogenous E. Coli RNA polymerase and sigma factor 70
    • Shin J, Noireaux V. 2010. Efficient cell-free expression with the endogenous E. Coli RNA polymerase and sigma factor 70. J Biol Eng 4:8.
    • (2010) J Biol Eng , vol.4 , pp. 8
    • Shin, J.1    Noireaux, V.2
  • 37
    • 84900523489 scopus 로고    scopus 로고
    • A continuous-exchange cell-free protein synthesis system based on extracts from cultured insect cells
    • Stech M, Quast RB, Sachse R, Schulze C, Wustenhagen DA, Kubick S. 2014. A continuous-exchange cell-free protein synthesis system based on extracts from cultured insect cells. PLoS ONE 9(5):-e96635.
    • (2014) PLoS ONE , vol.9 , Issue.5
    • Stech, M.1    Quast, R.B.2    Sachse, R.3    Schulze, C.4    Wustenhagen, D.A.5    Kubick, S.6
  • 38
    • 0024296609 scopus 로고
    • Physicochemical properties of phosphorothioate oligodeoxynucleotides
    • Stein CA, Subasinghe C, Shinozuka K, Cohen JS. 1988. Physicochemical properties of phosphorothioate oligodeoxynucleotides. Nucleic Acids Res 16(8):3209-3221.
    • (1988) Nucleic Acids Res , vol.16 , Issue.8 , pp. 3209-3221
    • Stein, C.A.1    Subasinghe, C.2    Shinozuka, K.3    Cohen, J.S.4
  • 39
    • 0036902363 scopus 로고    scopus 로고
    • Modification of galactose oxidase to introduce glucose 6-oxidase activity
    • Sun L, Bulter T, Alcalde M, Petrounia IP, Arnold FH. 2002. Modification of galactose oxidase to introduce glucose 6-oxidase activity. Chembiochem 3(8):781-783.
    • (2002) Chembiochem , vol.3 , Issue.8 , pp. 781-783
    • Sun, L.1    Bulter, T.2    Alcalde, M.3    Petrounia, I.P.4    Arnold, F.H.5
  • 40
    • 84899918637 scopus 로고    scopus 로고
    • Linear DNA for rapid prototyping of synthetic biological circuits in an Escherichia coli based TX-TL cell-free system
    • Sun ZZ, Yeung E, Hayes CA, Noireaux V, Murray RM. 2014. Linear DNA for rapid prototyping of synthetic biological circuits in an Escherichia coli based TX-TL cell-free system. ACS Synth Biol 3(6):387-397.
    • (2014) ACS Synth Biol , vol.3 , Issue.6 , pp. 387-397
    • Sun, Z.Z.1    Yeung, E.2    Hayes, C.A.3    Noireaux, V.4    Murray, R.M.5
  • 41
    • 83255176666 scopus 로고    scopus 로고
    • Transforming Biochemical Engineering with Cell-Free Biology
    • Swartz JR. 2012. Transforming Biochemical Engineering with Cell-Free Biology. Aiche Journal 58(1):5-13.
    • (2012) Aiche Journal , vol.58 , Issue.1 , pp. 5-13
    • Swartz, J.R.1
  • 42
    • 0034711439 scopus 로고    scopus 로고
    • Biochemical basis of oxidative protein folding in the endoplasmic reticulum
    • Tu BP, Ho-Schleyer SC, Travers KJ, Weissman JS. 2000. Biochemical basis of oxidative protein folding in the endoplasmic reticulum. Science 290(5496):1571-1574.
    • (2000) Science , vol.290 , Issue.5496 , pp. 1571-1574
    • Tu, B.P.1    Ho-Schleyer, S.C.2    Travers, K.J.3    Weissman, J.S.4
  • 43
    • 0842266604 scopus 로고    scopus 로고
    • Oxidative protein folding in eukaryotes: mechanisms and consequences
    • Tu BP, Weissman JS. 2004. Oxidative protein folding in eukaryotes: mechanisms and consequences. J Cell Biol 164(3):341-346.
