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Volumn 7, Issue , 2016, Pages

A general strategy for expanding polymerase function by droplet microfluidics

Author keywords

[No Author keywords available]

Indexed keywords

DNA POLYMERASE; MANGANESE; NUCLEIC ACID; RNA POLYMERASE; BIOMIMETIC MATERIAL; DNA DIRECTED DNA POLYMERASE; MONOSACCHARIDE;

EID: 84963994525     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms11235     Document Type: Article
Times cited : (133)

References (36)
  • 1
    • 84860013215 scopus 로고    scopus 로고
    • Synthetic genetic polymers capable of heredity and evolution
    • Pinheiro V. B., et al. Synthetic genetic polymers capable of heredity and evolution. Science 336, 341-344 (2012
    • (2012) Science , vol.336 , pp. 341-344
    • Pinheiro, V.B.1
  • 2
    • 84863116739 scopus 로고    scopus 로고
    • Darwinian evolution of an alternative genetic system provides support for TNA as an RNA progenitor
    • Yu H., Zhang S., & Chaput J. C. Darwinian evolution of an alternative genetic system provides support for TNA as an RNA progenitor. Nat. Chem. 4, 183-187 (2012
    • (2012) Nat. Chem , vol.4 , pp. 183-187
    • Yu, H.1    Zhang, S.2    Chaput, J.C.3
  • 3
    • 84874917623 scopus 로고    scopus 로고
    • An efficient and faithful in vitro replication system for threose nucleic acid
    • Yu H., Zhang S., Dunn M., & Chaput J. C. An efficient and faithful in vitro replication system for threose nucleic acid. J. Am. Chem. Soc. 135, 3583-3591 (2013
    • (2013) J. Am. Chem. Soc , vol.135 , pp. 3583-3591
    • Yu, H.1    Zhang, S.2    Dunn, M.3    Chaput, J.C.4
  • 4
    • 84870004833 scopus 로고    scopus 로고
    • The emerging world of synthetic genetics
    • Chaput J. C., Yu H., & Zhang S. The emerging world of synthetic genetics. Chem. Biol. 19, 1360-1371 (2012
    • (2012) Chem. Biol , vol.19 , pp. 1360-1371
    • Chaput, J.C.1    Yu, H.2    Zhang, S.3
  • 5
    • 84872379019 scopus 로고    scopus 로고
    • Synthetic polymers and their potential as genetic materials
    • Pinheiro V. B., Loakes D., & Holliger P. Synthetic polymers and their potential as genetic materials. Bioessays 35, 113-122 (2012
    • (2012) Bioessays , vol.35 , pp. 113-122
    • Pinheiro, V.B.1    Loakes, D.2    Holliger, P.3
  • 6
    • 84860015313 scopus 로고    scopus 로고
    • Toward an alternative biology
    • Joyce G. F. Toward an alternative biology. Science 336, 307-308 (2012
    • (2012) Science , vol.336 , pp. 307-308
    • Joyce, G.F.1
  • 7
    • 84964801157 scopus 로고    scopus 로고
    • The structural diversity of artificial genetic polymers
    • Anosova I., et al. The structural diversity of artificial genetic polymers. Nucleic Acids Res. 44, 1007-1021 (2016
    • (2016) Nucleic Acids Res , vol.44 , pp. 1007-1021
    • Anosova, I.1
  • 8
    • 19744365730 scopus 로고    scopus 로고
    • Kinetic analysis of an efficient DNA-dependent TNA polymerase
    • Horhota A., et al. Kinetic analysis of an efficient DNA-dependent TNA polymerase. J. Am. Chem. Soc. 127, 7427-7434 (2005
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 7427-7434
    • Horhota, A.1
  • 10
    • 68149136529 scopus 로고    scopus 로고
    • Polymerase engineering: Towards the encoded synthesis of unnatural polymers
    • Loakes D., & Holliger P. Polymerase engineering: towards the encoded synthesis of unnatural polymers. Chem. Commun. 4619-4631 (2009
    • (2009) Chem. Commun , pp. 4619-4631
    • Loakes, D.1    Holliger, P.2
  • 11
    • 84892371909 scopus 로고    scopus 로고
    • Directed polymerase evolution
    • Chen T., & Romesberg F. E. Directed polymerase evolution. FEBS Lett. 588, 219-229 (2014
    • (2014) FEBS Lett , vol.588 , pp. 219-229
    • Chen, T.1    Romesberg, F.E.2
  • 12
    • 0035836707 scopus 로고    scopus 로고
    • Directed evolution of polymerase function by compartmentalized self-replication
