메뉴 건너뛰기




Volumn 26, Issue 6, 2010, Pages 1590-1596

Miniaturized fluid array for high-throughput protein expression

Author keywords

Drug screening; Microarray; Microfluidics; Protein expression; Proteomics

Indexed keywords

ANALYSIS TIME; CELL FREE PROTEIN SYNTHESIS; CURRENT PRACTICES; DRUG COMPOUNDS; DRUG SCREENING; E. COLI; GALACTOSIDASES; GENE DISCOVERY; GLUCORONIDASE; HIGH-THROUGHPUT; HIGH-THROUGHPUT METHOD; INHIBITORY EFFECT; LACTAMASES; MICROPLATES; ORDERS OF MAGNITUDE; PROTEIN EXPRESSIONS; PROTEOMICS; REAGENT CONSUMPTION; RECOMBINANT PROTEIN;

EID: 78650198220     PISSN: 87567938     EISSN: 15206033     Source Type: Journal    
DOI: 10.1002/btpr.474     Document Type: Article
Times cited : (17)

References (36)
  • 1
    • 0036468948 scopus 로고    scopus 로고
    • Accelerating code to function: sizing up the protein production line
    • Gilbert M, Albala JS. Accelerating code to function: sizing up the protein production line. Curr Opin Chemi Biol. 2002; 6: 102-105.
    • (2002) Curr Opin Chemi Biol , vol.6 , pp. 102-105
    • Gilbert, M.1    Albala, J.S.2
  • 2
    • 0034677966 scopus 로고    scopus 로고
    • Drug discovery: a historical perspective
    • Drews J. Drug discovery: a historical perspective. Science. 2000; 287: 1960-1964.
    • (2000) Science , vol.287 , pp. 1960-1964
    • Drews, J.1
  • 4
    • 0024297305 scopus 로고
    • A continuous cell-free translation system capable of producing polypeptides in high yield
    • Spirin AS, Baranov VI, Ryabova LA, Ovodov SY, Alakhov YB. A continuous cell-free translation system capable of producing polypeptides in high yield. Science. 1988; 242: 1162-1164.
    • (1988) Science , vol.242 , pp. 1162-1164
    • Spirin, A.S.1    Baranov, V.I.2    Ryabova, L.A.3    Ovodov, S.Y.4    Alakhov, Y.B.5
  • 5
    • 13944274948 scopus 로고    scopus 로고
    • The past, present and future of cell-free protein synthesis
    • Katzen F, Chang G, Kudlicki W. The past, present and future of cell-free protein synthesis. Trends Biotechnol. 2005; 23: 150-156.
    • (2005) Trends Biotechnol , vol.23 , pp. 150-156
    • Katzen, F.1    Chang, G.2    Kudlicki, W.3
  • 6
    • 0031921676 scopus 로고    scopus 로고
    • E. coli-based in vitro transcription/translation: in vivo-specific synthesis rates and high yields in a batch system
    • Patnaik R, Swartz JR. E. coli-based in vitro transcription/translation: in vivo-specific synthesis rates and high yields in a batch system. Biotechniques. 1998; 24: 862-868.
    • (1998) Biotechniques , vol.24 , pp. 862-868
    • Patnaik, R.1    Swartz, J.R.2
  • 8
    • 68449097384 scopus 로고    scopus 로고
    • Species-independent translational leaders facilitate cell-free expression
    • Mureev S, Kovtun O, Nguyen UT, Alexandrov K. Species-independent translational leaders facilitate cell-free expression. Nat Biotechnol. 2009; 27: 747-752.
    • (2009) Nat Biotechnol , vol.27 , pp. 747-752
    • Mureev, S.1    Kovtun, O.2    Nguyen, U.T.3    Alexandrov, K.4
  • 10
    • 0035430843 scopus 로고    scopus 로고
    • Single step generation of protein arrays from DNA by cell-free expression and in situ immobilisation (PISA method)
    • He M, Taussig MJ. Single step generation of protein arrays from DNA by cell-free expression and in situ immobilisation (PISA method). Nucleic Acids Res. 2001; 29: E73-E73.
    • (2001) Nucleic Acids Res. , vol.29
    • He, M.1    Taussig, M.J.2
  • 11
    • 11144247743 scopus 로고    scopus 로고
    • Accurate multiplex gene synthesis from programmable DNA microchips
    • Tian J, Gong H, Sheng N, Zhou X, Gulari E, Gao, X, Church, G. Accurate multiplex gene synthesis from programmable DNA microchips. Nature. 2004; 432: 1050-1054.
