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Volumn 280, Issue 13, 2013, Pages 2979-2996

Reporter-based screening and selection of enzymes

Author keywords

enzyme; high throughput; in vivo; library; post translational modification; reporter; riboswitch; screening; selection; transcriptional regulator

Indexed keywords

ANTIBIOTIC AGENT; REGULATOR PROTEIN; RIBOZYME;

EID: 84879223038     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.12281     Document Type: Conference Paper
Times cited : (54)

References (77)
  • 1
    • 0035843170 scopus 로고    scopus 로고
    • Industrial biocatalysis today and tomorrow
    • DOI 10.1038/35051736
    • Schmid A, Dordick JS, Hauer B, Kiener A, Wubbolts M, &, Witholt B, (2001) Industrial biocatalysis today and tomorrow. Nature 409, 258-268. (Pubitemid 32144296)
    • (2001) Nature , vol.409 , Issue.6817 , pp. 258-268
    • Schmid, A.1    Dordick, J.S.2    Hauer, B.3    Kiener, A.4    Wubbolts, M.5    Witholt, B.6
  • 2
    • 79251494754 scopus 로고    scopus 로고
    • Enzymes and bioconversions of industrial, pharmaceutical, and biotechnological significance
    • Sanchez S, &, Demain AL, (2011) Enzymes and bioconversions of industrial, pharmaceutical, and biotechnological significance. Org Process Res Dev 15, 224-230.
    • (2011) Org Process Res Dev , vol.15 , pp. 224-230
    • Sanchez, S.1    Demain, A.L.2
  • 3
    • 68049085915 scopus 로고    scopus 로고
    • Directed evolution of enzymes: Library screening strategies
    • Leemhuis H, Kelly RM, &, Dijkhuizen L, (2009) Directed evolution of enzymes: library screening strategies. IUBMB Life 61, 222-228.
    • (2009) IUBMB Life , vol.61 , pp. 222-228
    • Leemhuis, H.1    Kelly, R.M.2    Dijkhuizen, L.3
  • 4
    • 83655197793 scopus 로고    scopus 로고
    • Strategies for discovery and improvement of enzyme function: State of the art and opportunities
    • Kaul P, &, Asano Y, (2012) Strategies for discovery and improvement of enzyme function: state of the art and opportunities. Microb Biotechnol 5, 18-33.
    • (2012) Microb Biotechnol , vol.5 , pp. 18-33
    • Kaul, P.1    Asano, Y.2
  • 5
    • 84862699285 scopus 로고    scopus 로고
    • Nature versus nurture: Developing enzymes that function under extreme conditions
    • Liszka MJ, Clark ME, Schneider E, &, Clark DS, (2012) Nature versus nurture: developing enzymes that function under extreme conditions. Annu Rev Chem Biomol Eng 3, 77-102.
    • (2012) Annu Rev Chem Biomol Eng , vol.3 , pp. 77-102
    • Liszka, M.J.1    Clark, M.E.2    Schneider, E.3    Clark, D.S.4
  • 9
    • 80052794803 scopus 로고    scopus 로고
    • Functional metagenomic strategies for the discovery of novel enzymes and biosurfactants with biotechnological applications from marine ecosystems
    • Kennedy J, O'Leary ND, Kiran GS, Morrissey JP, O'Gara F, Selvin J, &, Dobson ADW, (2011) Functional metagenomic strategies for the discovery of novel enzymes and biosurfactants with biotechnological applications from marine ecosystems. J Appl Microbiol 111, 787-799.
    • (2011) J Appl Microbiol , vol.111 , pp. 787-799
    • Kennedy, J.1    O'Leary, N.D.2    Kiran, G.S.3    Morrissey, J.P.4    O'Gara, F.5    Selvin, J.6    Dobson, A.D.W.7
  • 10
    • 70449727646 scopus 로고    scopus 로고
    • Functional metagenomics for enzyme discovery: Challenges to efficient screening
    • Uchiyama T, &, Miyazaki K, (2009) Functional metagenomics for enzyme discovery: challenges to efficient screening. Curr Opin Biotechnol 20, 616-622.
