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Volumn 115, Issue 3, 2018, Pages 619-624

Engineering posttranslational proofreading to discriminate nonstandard amino acids

Author keywords

Amino acids; Genetic code expansion; N end rule; Nonstandard; Protein degradation; Synthetic biology

Indexed keywords

AMINO ACID; BACTERIAL PROTEIN; BACTERIAL PROTEIN CLPS; NONSTANDARD AMINO ACID; PHENYLALANINE; TYROSINE TRANSFER RNA; TYROSINE TRANSFER RNA LIGASE; UNCLASSIFIED DRUG; AMINOBIPHENYL DERIVATIVE; ARCHAEAL PROTEIN;

EID: 85040566246     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1715137115     Document Type: Article
Times cited : (30)

References (57)
  • 1
    • 84900420574 scopus 로고    scopus 로고
    • Expanding and reprogramming the genetic code of cells and animals
    • Chin JW (2014) Expanding and reprogramming the genetic code of cells and animals. Annu Rev Biochem 83:379–408.
    • (2014) Annu Rev Biochem , vol.83 , pp. 379-408
    • Chin, J.W.1
  • 2
    • 84915756442 scopus 로고    scopus 로고
    • Designing logical codon reassignment–Expanding the chemistry in biology
    • Dumas A, Lercher L, Spicer CD, Davis BG (2015) Designing logical codon reassignment–Expanding the chemistry in biology. Chem Sci (Camb) 6:50–69.
    • (2015) Chem Sci (Camb) , vol.6 , pp. 50-69
    • Dumas, A.1    Lercher, L.2    Spicer, C.D.3    Davis, B.G.4
  • 3
    • 84923112573 scopus 로고    scopus 로고
    • Biocontainment of genetically modified organisms by synthetic protein design
    • Mandell DJ, et al. (2015) Biocontainment of genetically modified organisms by synthetic protein design. Nature 518:55–60.
    • (2015) Nature , vol.518 , pp. 55-60
    • Mandell, D.J.1
  • 4
    • 84922595374 scopus 로고    scopus 로고
    • Recoded organisms engineered to depend on synthetic amino acids
    • Rovner AJ, et al. (2015) Recoded organisms engineered to depend on synthetic amino acids. Nature 518:89–93.
    • (2015) Nature , vol.518 , pp. 89-93
    • Rovner, A.J.1
  • 5
    • 84983523350 scopus 로고    scopus 로고
    • Design, synthesis, and testing toward a 57-codon genome
    • Ostrov N, et al. (2016) Design, synthesis, and testing toward a 57-codon genome. Science 353:819–822.
    • (2016) Science , vol.353 , pp. 819-822
    • Ostrov, N.1
  • 6
    • 84885791219 scopus 로고    scopus 로고
    • Genomically recoded organisms expand biological functions
    • Lajoie MJ, et al. (2013) Genomically recoded organisms expand biological functions. Science 342:357–360.
    • (2013) Science , vol.342 , pp. 357-360
    • Lajoie, M.J.1
  • 7
    • 84978879822 scopus 로고    scopus 로고
    • Genomic recoding broadly obstructs the propagation of horizontally transferred genetic elements
    • Ma NJ, Isaacs FJ (2016) Genomic recoding broadly obstructs the propagation of horizontally transferred genetic elements. Cell Syst 3:199–207.
    • (2016) Cell Syst , vol.3 , pp. 199-207
    • Ma, N.J.1    Isaacs, F.J.2
  • 8
    • 11144357971 scopus 로고    scopus 로고
    • Aminoacyl-tRNAs: Setting the limits of the genetic code
    • Ibba M, Söll D (2004) Aminoacyl-tRNAs: Setting the limits of the genetic code. Genes Dev 18:731–738.
    • (2004) Genes Dev , vol.18 , pp. 731-738
    • Ibba, M.1    Söll, D.2
  • 9
    • 51649087417 scopus 로고    scopus 로고
    • Transplantation of a tyrosine editing domain into a tyrosyl-tRNA synthetase variant enhances its specificity for a tyrosine analog
    • Oki K, Sakamoto K, Kobayashi T, Sasaki HM, Yokoyama S (2008) Transplantation of a tyrosine editing domain into a tyrosyl-tRNA synthetase variant enhances its specificity for a tyrosine analog. Proc Natl Acad Sci USA 105:13298–13303.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 13298-13303
    • Oki, K.1    Sakamoto, K.2    Kobayashi, T.3    Sasaki, H.M.4    Yokoyama, S.5
  • 10
    • 73149104141 scopus 로고    scopus 로고
    • An enhanced system for unnatural amino acid mutagenesis in E. Coli
    • Young TS, Ahmad I, Yin JA, Schultz PG (2010) An enhanced system for unnatural amino acid mutagenesis in E. coli. J Mol Biol 395:361–374.