    • (2004) J Cell Biol , vol.164 , Issue.3 , pp. 341-346
    • Tu, B.P.1    Weissman, J.S.2
  • 44
    • 11944267365 scopus 로고
    • Antisense Oligonucleotides-A New Therapeutic Principle
    • Uhlmann E, Peyman A. 1990. Antisense Oligonucleotides-A New Therapeutic Principle. Chem Rev 90(4):543-584.
    • (1990) Chem Rev , vol.90 , Issue.4 , pp. 543-584
    • Uhlmann, E.1    Peyman, A.2
  • 45
    • 67349089548 scopus 로고    scopus 로고
    • Enhanced production of amidase from Rhodococcus erythropolis MTCC 1526 by medium optimisation using a statistical experimental design
    • Vaidya BK, Mutalik SR, Joshi RM, Nene SN, Kulkarni BD. 2009. Enhanced production of amidase from Rhodococcus erythropolis MTCC 1526 by medium optimisation using a statistical experimental design. J Ind Microbiol Biotechnol 36(5):671-678.
    • (2009) J Ind Microbiol Biotechnol , vol.36 , Issue.5 , pp. 671-678
    • Vaidya, B.K.1    Mutalik, S.R.2    Joshi, R.M.3    Nene, S.N.4    Kulkarni, B.D.5
  • 46
    • 0034896499 scopus 로고    scopus 로고
    • Unassembled Ig heavy chains do not cycle from BiP in vivo but require light chains to trigger their release
    • Vanhove M, Usherwood YK, Hendershot LM. 2001. Unassembled Ig heavy chains do not cycle from BiP in vivo but require light chains to trigger their release. Immunity 15(1):105-114.
    • (2001) Immunity , vol.15 , Issue.1 , pp. 105-114
    • Vanhove, M.1    Usherwood, Y.K.2    Hendershot, L.M.3
  • 47
    • 84877100737 scopus 로고    scopus 로고
    • Replacing amino acids in translation: Expanding chemical diversity with non-natural variants
    • White ER, Reed TM, Ma Z, Hartman MCT. 2013. Replacing amino acids in translation: Expanding chemical diversity with non-natural variants. Methods 60:70-74.
    • (2013) Methods , vol.60 , pp. 70-74
    • White, E.R.1    Reed, T.M.2    Ma, Z.3    Hartman, M.C.T.4
  • 48
    • 34250826547 scopus 로고    scopus 로고
    • Cell-free transcription/translation from PCR-amplified DNA for high-throughput NMR studies
    • Wu PS, Ozawa K, Lim SP, Vasudevan SG, Dixon NE, Otting G. 2007a. Cell-free transcription/translation from PCR-amplified DNA for high-throughput NMR studies. Angew Chem Int Ed Engl 46(18):3356-3358.
    • (2007) Angew Chem Int Ed Engl , vol.46 , Issue.18 , pp. 3356-3358
    • Wu, P.S.1    Ozawa, K.2    Lim, S.P.3    Vasudevan, S.G.4    Dixon, N.E.5    Otting, G.6
  • 49
    • 34548319457 scopus 로고    scopus 로고
    • Optimization of riboflavin production by recombinant Bacillus subtilis RH44 using statistical designs
    • Wu QL, Chen T, Gan Y, Chen X, Zhao XM. 2007b. Optimization of riboflavin production by recombinant Bacillus subtilis RH44 using statistical designs. Appl Microbiol Biotechnol 76(4):783-794.
    • (2007) Appl Microbiol Biotechnol , vol.76 , Issue.4 , pp. 783-794
    • Wu, Q.L.1    Chen, T.2    Gan, Y.3    Chen, X.4    Zhao, X.M.5
  • 50
    • 25444494737 scopus 로고    scopus 로고
    • High-level expression of soluble human beta-defensin-2 fused with green fluorescent protein in Escherichia coli cell-free system
    • Xu Z, Chen H, Yin X, Xu N, Cen P. 2005. High-level expression of soluble human beta-defensin-2 fused with green fluorescent protein in Escherichia coli cell-free system. Appl Biochem Biotechnol 127(1):53-62.