    • (2009) Curr Opin Biotechnol , vol.20 , pp. 616-622
    • Uchiyama, T.1    Miyazaki, K.2
  • 13
    • 34247374701 scopus 로고    scopus 로고
    • Selection strategies for improved biocatalysts
    • DOI 10.1111/j.1742-4658.2007.05782.x
    • Boersma YL, Dröge MJ, &, Quax WJ, (2007) Selection strategies for improved biocatalysts. FEBS J 274, 2181-2195. (Pubitemid 46633470)
    • (2007) FEBS Journal , vol.274 , Issue.9 , pp. 2181-2195
    • Boersma, Y.L.1    Droge, M.J.2    Quax, W.J.3
  • 14
    • 84865306330 scopus 로고    scopus 로고
    • Directed enzyme evolution: Beyond the low-hanging fruit
    • Goldsmith M, &, Tawfik DS, (2012) Directed enzyme evolution: beyond the low-hanging fruit. Curr Opin Struct Biol 22, 406-412.
    • (2012) Curr Opin Struct Biol , vol.22 , pp. 406-412
    • Goldsmith, M.1    Tawfik, D.S.2
  • 16
    • 84873734989 scopus 로고    scopus 로고
    • A new screening method for the directed evolution of thermostable bacteriolytic enzymes
    • Heselpoth RD, &, Nelson DC, (2012) A new screening method for the directed evolution of thermostable bacteriolytic enzymes. J Vis Exp, 69, e4216.
    • (2012) J Vis Exp , vol.69
    • Heselpoth, R.D.1    Nelson, D.C.2
  • 17
    • 4143110558 scopus 로고    scopus 로고
    • Structural basis of selection and thermostability of laboratory evolved Bacillus subtilis lipase
    • DOI 10.1016/j.jmb.2004.06.059, PII S0022283604007636
    • Acharya P, Rajakumara E, Sankaranarayanan R, &, Rao NM, (2004) Structural basis of selection and thermostability of laboratory evolved Bacillus subtilis lipase. J Mol Biol 341, 1271-1281. (Pubitemid 39092314)
    • (2004) Journal of Molecular Biology , vol.341 , Issue.5 , pp. 1271-1281
    • Acharya, P.1    Rajakumara, E.2    Sankaranarayanan, R.3    Rao, N.M.4
  • 18
    • 84867777175 scopus 로고    scopus 로고
    • Computational protein engineering: Bridging the gap between rational design and laboratory evolution
    • Barrozo A, Borstnar R, Marloie G, &, Kamerlin SCL, (2012) Computational protein engineering: bridging the gap between rational design and laboratory evolution. Int J Mol Sci 13, 12428-12460.
    • (2012) Int J Mol Sci , vol.13 , pp. 12428-12460
    • Barrozo, A.1    Borstnar, R.2    Marloie, G.3    Kamerlin, S.C.L.4
  • 19
    • 77953642931 scopus 로고    scopus 로고
    • High-throughput metabolic engineering: Advances in small-molecule screening and selection
    • Dietrich JA, McKee AE, &, Keasling JD, (2010) High-throughput metabolic engineering: advances in small-molecule screening and selection. Annu Rev Biochem 79, 563-590.
    • (2010) Annu Rev Biochem , vol.79 , pp. 563-590
    • Dietrich, J.A.1    McKee, A.E.2    Keasling, J.D.3
  • 21
    • 84865405490 scopus 로고    scopus 로고
    • Comparison of designed and randomly generated catalysts for simple chemical reactions
    • Kipnis Y, &, Baker D, (2012) Comparison of designed and randomly generated catalysts for simple chemical reactions. Protein Sci 21, 1388-1395.
    • (2012) Protein Sci , vol.21 , pp. 1388-1395
    • Kipnis, Y.1    Baker, D.2
  • 22
    • 84876020987 scopus 로고    scopus 로고
    • Emerging themes in the computational design of novel enzymes and protein-protein interfaces
    • Khare SD, &, Fleishman SJ, (2012) Emerging themes in the computational design of novel enzymes and protein-protein interfaces. FEBS Lett 587, 1147-1154.
    • (2012) FEBS Lett , vol.587 , pp. 1147-1154
    • Khare, S.D.1    Fleishman, S.J.2
  • 24
    • 84862167101 scopus 로고    scopus 로고
    • High-throughput enzyme evolution in Saccharomyces cerevisiae using a synthetic RNA switch
    • Michener JK, &, Smolke CD, (2012) High-throughput enzyme evolution in Saccharomyces cerevisiae using a synthetic RNA switch. Metab Eng 14, 306-316.