    • (2010) J Mol Biol , vol.395 , pp. 361-374
    • Young, T.S.1    Ahmad, I.2    Yin, J.A.3    Schultz, P.G.4
  • 11
    • 79952140370 scopus 로고    scopus 로고
    • Importance of single molecular determinants in the fidelity of expanded genetic codes
    • Antonczak AK, et al. (2011) Importance of single molecular determinants in the fidelity of expanded genetic codes. Proc Natl Acad Sci USA 108:1320–1325.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 1320-1325
    • Antonczak, A.K.1
  • 12
    • 84859498501 scopus 로고    scopus 로고
    • Performance analysis of orthogonal pairs designed for an expanded eukaryotic genetic code
    • Nehring S, Budisa N, Wiltschi B (2012) Performance analysis of orthogonal pairs designed for an expanded eukaryotic genetic code. PLoS One 7:e31992.
    • (2012) PLoS One , vol.7
    • Nehring, S.1    Budisa, N.2    Wiltschi, B.3
  • 13
    • 85013083067 scopus 로고    scopus 로고
    • Rapid and inexpensive evaluation of nonstandard amino acid incorporation in Escherichia coli
    • Monk JW, et al. (2017) Rapid and inexpensive evaluation of nonstandard amino acid incorporation in Escherichia coli. ACS Synth Biol 6:45–54.
    • (2017) ACS Synth Biol , vol.6 , pp. 45-54
    • Monk, J.W.1
  • 14
    • 84906056183 scopus 로고    scopus 로고
    • Exploring the substrate range of wild-type aminoacyl-tRNA synthetases
    • Fan C, Ho JML, Chirathivat N, Söll D, Wang Y-S (2014) Exploring the substrate range of wild-type aminoacyl-tRNA synthetases. ChemBioChem 15:1805–1809.
    • (2014) ChemBioChem , vol.15 , pp. 1805-1809
    • Fan, C.1    Ho, J.M.L.2    Chirathivat, N.3    Söll, D.4    Wang, Y.-S.5
  • 15
    • 84912074071 scopus 로고    scopus 로고
    • Polyspecific pyrrolysyl-tRNA synthetases from directed evolution
    • Guo L-T, et al. (2014) Polyspecific pyrrolysyl-tRNA synthetases from directed evolution. Proc Natl Acad Sci USA 111:16724–16729.
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 16724-16729
    • Guo, L.-T.1
  • 16
    • 79951644876 scopus 로고    scopus 로고
    • The de novo engineering of pyrrolysyl-tRNA synthetase for genetic incorporation of L-phenylalanine and its derivatives
    • Wang Y-S, et al. (2011) The de novo engineering of pyrrolysyl-tRNA synthetase for genetic incorporation of L-phenylalanine and its derivatives. Mol Biosyst 7:714–717.
    • (2011) Mol Biosyst , vol.7 , pp. 714-717
    • Wang, Y.-S.1
  • 17
    • 37349066767 scopus 로고    scopus 로고
    • A genetically encoded bidentate, metal-binding amino acid
    • Xie J, Liu W, Schultz PG (2007) A genetically encoded bidentate, metal-binding amino acid. Angew Chem Int Ed Engl 46:9239–9242.
    • (2007) Angew Chem Int Ed Engl , vol.46 , pp. 9239-9242
    • Xie, J.1    Liu, W.2    Schultz, P.G.3
  • 18
    • 0023003380 scopus 로고
    • In vivo half-life of a protein is a function of its amino-terminal residue
    • Bachmair A, Finley D, Varshavsky A (1986) In vivo half-life of a protein is a function of its amino-terminal residue. Science 234:179–186.
    • (1986) Science , vol.234 , pp. 179-186
    • Bachmair, A.1    Finley, D.2    Varshavsky, A.3
  • 21
    • 85021091827 scopus 로고    scopus 로고
    • Targeting the N terminus for site-selective protein modification
    • Rosen CB, Francis MB (2017) Targeting the N terminus for site-selective protein modification. Nat Chem Biol 13:697–705.