    • (2005) Appl Biochem Biotechnol , vol.127 , Issue.1 , pp. 53-62
    • Xu, Z.1    Chen, H.2    Yin, X.3    Xu, N.4    Cen, P.5
  • 53
    • 1542538048 scopus 로고    scopus 로고
    • Enhancing multiple disulfide bonded protein folding in a cell-free system
    • Yin G, Swartz JR. 2004. Enhancing multiple disulfide bonded protein folding in a cell-free system. Biotechnol Bioeng 86(2):188-195.
    • (2004) Biotechnol Bioeng , vol.86 , Issue.2 , pp. 188-195
    • Yin, G.1    Swartz, J.R.2
  • 54
    • 84555196325 scopus 로고    scopus 로고
    • Preparation and testing of E. coli S30 in vitro transcription translation extracts
    • Zawada JF. 2012. Preparation and testing of E. coli S30 in vitro transcription translation extracts. Methods Mol Biol 805:31-41.
    • (2012) Methods Mol Biol , vol.805 , pp. 31-41
    • Zawada, J.F.1
  • 55
    • 79956158054 scopus 로고    scopus 로고
    • Microscale to manufacturing scale-up of cell-free cytokine production-a new approach for shortening protein production development timelines
    • Zawada JF, Yin G, Steiner AR, Yang J, Naresh A, Roy SM, Gold DS, Heinsohn HG, Murray CJ. 2011. Microscale to manufacturing scale-up of cell-free cytokine production-a new approach for shortening protein production development timelines. Biotechnol Bioeng 108(7):1570-1580.
    • (2011) Biotechnol Bioeng , vol.108 , Issue.7 , pp. 1570-1580
    • Zawada, J.F.1    Yin, G.2    Steiner, A.R.3    Yang, J.4    Naresh, A.5    Roy, S.M.6    Gold, D.S.7    Heinsohn, H.G.8    Murray, C.J.9
  • 56
    • 33645996396 scopus 로고    scopus 로고
    • Protein folding in the endoplasmic reticulum and the unfolded protein response
    • Zhang K, Kaufman RJ. 2006. Protein folding in the endoplasmic reticulum and the unfolded protein response. Handb Exp Pharmacol 172: 69-91.
    • (2006) Handb Exp Pharmacol , vol.172 , pp. 69-91
    • Zhang, K.1    Kaufman, R.J.2
  • 57
    • 77952835458 scopus 로고    scopus 로고
    • Optimization of phenazine-1-carboxylic acid production by a gacA/qscR-inactivated Pseudomonas sp M18GQ harboring pME6032Phz using response surface methodology
    • Zhou Q, Su JJ, Jiang HX, Huang XQ, Xu YQ. 2010. Optimization of phenazine-1-carboxylic acid production by a gacA/qscR-inactivated Pseudomonas sp M18GQ harboring pME6032Phz using response surface methodology. Applied Microbiology and Biotechnology 86(6):1761-1773.
    • (2010) Applied Microbiology and Biotechnology , vol.86 , Issue.6 , pp. 1761-1773
    • Zhou, Q.1    Su, J.J.2    Jiang, H.X.3    Huang, X.Q.4    Xu, Y.Q.5
  • 58
    • 33645864661 scopus 로고    scopus 로고
    • Making glucose oxidase fit for biofuel cell applications by directed protein evolution
    • Zhu Z, Momeu C, Zakhartsev M, Schwaneberg U. 2006. Making glucose oxidase fit for biofuel cell applications by directed protein evolution. Biosens Bioelectron 21(11):2046-2051.
    • (2006) Biosens Bioelectron , vol.21 , Issue.11 , pp. 2046-2051
    • Zhu, Z.1    Momeu, C.2    Zakhartsev, M.3    Schwaneberg, U.4


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