    • (2012) Metab Eng , vol.14 , pp. 306-316
    • Michener, J.K.1    Smolke, C.D.2
  • 25
    • 84859245861 scopus 로고    scopus 로고
    • Protein and RNA engineering to customize microbial molecular reporting
    • Gredell JA, Frei CS, &, Cirino PC, (2012) Protein and RNA engineering to customize microbial molecular reporting. Biotechnol J 7, 477-499.
    • (2012) Biotechnol J , vol.7 , pp. 477-499
    • Gredell, J.A.1    Frei, C.S.2    Cirino, P.C.3
  • 26
    • 73149119826 scopus 로고    scopus 로고
    • Ultrahigh-throughput FACS-based screening for directed enzyme evolution
    • Yang G, &, Withers SG, (2009) Ultrahigh-throughput FACS-based screening for directed enzyme evolution. ChemBioChem 10, 2704-2715.
    • (2009) ChemBioChem , vol.10 , pp. 2704-2715
    • Yang, G.1    Withers, S.G.2
  • 27
    • 33744810604 scopus 로고    scopus 로고
    • Select the best: novel biocatalysts for industrial applications
    • DOI 10.1016/j.tibtech.2006.04.004, PII S0167779906001016
    • Konarzycka-Bessler M, &, Jaeger KE, (2006) Select the best: novel biocatalysts for industrial applications. Trends Biotechnol 24, 248-250. (Pubitemid 43831240)
    • (2006) Trends in Biotechnology , vol.24 , Issue.6 , pp. 248-250
    • Konarzycka-Bessler, M.1    Jaeger, K.-E.2
  • 28
    • 0036829913 scopus 로고    scopus 로고
    • Altering the substrate specificity of cephalosporin acylase by directed evolution of the β-subunit
    • DOI 10.1074/jbc.M208317200
    • Otten LG, Sio CF, Vrielink J, Cool RH, &, Quax WJ, (2002) Altering the substrate specificity of cephalosporin acylase by directed evolution of the β-subunit. J Biol Chem 277, 42121-42127. (Pubitemid 35257528)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.44 , pp. 42121-42127
    • Otten, L.G.1    Sio, C.F.2    Vrielink, J.3    Cool, R.H.4    Quax, W.J.5
  • 30
    • 79952117732 scopus 로고    scopus 로고
    • Screens for active and stereoselective hydrolytic enzymes
    • Böttcher D, Schmidt M, &, Bornscheuer UT, (2010) Screens for active and stereoselective hydrolytic enzymes. Methods Mol Biol 668, 169-176.
    • (2010) Methods Mol Biol , vol.668 , pp. 169-176
    • Böttcher, D.1    Schmidt, M.2    Bornscheuer, U.T.3
  • 31
    • 84864420613 scopus 로고    scopus 로고
    • Development of a high-throughput screening method for racemase activity and its application to the identification of alanine racemase variants with activity towards l -arginine
    • Willies SC, White JL, &, Turner NJ, (2012) Development of a high-throughput screening method for racemase activity and its application to the identification of alanine racemase variants with activity towards l -arginine. Tetrahedron 68, 7564-7567.
    • (2012) Tetrahedron , vol.68 , pp. 7564-7567
    • Willies, S.C.1    White, J.L.2    Turner, N.J.3
  • 33
    • 84862817365 scopus 로고    scopus 로고
    • Microplate-based active/inactive 1 degrees screen for biomass degrading enzyme library purification and gene discovery
    • Wagschal K, &, Lee CC, (2012) Microplate-based active/inactive 1 degrees screen for biomass degrading enzyme library purification and gene discovery. J Microbiol Methods 89, 83-85.