    • (2017) Nat Chem Biol , vol.13 , pp. 697-705
    • Rosen, C.B.1    Francis, M.B.2
  • 22
    • 80054854782 scopus 로고    scopus 로고
    • RF1 knockout allows ribosomal incorporation of unnatural amino acids at multiple sites
    • Johnson DBF, et al. (2011) RF1 knockout allows ribosomal incorporation of unnatural amino acids at multiple sites. Nat Chem Biol 7:779–786.
    • (2011) Nat Chem Biol , vol.7 , pp. 779-786
    • Johnson, D.B.F.1
  • 23
    • 84868088312 scopus 로고    scopus 로고
    • Near-cognate suppression of amber, opal and quadruplet codons competes with aminoacyl-tRNAPyl for genetic code expansion
    • O’Donoghue P, et al. (2012) Near-cognate suppression of amber, opal and quadruplet codons competes with aminoacyl-tRNAPyl for genetic code expansion. FEBS Lett 586: 3931–3937.
    • (2012) FEBS Lett , vol.586 , pp. 3931-3937
    • O’Donoghue, P.1
  • 24
    • 33847226240 scopus 로고    scopus 로고
    • ClpS modulates but is not essential for bacterial N-end rule degradation
    • Wang KH, Sauer RT, Baker TA (2007) ClpS modulates but is not essential for bacterial N-end rule degradation. Genes Dev 21:403–408.
    • (2007) Genes Dev , vol.21 , pp. 403-408
    • Wang, K.H.1    Sauer, R.T.2    Baker, T.A.3
  • 25
    • 54049111071 scopus 로고    scopus 로고
    • Tuning the strength of a bacterial N-end rule degradation signal
    • Wang KH, Oakes ESC, Sauer RT, Baker TA (2008) Tuning the strength of a bacterial N-end rule degradation signal. J Biol Chem 283:24600–24607.
    • (2008) J Biol Chem , vol.283 , pp. 24600-24607
    • Wang, K.H.1    Oakes, E.S.C.2    Sauer, R.T.3    Baker, T.A.4
  • 26
    • 84949796862 scopus 로고    scopus 로고
    • Evolution of translation machinery in recoded bacteria enables multi-site incorporation of nonstandard amino acids
    • Amiram M, et al. (2015) Evolution of translation machinery in recoded bacteria enables multi-site incorporation of nonstandard amino acids. Nat Biotechnol 33:1272–1279.
    • (2015) Nat Biotechnol , vol.33 , pp. 1272-1279
    • Amiram, M.1
  • 27
    • 84855908601 scopus 로고    scopus 로고
    • Quantifying plasmid copy number to investigate plasmid dosage effects associated with directed protein evolution
    • Million-Weaver S, Alexander DL, Allen JM, Camps M (2012) Quantifying plasmid copy number to investigate plasmid dosage effects associated with directed protein evolution. Methods Mol Biol 834:33–48.
    • (2012) Methods Mol Biol , vol.834 , pp. 33-48
    • Million-Weaver, S.1    Alexander, D.L.2    Allen, J.M.3    Camps, M.4
  • 28
    • 0025991456 scopus 로고
    • Cloning and functional analysis of the ubiquitin-specific protease gene UBP1 of Saccharomyces cerevisiae
    • Tobias JW, Varshavsky A (1991) Cloning and functional analysis of the ubiquitin-specific protease gene UBP1 of Saccharomyces cerevisiae. J Biol Chem 266:12021–12028.
    • (1991) J Biol Chem , vol.266 , pp. 12021-12028
    • Tobias, J.W.1    Varshavsky, A.2
  • 29
    • 26844527708 scopus 로고    scopus 로고
    • Expression of yeast deubiquitination enzyme UBP1 analogues in E. Coli
    • Wojtowicz A, et al. (2005) Expression of yeast deubiquitination enzyme UBP1 analogues in E. coli. Microb Cell Fact 4:17.
    • (2005) Microb Cell Fact , vol.4 , pp. 17
    • Wojtowicz, A.1
  • 30
    • 79960451307 scopus 로고    scopus 로고
    • The ClpS adaptor mediates staged delivery of N-end rule substrates to the AAA+ ClpAP protease
    • Román-Hernández G, Hou JY, Grant RA, Sauer RT, Baker TA (2011) The ClpS adaptor mediates staged delivery of N-end rule substrates to the AAA+ ClpAP protease. Mol Cell 43:217–228.