    • (2004) Nature , vol.432 , pp. 1050-1054
    • Tian, J.1    Gong, H.2    Sheng, N.3    Zhou, X.4    Gulari, E.5    Gao, X.6    Church, G.7
  • 12
    • 33749863636 scopus 로고    scopus 로고
    • Protein chip fabrication by capture of nascent polypeptides
    • Tao SC, Zhu H. Protein chip fabrication by capture of nascent polypeptides. Nat Biotechnol. 2006; 24: 1253-1254.
    • (2006) Nat Biotechnol , vol.24 , pp. 1253-1254
    • Tao, S.C.1    Zhu, H.2
  • 13
    • 33748289981 scopus 로고    scopus 로고
    • Wheat germ cell-free platform for eukaryotic protein production
    • Vinarov DA, Loushin Newman CL, Markley JL. Wheat germ cell-free platform for eukaryotic protein production. Febs J. 2006; 273: 4160-4169.
    • (2006) Febs J , vol.273 , pp. 4160-4169
    • Vinarov, D.A.1    Loushin Newman, C.L.2    Markley, J.L.3
  • 14
    • 33745196264 scopus 로고    scopus 로고
    • Rapid production of milligram quantities of proteins in a batch cell-free protein synthesis system
    • Kim TW, Kim DM, Choi CY. Rapid production of milligram quantities of proteins in a batch cell-free protein synthesis system. J Biotechnol. 2006; 124: 373-380.
    • (2006) J Biotechnol , vol.124 , pp. 373-380
    • Kim, T.W.1    Kim, D.M.2    Choi, C.Y.3
  • 15
    • 36048940106 scopus 로고    scopus 로고
    • A sequential expression system for high-throughput functional genomic analysis
    • Woodrow KA, Swartz JR. A sequential expression system for high-throughput functional genomic analysis. Proteomics. 2007; 7: 3870-3879.
    • (2007) Proteomics , vol.7 , pp. 3870-3879
    • Woodrow, K.A.1    Swartz, J.R.2
  • 16
    • 33845454189 scopus 로고    scopus 로고
    • Rapid expression of functional genomic libraries
    • Woodrow KA, Airen IO, Swartz JR. Rapid expression of functional genomic libraries. J Proteome Res. 2006; 5: 3288-3300.
    • (2006) J Proteome Res , vol.5 , pp. 3288-3300
    • Woodrow, K.A.1    Airen, I.O.2    Swartz, J.R.3
  • 18
    • 24644512785 scopus 로고    scopus 로고
    • Toxin detection by a miniaturized in vitro protein expression array
    • Mei Q, Fredrickson CK, Jin S, Fan ZH. Toxin detection by a miniaturized in vitro protein expression array. Anal Chem. 2005; 77: 5494-5500.
    • (2005) Anal Chem , vol.77 , pp. 5494-5500
    • Mei, Q.1    Fredrickson, C.K.2    Jin, S.3    Fan, Z.H.4
  • 19
    • 0141886248 scopus 로고    scopus 로고
    • PDMS-glass hybrid microreactor array with embedded temperature control device. Application to cell-free protein synthesis
    • Yamamoto T, Fujii T, Nojima T. PDMS-glass hybrid microreactor array with embedded temperature control device. Application to cell-free protein synthesis. Lab Chip. 2002; 2: 197-202.
    • (2002) Lab Chip , vol.2 , pp. 197-202
    • Yamamoto, T.1    Fujii, T.2    Nojima, T.3
  • 20
  • 21
    • 64649102767 scopus 로고    scopus 로고
    • Facile single step fabrication of microchannels with varying size
    • Asthana A, Kim KO, Perumal J, Kim DM, Kim DP. Facile single step fabrication of microchannels with varying size. Lab Chip. 2009; 9: 1138-1142.
    • (2009) Lab Chip , vol.9 , pp. 1138-1142
    • Asthana, A.1    Kim, K.O.2    Perumal, J.3    Kim, D.M.4    Kim, D.P.5
  • 23
    • 33751232976 scopus 로고    scopus 로고
    • Ricin detection by biological signal amplification in a well-in-a-well device
    • Mei Q, Fredrickson CK, Lian W, Jin S, Fan ZH. Ricin detection by biological signal amplification in a well-in-a-well device. Anal Chem. 2006; 78: 7659-7664.
    • (2006) Anal Chem , vol.78 , pp. 7659-7664
    • Mei, Q.1    Fredrickson, C.K.2    Lian, W.3    Jin, S.4    Fan, Z.H.5
  • 24
    • 57449092083 scopus 로고    scopus 로고