    • (2012) J Microbiol Methods , vol.89 , pp. 83-85
    • Wagschal, K.1    Lee, C.C.2
  • 34
    • 0033120651 scopus 로고    scopus 로고
    • Directed evolution of industrial enzymes
    • DOI 10.1016/S0167-7799(98)01283-9, PII S0167779998012839
    • Schmidt-Dannert C, &, Arnold FH, (1999) Directed evolution of industrial enzymes. Trends Biotechnol 17, 135-136. (Pubitemid 29273942)
    • (1999) Trends in Biotechnology , vol.17 , Issue.4 , pp. 135-136
    • Schmidt-Dannert, C.1    Arnold, F.H.2
  • 36
    • 84873985413 scopus 로고    scopus 로고
    • Flow cytometry-based ultra-high-throughput screening assay for cellulase activity
    • Ostafe R, Prodanovic R, Commandeur U, &, Fischer R, (2013) Flow cytometry-based ultra-high-throughput screening assay for cellulase activity. Anal Biochem 435, 93-98.
    • (2013) Anal Biochem , vol.435 , pp. 93-98
    • Ostafe, R.1    Prodanovic, R.2    Commandeur, U.3    Fischer, R.4
  • 37
    • 77955042704 scopus 로고    scopus 로고
    • Fluorescence activated cell sorting as a general ultra-high-throughput screening method for directed evolution of glycosyltransferases
    • Yang G, Rich JR, Gilbert M, Wakarchuk WW, Feng Y, &, Withers SG, (2010) Fluorescence activated cell sorting as a general ultra-high-throughput screening method for directed evolution of glycosyltransferases. J Am Chem Soc 132, 10570-10577.
    • (2010) J Am Chem Soc , vol.132 , pp. 10570-10577
    • Yang, G.1    Rich, J.R.2    Gilbert, M.3    Wakarchuk, W.W.4    Feng, Y.5    Withers, S.G.6
  • 38
    • 79751479307 scopus 로고    scopus 로고
    • Ultrahigh throughput screening system for directed glucose oxidase evolution in yeast cells
    • Prodanovic R, Ostafe R, Scacioc A, &, Schwaneberg U, (2011) Ultrahigh throughput screening system for directed glucose oxidase evolution in yeast cells. Comb Chem High Throughput Screen 14, 55-60.
    • (2011) Comb Chem High Throughput Screen , vol.14 , pp. 55-60
    • Prodanovic, R.1    Ostafe, R.2    Scacioc, A.3    Schwaneberg, U.4
  • 40
    • 84857050180 scopus 로고    scopus 로고
    • Applications of genetically-encoded biosensors for the construction and control of biosynthetic pathways
    • Michener JK, Thodey K, Liang JC, &, Smolke CD, (2012) Applications of genetically-encoded biosensors for the construction and control of biosynthetic pathways. Metab Eng 14, 212-222.
    • (2012) Metab Eng , vol.14 , pp. 212-222
    • Michener, J.K.1    Thodey, K.2    Liang, J.C.3    Smolke, C.D.4
  • 41
    • 84867331009 scopus 로고    scopus 로고
    • Bioluminescence based in vivo screening technologies
    • Kelkar M, &, De A, (2012) Bioluminescence based in vivo screening technologies. Curr Opin Pharmacol 12, 592-600.
    • (2012) Curr Opin Pharmacol , vol.12 , pp. 592-600
    • Kelkar, M.1    De, A.2
  • 42
    • 53149116351 scopus 로고    scopus 로고
    • Tracing explosives in soil with transcriptional regulators of Pseudomonas putida evolved for responding to nitrotoluenes
    • Garmendia J, de las Heras A, Galvão TC, &, de Lorenzo V, (2008) Tracing explosives in soil with transcriptional regulators of Pseudomonas putida evolved for responding to nitrotoluenes. Microb Biotechnol 1, 236-246.
    • (2008) Microb Biotechnol , vol.1 , pp. 236-246
    • Garmendia, J.1    De Las Heras, A.2    Galvão, T.C.3    De Lorenzo, V.4
  • 43
    • 84855895452 scopus 로고    scopus 로고
    • Engineering whole-cell biosensors with no antibiotic markers for monitoring aromatic compounds in the environment
    • de Las Heras A, &, de Lorenzo V, (2012) Engineering whole-cell biosensors with no antibiotic markers for monitoring aromatic compounds in the environment. Methods Mol Biol 834, 261-281.
    • (2012) Methods Mol Biol , vol.834 , pp. 261-281
    • De Las Heras, A.1    De Lorenzo, V.2
  • 44
    • 77952507419 scopus 로고    scopus 로고
    • Reprogramming bacteria to seek and destroy an herbicide
    • Sinha J, Reyes SJ, &, Gallivan JP, (2010) Reprogramming bacteria to seek and destroy an herbicide. Nat Chem Biol 6, 464-470.