    • (2011) Mol Cell , vol.43 , pp. 217-228
    • Román-Hernández, G.1    Hou, J.Y.2    Grant, R.A.3    Sauer, R.T.4    Baker, T.A.5
  • 31
    • 0036210995 scopus 로고    scopus 로고
    • ClpS, a substrate modulator of the ClpAP machine
    • Dougan DA, Reid BG, Horwich AL, Bukau B (2002) ClpS, a substrate modulator of the ClpAP machine. Mol Cell 9:673–683.
    • (2002) Mol Cell , vol.9 , pp. 673-683
    • Dougan, D.A.1    Reid, B.G.2    Horwich, A.L.3    Bukau, B.4
  • 33
    • 0035917812 scopus 로고    scopus 로고
    • Expanding the genetic code of Escherichia coli
    • Wang L, Brock A, Herberich B, Schultz PG (2001) Expanding the genetic code of Escherichia coli. Science 292:498–500.
    • (2001) Science , vol.292 , pp. 498-500
    • Wang, L.1    Brock, A.2    Herberich, B.3    Schultz, P.G.4
  • 34
    • 0035812828 scopus 로고    scopus 로고
    • Uniform binding of aminoacyl-tRNAs to elongation factor Tu by thermodynamic compensation
    • LaRiviere FJ, Wolfson AD, Uhlenbeck OC (2001) Uniform binding of aminoacyl-tRNAs to elongation factor Tu by thermodynamic compensation. Science 294:165–168.
    • (2001) Science , vol.294 , pp. 165-168
    • LaRiviere, F.J.1    Wolfson, A.D.2    Uhlenbeck, O.C.3
  • 35
    • 60849128493 scopus 로고    scopus 로고
    • Understanding the sequence specificity of tRNA binding to elongation factor Tu using tRNA mutagenesis
    • Schrader JM, Chapman SJ, Uhlenbeck OC (2009) Understanding the sequence specificity of tRNA binding to elongation factor Tu using tRNA mutagenesis. J Mol Biol 386:1255–1264.
    • (2009) J Mol Biol , vol.386 , pp. 1255-1264
    • Schrader, J.M.1    Chapman, S.J.2    Uhlenbeck, O.C.3
  • 36
    • 0035377246 scopus 로고    scopus 로고
    • Dual system to reinforce biological containment of recombinant bacteria designed for rhizoremediation
    • Ronchel MC, Ramos JL (2001) Dual system to reinforce biological containment of recombinant bacteria designed for rhizoremediation. Appl Environ Microbiol 67:2649–2656.
    • (2001) Appl Environ Microbiol , vol.67 , pp. 2649-2656
    • Ronchel, M.C.1    Ramos, J.L.2
  • 37
    • 61449233980 scopus 로고    scopus 로고
    • A fluorescent, genetically engineered microorganism that degrades organophosphates and commits suicide when required
    • Li Q, Wu Y-J (2009) A fluorescent, genetically engineered microorganism that degrades organophosphates and commits suicide when required. Appl Microbiol Biotechnol 82:749–756.
    • (2009) Appl Microbiol Biotechnol , vol.82 , pp. 749-756
    • Li, Q.1    Wu, Y.-J.2
  • 38
    • 79957929747 scopus 로고    scopus 로고
    • Characterization of a synthetic bacterial self-destruction device for programmed cell death and for recombinant proteins release
    • Pasotti L, Zucca S, Lupotto M, Cusella De Angelis MG, Magni P (2011) Characterization of a synthetic bacterial self-destruction device for programmed cell death and for recombinant proteins release. J Biol Eng 5:8.
    • (2011) J Biol Eng , vol.5 , pp. 8
    • Pasotti, L.1    Zucca, S.2    Lupotto, M.3    De Angelis, C.M.G.4    Magni, P.5
  • 39
    • 84925610163 scopus 로고    scopus 로고
    • GeneGuard: A modular plasmid system designed for biosafety
    • Wright O, Delmans M, Stan G-B, Ellis T (2015) GeneGuard: A modular plasmid system designed for biosafety. ACS Synth Biol 4:307–316.
    • (2015) ACS Synth Biol , vol.4 , pp. 307-316
    • Wright, O.1    Delmans, M.2    Stan, G.-B.3    Ellis, T.4
  • 40
    • 84955192252 scopus 로고    scopus 로고
    • Deadman’ and ‘Passcode’ microbial kill switches for bacterial containment
    • Chan CTY, Lee JW, Cameron DE, Bashor CJ, Collins JJ (2016) ‘Deadman’ and ‘Passcode’ microbial kill switches for bacterial containment. Nat Chem Biol 12:82–86.