    • Cell-free protein expression in a microchannel array with passive pumping
    • Khnouf R, Beebe DJ, Fan ZH. Cell-free protein expression in a microchannel array with passive pumping. Lab Chip. 2009; 9: 56-61.
    • (2009) Lab Chip , vol.9 , pp. 56-61
    • Khnouf, R.1    Beebe, D.J.2    Fan, Z.H.3
  • 25
    • 34248182605 scopus 로고    scopus 로고
    • Leakage-free bonding of porous membranes into layered microfluidic array systems
    • Chueh BH, Huh D, Kyrtsos CR, Houssin T, Futai N, Takayama, S. Leakage-free bonding of porous membranes into layered microfluidic array systems. Anal Chem. 2007; 79: 3504-3508.
    • (2007) Anal Chem , vol.79 , pp. 3504-3508
    • Chueh, B.H.1    Huh, D.2    Kyrtsos, C.R.3    Houssin, T.4    Futai, N.5    Takayama, S.6
  • 26
    • 0037302828 scopus 로고    scopus 로고
    • Rapid translation system (RTS): a promising alternative for recombinant protein production
    • Betton JM. Rapid translation system (RTS): a promising alternative for recombinant protein production. Curr Protein Pept Sci. 2003; 4: 73-80.
    • (2003) Curr Protein Pept Sci , vol.4 , pp. 73-80
    • Betton, J.M.1
  • 27
    • 0035051181 scopus 로고    scopus 로고
    • Reliable quantification of in vitro synthesized green fluorescent protein: comparison of fluorescence activity and total protein levels
    • Nemetz C, Reichhuber R, Schweizer R, Hloch P, Watzele M. Reliable quantification of in vitro synthesized green fluorescent protein: comparison of fluorescence activity and total protein levels. Electrophoresis. 2001; 22: 966-969.
    • (2001) Electrophoresis , vol.22 , pp. 966-969
    • Nemetz, C.1    Reichhuber, R.2    Schweizer, R.3    Hloch, P.4    Watzele, M.5
  • 28
    • 4644301876 scopus 로고    scopus 로고
    • Resistance to beta-lactam antibiotics
    • Poole K. Resistance to beta-lactam antibiotics. Cell Mol Life Sci. 2004; 61: 2200-2223.
    • (2004) Cell Mol Life Sci , vol.61 , pp. 2200-2223
    • Poole, K.1
  • 29
    • 0031747315 scopus 로고    scopus 로고
    • Beta-lactamase-mediated resistance and opportunities for its control
    • Livermore DM. Beta-lactamase-mediated resistance and opportunities for its control. J Antimicrob Chemother. 1998; 41 Suppl D: 25-41.
    • (1998) J Antimicrob Chemother , vol.41 , Issue.SUPPL. D , pp. 25-41
    • Livermore, D.M.1
  • 30
    • 0028219728 scopus 로고
    • Comparative activities of clavulanic acid, sulbactam, and tazobactam against clinically important beta-lactamases
    • Payne DJ, Cramp R, Winstanley DJ, Knowles DJ. Comparative activities of clavulanic acid, sulbactam, and tazobactam against clinically important beta-lactamases. Antimicrob Agents Chemother. 1994; 38: 767-772.
    • (1994) Antimicrob Agents Chemother , vol.38 , pp. 767-772
    • Payne, D.J.1    Cramp, R.2    Winstanley, D.J.3    Knowles, D.J.4
  • 31
    • 0343185958 scopus 로고    scopus 로고
    • Cloning, nucleotide sequencing, and analysis of the gene encoding an AmpC beta-lactamase in Acinetobacter baumannii
    • Bou G, Martinez-Beltran J. Cloning, nucleotide sequencing, and analysis of the gene encoding an AmpC beta-lactamase in Acinetobacter baumannii. Antimicrob Agents Chemother. 2000; 44: 428-432.
    • (2000) Antimicrob Agents Chemother , vol.44 , pp. 428-432
    • Bou, G.1    Martinez-Beltran, J.2
  • 34
    • 67651245201 scopus 로고    scopus 로고
    • Protein arrays as tools for serum autoantibody marker discovery in cancer
    • Kijanka G, Murphy D. Protein arrays as tools for serum autoantibody marker discovery in cancer. J Proteomics. 2009; 72: 936-944.
    • (2009) J Proteomics , vol.72 , pp. 936-944
    • Kijanka, G.1    Murphy, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.