    • (2010) Nat Chem Biol , vol.6 , pp. 464-470
    • Sinha, J.1    Reyes, S.J.2    Gallivan, J.P.3
  • 45
    • 45849125844 scopus 로고    scopus 로고
    • Mutant HbpR transcription activator isolation for 2-chlorobiphenyl via green fluorescent protein-based flow cytometry and cell sorting
    • Beggah S, Vogne C, Zenaro E, &, Van Der Meer JR, (2008) Mutant HbpR transcription activator isolation for 2-chlorobiphenyl via green fluorescent protein-based flow cytometry and cell sorting. Microb Biotechnol 1, 68-78.
    • (2008) Microb Biotechnol , vol.1 , pp. 68-78
    • Beggah, S.1    Vogne, C.2    Zenaro, E.3    Van Der Meer, J.R.4
  • 46
    • 19144369096 scopus 로고    scopus 로고
    • Substrate-induced gene-expression screening of environmental metagenome libraries for isolation of catabolic genes
    • DOI 10.1038/nbt1048
    • Uchiyama T, Abe T, Ikemura T, &, Watanabe K, (2005) Substrate-induced gene-expression screening of environmental metagenome libraries for isolation of catabolic genes. Nat Biotechnol 23, 88-93. (Pubitemid 41724630)
    • (2005) Nature Biotechnology , vol.23 , Issue.1 , pp. 88-93
    • Uchiyama, T.1    Abe, T.2    Ikemura, T.3    Watanabe, K.4
  • 47
    • 50249171225 scopus 로고    scopus 로고
    • Substrate-induced gene expression (SIGEX) screening of metagenome libraries
    • Uchiyama T, &, Watanabe K, (2008) Substrate-induced gene expression (SIGEX) screening of metagenome libraries. Nat Protoc 3, 1202-1212.
    • (2008) Nat Protoc , vol.3 , pp. 1202-1212
    • Uchiyama, T.1    Watanabe, K.2
  • 48
    • 80053934387 scopus 로고    scopus 로고
    • Association of dnt genes of Burkholderia sp. DNT with the substrate-blind regulator DntR draws the evolutionary itinerary of 2,4-dinitrotoluene biodegradation
    • de Las Heras A, Chavarría M, &, de Lorenzo V, (2011) Association of dnt genes of Burkholderia sp. DNT with the substrate-blind regulator DntR draws the evolutionary itinerary of 2,4-dinitrotoluene biodegradation. Mol Microbiol 82, 287-299.
    • (2011) Mol Microbiol , vol.82 , pp. 287-299
    • De Las Heras, A.1    Chavarría, M.2    De Lorenzo, V.3
  • 49
    • 27144452575 scopus 로고    scopus 로고
    • Problems with metagenomic screening
    • author reply, 1045-1046
    • de Lorenzo V, (2005) Problems with metagenomic screening. Nat Biotechnol 23, 1045; author reply, 1045-1046.