    • (2016) Nat Chem Biol , vol.12 , pp. 82-86
    • Chan, C.T.Y.1    Lee, J.W.2    Cameron, D.E.3    Bashor, C.J.4    Collins, J.J.5
  • 41
    • 70349320611 scopus 로고    scopus 로고
    • Discovery of Escherichia coli methionyl-tRNA synthetase mutants for efficient labeling of proteins with azidonorleucine in vivo
    • Tanrikulu IC, Schmitt E, Mechulam Y, Goddard WA, 3rd, Tirrell DA (2009) Discovery of Escherichia coli methionyl-tRNA synthetase mutants for efficient labeling of proteins with azidonorleucine in vivo. Proc Natl Acad Sci USA 106:15285–15290.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 15285-15290
    • Tanrikulu, I.C.1    Schmitt, E.2    Mechulam, Y.3    Goddard, W.A.4    Tirrell, D.A.5
  • 42
    • 84892823522 scopus 로고    scopus 로고
    • Experimental challenges of sense codon reassignment: An innovative approach to genetic code expansion
    • Krishnakumar R, Ling J (2014) Experimental challenges of sense codon reassignment: An innovative approach to genetic code expansion. FEBS Lett 588:383–388.
    • (2014) FEBS Lett , vol.588 , pp. 383-388
    • Krishnakumar, R.1    Ling, J.2
  • 43
    • 84951731246 scopus 로고    scopus 로고
    • Evaluating sense codon reassignment with a simple fluorescence screen
    • Biddle W, Schmitt MA, Fisk JD (2015) Evaluating sense codon reassignment with a simple fluorescence screen. Biochemistry 54:7355–7364.
    • (2015) Biochemistry , vol.54 , pp. 7355-7364
    • Biddle, W.1    Schmitt, M.A.2    Fisk, J.D.3
  • 44
    • 84868135871 scopus 로고    scopus 로고
    • A sensitive green fluorescent protein biomarker of N-glycosylation site occupancy
    • Losfeld M-E, Soncin F, Ng BG, Singec I, Freeze HH (2012) A sensitive green fluorescent protein biomarker of N-glycosylation site occupancy. FASEB J 26:4210–4217.
    • (2012) FASEB J , vol.26 , pp. 4210-4217
    • Losfeld, M.-E.1    Soncin, F.2    Ng, B.G.3    Singec, I.4    Freeze, H.H.5
  • 45
    • 84894445908 scopus 로고    scopus 로고
    • Production of site-specific antibody-drug conjugates using optimized non-natural amino acids in a cell-free expression system
    • Zimmerman ES, et al. (2014) Production of site-specific antibody-drug conjugates using optimized non-natural amino acids in a cell-free expression system. Bioconjug Chem 25: 351–361.
    • (2014) Bioconjug Chem , vol.25 , pp. 351-361
    • Zimmerman, E.S.1
  • 46
    • 85013793402 scopus 로고    scopus 로고
    • Coupling genetic code expansion and metabolic engineering for synthetic cells
    • Völler J-S, Budisa N (2017) Coupling genetic code expansion and metabolic engineering for synthetic cells. Curr Opin Biotechnol 48:1–7.
    • (2017) Curr Opin Biotechnol , vol.48 , pp. 1-7
    • Völler, J.-S.1    Budisa, N.2
  • 47
    • 85017885362 scopus 로고    scopus 로고
    • An N-end rule pathway that recognizes proline and destroys gluconeogenic enzymes
    • Chen S-J, Wu X, Wadas B, Oh J-H, Varshavsky A (2017) An N-end rule pathway that recognizes proline and destroys gluconeogenic enzymes. Science 355:eaal3655.
    • (2017) Science , vol.355 , pp. eaal3655
    • Chen, S.-J.1    Wu, X.2    Wadas, B.3    Oh, J.-H.4    Varshavsky, A.5
  • 48
    • 3042672710 scopus 로고    scopus 로고
    • Removal of N-terminal methionine from recombinant proteins by engineered E. Coli methionine aminopeptidase
    • Liao Y-D, Jeng J-C, Wang C-F, Wang S-C, Chang S-T (2004) Removal of N-terminal methionine from recombinant proteins by engineered E. coli methionine aminopeptidase. Protein Sci 13:1802–1810.