    • (2005) Nat Biotechnol , vol.23 , pp. 1045
    • De Lorenzo, V.1
  • 50
    • 78149437429 scopus 로고    scopus 로고
    • Product-induced gene expression, a product-responsive reporter assay used to screen metagenomic libraries for enzyme-encoding genes
    • Uchiyama T, &, Miyazaki K, (2010) Product-induced gene expression, a product-responsive reporter assay used to screen metagenomic libraries for enzyme-encoding genes. Appl Environ Microbiol 76, 7029-7035.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 7029-7035
    • Uchiyama, T.1    Miyazaki, K.2
  • 52
    • 0038752617 scopus 로고    scopus 로고
    • Computational design of receptor and sensor proteins with novel functions
    • DOI 10.1038/nature01556
    • Looger LL, Dwyer MA, Smith JJ, &, Hellinga HW, (2003) Computational design of receptor and sensor proteins with novel functions. Nature 423, 185-190. (Pubitemid 36569543)
    • (2003) Nature , vol.423 , Issue.6936 , pp. 185-190
    • Looger, L.L.1    Dwyer, M.A.2    Smith, J.J.3    Hellinga, H.W.4
  • 53
    • 73249124179 scopus 로고    scopus 로고
    • Computational design of ligand binding is not a solved problem
    • Schreier B, Stumpp C, Wiesner S, &, Höcker B, (2009) Computational design of ligand binding is not a solved problem. Proc Natl Acad Sci USA 106, 18491-18496.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 18491-18496
    • Schreier, B.1    Stumpp, C.2    Wiesner, S.3    Höcker, B.4
  • 56
    • 0031041234 scopus 로고    scopus 로고
    • Effector specificity mutants of the transcriptional activator NahR of naphthalene degrading Pseudomonas define protein sites involved in binding of aromatic inducers
    • DOI 10.1074/jbc.272.7.3986
    • Cebolla A, Sousa C, &, de Lorenzo V, (1997) Effector specificity mutants of the transcriptional activator NahR of naphthalene degrading Pseudomonas define protein sites involved in binding of aromatic inducers. J Biol Chem 272, 3986-3992. (Pubitemid 27078458)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.7 , pp. 3986-3992
    • Cebolla, A.1    Sousa, C.2    De Lorenzo, V.3
  • 57
    • 33644956913 scopus 로고    scopus 로고
    • Surveying biotransformations with à la carte genetic traps: Translating dehydrochlorination of lindane (gamma-hexachlorocyclohexane) into lacZ-based phenotypes
    • Mohn WW, Garmendia J, Galvao TC, &, de Lorenzo V, (2006) Surveying biotransformations with à la carte genetic traps: translating dehydrochlorination of lindane (gamma-hexachlorocyclohexane) into lacZ-based phenotypes. Environ Microbiol 8, 546-555.
    • (2006) Environ Microbiol , vol.8 , pp. 546-555
    • Mohn, W.W.1    Garmendia, J.2    Galvao, T.C.3    De Lorenzo, V.4
  • 58
    • 79251580632 scopus 로고    scopus 로고
    • Design and application of a mevalonate-responsive regulatory protein
    • Tang SY, &, Cirino PC, (2011) Design and application of a mevalonate-responsive regulatory protein. Angew Chem Int Ed Engl 50, 1084-1086.
    • (2011) Angew Chem Int Ed Engl , vol.50 , pp. 1084-1086
    • Tang, S.Y.1    Cirino, P.C.2
  • 59
    • 0034022841 scopus 로고    scopus 로고
    • Using an AraC-based three-hybrid system to detect biocatalysts in vivo
    • DOI 10.1038/75414
    • Firestine SM, Salinas F, Nixon AE, Baker SJ, &, Benkovic SJ, (2000) Using an AraC-based three-hybrid system to detect biocatalysts in vivo. Nat Biotechnol 18, 544-547. (Pubitemid 30313960)
    • (2000) Nature Biotechnology , vol.18 , Issue.5 , pp. 544-547
    • Firestine, S.M.1    Salinas, F.2    Nixon, A.E.3    Baker, S.J.4    Benkovic, S.J.5
  • 61
    • 9344270529 scopus 로고    scopus 로고
    • Directed evolution of a glycosynthase via chemical complementation
    • DOI 10.1021/ja046238v
    • Lin H, Tao HY, &, Cornish VW, (2004) Directed evolution of a glycosynthase via chemical complementation. J Am Chem Soc 126, 15051-15059. (Pubitemid 39557264)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.46 , pp. 15051-15059
    • Lin, H.1    Tao, H.2    Cornish, V.W.3
  • 62
    • 84869576288 scopus 로고    scopus 로고
    • High-throughput selection for cellulase catalysts using chemical complementation
    • Peralta-Yahya P, Carter BT, Lin H, Tao H, &, Cornish VW, (2008) High-throughput selection for cellulase catalysts using chemical complementation. J Am Chem Soc 130, 17446-17452.
    • (2008) J Am Chem Soc , vol.130 , pp. 17446-17452
    • Peralta-Yahya, P.1    Carter, B.T.2    Lin, H.3    Tao, H.4    Cornish, V.W.5
  • 63
    • 84858650282 scopus 로고    scopus 로고
    • Intracellular detection and evolution of site-specific proteases using a genetic selection system
    • Verhoeven KD, Altstadt OC, &, Savinov SN, (2012) Intracellular detection and evolution of site-specific proteases using a genetic selection system. Appl Biochem Biotechnol 166, 1340-1354.