    • (2004) Protein Sci , vol.13 , pp. 1802-1810
    • Liao, Y.-D.1    Jeng, J.-C.2    Wang, C.-F.3    Wang, S.-C.4    Chang, S.-T.5
  • 49
    • 33644786997 scopus 로고    scopus 로고
    • Aminoacyl-transferases and the N-end rule pathway of prokaryotic/ eukaryotic specificity in a human pathogen
    • Graciet E, et al. (2006) Aminoacyl-transferases and the N-end rule pathway of prokaryotic/ eukaryotic specificity in a human pathogen. Proc Natl Acad Sci USA 103:3078–3083.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 3078-3083
    • Graciet, E.1
  • 50
    • 0037422608 scopus 로고    scopus 로고
    • Addition of the keto functional group to the genetic code of Escherichia coli
    • Wang L, Zhang Z, Brock A, Schultz PG (2003) Addition of the keto functional group to the genetic code of Escherichia coli. Proc Natl Acad Sci USA 100:56–61.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 56-61
    • Wang, L.1    Zhang, Z.2    Brock, A.3    Schultz, P.G.4
  • 51
    • 0037036727 scopus 로고    scopus 로고
    • Addition of p-azido-L-phenylalanine to the genetic code of Escherichia coli
    • Chin JW, et al. (2002) Addition of p-azido-L-phenylalanine to the genetic code of Escherichia coli. J Am Chem Soc 124:9026–9027.
    • (2002) J Am Chem Soc , vol.124 , pp. 9026-9027
    • Chin, J.W.1
  • 52
    • 0037028931 scopus 로고    scopus 로고
    • Adding L-3-(2-Naphthyl)alanine to the genetic code of E. Coli
    • Wang L, Brock A, Schultz PG (2002) Adding L-3-(2-Naphthyl)alanine to the genetic code of E. coli. J Am Chem Soc 124:1836–1837.
    • (2002) J Am Chem Soc , vol.124 , pp. 1836-1837
    • Wang, L.1    Brock, A.2    Schultz, P.G.3
  • 53
    • 67349270900 scopus 로고    scopus 로고
    • Enzymatic assembly of DNA molecules up to several hundred kilobases
    • Gibson DG, et al. (2009) Enzymatic assembly of DNA molecules up to several hundred kilobases. Nat Methods 6:343–345.
    • (2009) Nat Methods , vol.6 , pp. 343-345
    • Gibson, D.G.1
  • 54
    • 78049389374 scopus 로고    scopus 로고
    • Rational design of an orthogonal tryptophanyl nonsense suppressor tRNA
    • Hughes RA, Ellington AD (2010) Rational design of an orthogonal tryptophanyl nonsense suppressor tRNA. Nucleic Acids Res 38:6813–6830.
    • (2010) Nucleic Acids Res , vol.38 , pp. 6813-6830
    • Hughes, R.A.1    Ellington, A.D.2
  • 55
    • 84892184252 scopus 로고    scopus 로고
    • Directed evolution of genetic parts and circuits by compartmentalized partnered replication
    • Ellefson JW, et al. (2014) Directed evolution of genetic parts and circuits by compartmentalized partnered replication. Nat Biotechnol 32:97–101.
    • (2014) Nat Biotechnol , vol.32 , pp. 97-101
    • Ellefson, J.W.1
  • 56
    • 70349964350 scopus 로고    scopus 로고
    • Automated design of synthetic ribosome binding sites to control protein expression
    • Salis HM, Mirsky EA, Voigt CA (2009) Automated design of synthetic ribosome binding sites to control protein expression. Nat Biotechnol 27:946–950.
    • (2009) Nat Biotechnol , vol.27 , pp. 946-950
    • Salis, H.M.1    Mirsky, E.A.2    Voigt, C.A.3
  • 57
    • 84906330621 scopus 로고    scopus 로고
    • Synthesis and accumulation of aromatic aldehydes in an engineered strain of Escherichia coli
    • Kunjapur AM, Tarasova Y, Prather KLJ (2014) Synthesis and accumulation of aromatic aldehydes in an engineered strain of Escherichia coli. J Am Chem Soc 136: 11644–11654.
    • (2014) J Am Chem Soc , vol.136 , pp. 11644-11654
    • Kunjapur, A.M.1    Tarasova, Y.2    Prather, K.L.J.3


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