    • (2012) Appl Biochem Biotechnol , vol.166 , pp. 1340-1354
    • Verhoeven, K.D.1    Altstadt, O.C.2    Savinov, S.N.3
  • 66
    • 6044261460 scopus 로고    scopus 로고
    • Genetic screens and selections for small molecules based on a synthetic riboswitch that activates protein translation
    • DOI 10.1021/ja048634j
    • Desai SK, &, Gallivan JP, (2004) Genetic screens and selections for small molecules based on a synthetic riboswitch that activates protein translation. J Am Chem Soc 126, 13247-13254. (Pubitemid 39382751)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.41 , pp. 13247-13254
    • Desai, S.K.1    Gallivan, J.P.2
  • 67
    • 79251539925 scopus 로고    scopus 로고
    • Substrate profiling of tobacco etch virus protease using a novel fluorescence-assisted whole-cell assay
    • Kostallas G, Löfdahl PA, &, Samuelson P, (2011) Substrate profiling of tobacco etch virus protease using a novel fluorescence-assisted whole-cell assay. PLoS One 6, e16136.
    • (2011) PLoS One , vol.6
    • Kostallas, G.1    Löfdahl, P.A.2    Samuelson, P.3
  • 68
    • 33644900247 scopus 로고    scopus 로고
    • Diversification and specialization of HIV protease function during in vitro evolution
    • O'Loughlin TL, Greene DN, &, Matsumura I, (2006) Diversification and specialization of HIV protease function during in vitro evolution. Mol Biol Evol 23, 764-778.
    • (2006) Mol Biol Evol , vol.23 , pp. 764-778
    • O'Loughlin, T.L.1    Greene, D.N.2    Matsumura, I.3
  • 69
    • 84859988527 scopus 로고    scopus 로고
    • A functional screen for recovery of 4′-phosphopantetheinyl transferase and associated natural product biosynthesis genes from metagenome libraries
    • Owen JG, Robins KJ, Parachin NS, &, Ackerley DF, (2012) A functional screen for recovery of 4′-phosphopantetheinyl transferase and associated natural product biosynthesis genes from metagenome libraries. Environ Microbiol 14, 1198-1209.
    • (2012) Environ Microbiol , vol.14 , pp. 1198-1209
    • Owen, J.G.1    Robins, K.J.2    Parachin, N.S.3    Ackerley, D.F.4
  • 70
    • 56149121547 scopus 로고    scopus 로고
    • Directed enzyme evolution via small and effective neutral drift libraries
    • Gupta RD, &, Tawfik DS, (2008) Directed enzyme evolution via small and effective neutral drift libraries. Nat Methods 5, 939-942.
    • (2008) Nat Methods , vol.5 , pp. 939-942
    • Gupta, R.D.1    Tawfik, D.S.2
  • 71
    • 26444588105 scopus 로고    scopus 로고
    • A simple dual selection for functionally active mutants of Plasmodium falciparum dihydrofolate reductase with improved solubility
    • DOI 10.1093/protein/gzi044
    • Japrung D, Chusacultanachai S, Yuvaniyama J, Wilairat P, &, Yuthavong Y, (2005) A simple dual selection for functionally active mutants of Plasmodium falciparum dihydrofolate reductase with improved solubility. Protein Eng Des Sel 18, 457-464. (Pubitemid 41433102)
    • (2005) Protein Engineering, Design and Selection , vol.18 , Issue.10 , pp. 457-464
    • Japrung, D.1    Chusacultanachai, S.2    Yuvaniyama, J.3    Wilairat, P.4    Yuthavong, Y.5
  • 73
  • 74
    • 0034049099 scopus 로고    scopus 로고
    • Escherichia coli one- and two-hybrid systems for the analysis and identification of protein-protein interactions
    • DOI 10.1006/meth.1999.0908
    • Hu JC, Kornacker MG, &, Hochschild A, (2000) Escherichia coli one- and two-hybrid systems for the analysis and identification of protein-protein interactions. Methods 20, 80-94. (Pubitemid 30119603)
    • (2000) Methods , vol.20 , Issue.1 , pp. 80-94
    • Hu, J.C.1    Kornacker, M.G.2    Hochschild, A.3


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