    • Ghadessy F. J., Ong J. L., & Holliger P. Directed evolution of polymerase function by compartmentalized self-replication. Proc. Natl Acad. Sci. USA 98, 4552-4557 (2001
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 4552-4557
    • Ghadessy, F.J.1    Ong, J.L.2    Holliger, P.3
  • 13
    • 68049106179 scopus 로고    scopus 로고
    • Directed evolution drives the next generation of biocatalysts
    • Turner N. J. Directed evolution drives the next generation of biocatalysts. Nat. Chem. Biol. 5, 567-573 (2009
    • (2009) Nat. Chem. Biol , vol.5 , pp. 567-573
    • Turner, N.J.1
  • 14
    • 0033908031 scopus 로고    scopus 로고
    • Man-made enzymes-from design to in vitro compartmentalization
    • Griffiths A. D., & Tawfik D. S. Man-made enzymes-from design to in vitro compartmentalization. Curr. Opin. Biotechnol. 11, 338-353 (2000
    • (2000) Curr. Opin. Biotechnol , vol.11 , pp. 338-353
    • Griffiths, A.D.1    Tawfik, D.S.2
  • 15
    • 0031854986 scopus 로고    scopus 로고
    • Man-made cell-like compartments for molecular evolution
    • Tawfik D. S., & Griffiths A. D. Man-made cell-like compartments for molecular evolution. Nat. Biotechnol. 16, 652-656 (1998
    • (1998) Nat. Biotechnol , vol.16 , pp. 652-656
    • Tawfik, D.S.1    Griffiths, A.D.2
  • 16
    • 85047289331 scopus 로고    scopus 로고
    • A simple method to evaluate the biochemical compatability of oil/surfactant mixtures for experiements in microdroplets
    • Kaltenbach M., Devenish S. R., & Hollfelder F. A simple method to evaluate the biochemical compatability of oil/surfactant mixtures for experiements in microdroplets. Lab Chip 12, 4185-4192 (2012
    • (2012) Lab Chip , vol.12 , pp. 4185-4192
    • Kaltenbach, M.1    Devenish, S.R.2    Hollfelder, F.3
  • 17
    • 0037455351 scopus 로고    scopus 로고
    • Formation of dispersions using 'flow focusing' in microchannels
    • Anna S. L., Bontoux N., & Stone H. A. Formation of dispersions using 'flow focusing' in microchannels. Appl. Phys. Lett. 82, 364-366 (2003
    • (2003) Appl. Phys. Lett , vol.82 , pp. 364-366
    • Anna, S.L.1    Bontoux, N.2    Stone, H.A.3
  • 18
    • 0033640011 scopus 로고    scopus 로고
    • Monodisperse emulsion generation via drop break off in a coflowing stream
    • Umbanhowar P. B., Prasad V., & Weitz D. A. Monodisperse emulsion generation via drop break off in a coflowing stream. Langmuir 16, 347-351 (2000
    • (2000) Langmuir , vol.16 , pp. 347-351
    • Umbanhowar, P.B.1    Prasad, V.2    Weitz, D.A.3
  • 19
    • 77749270677 scopus 로고    scopus 로고
    • Ultrahigh-throughput screening in drop-based microfluidics for directed evolution
    • Agresti J. J., et al. Ultrahigh-throughput screening in drop-based microfluidics for directed evolution. Proc. Natl Acad. Sci. USA 107, 4004-4009 (2010
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 4004-4009
    • Agresti, J.J.1
  • 20
    • 84893020696 scopus 로고    scopus 로고
    • High-throughput screening for industrial enzyme production hosts by droplet microfluidics
    • Sjostrom S. L., et al. High-throughput screening for industrial enzyme production hosts by droplet microfluidics. Lab Chip 14, 806-813 (2014
    • (2014) Lab Chip , vol.14 , pp. 806-813
    • Sjostrom, S.L.1
  • 21
    • 84906549486 scopus 로고    scopus 로고
    • Evolution of enzyme catalysts caged in biomimetic gel-shell beads
    • Fischlechner M., et al. Evolution of enzyme catalysts caged in biomimetic gel-shell beads. Nat. Chem. 6, 791-796 (2014
    • (2014) Nat. Chem , vol.6 , pp. 791-796
    • Fischlechner, M.1
  • 22
    • 0037020347 scopus 로고    scopus 로고
    • A molecular beacon for quantitative monitoring of the DNA polymerase reaction in real-time
    • Summerer D., & Marx A. A molecular beacon for quantitative monitoring of the DNA polymerase reaction in real-time. Angew. Chem. Int. Ed. 31, 3620-3622 (2002
    • (2002) Angew. Chem. Int. Ed. , vol.31 , pp. 3620-3622
    • Summerer, D.1    Marx, A.2
  • 23
    • 71049146040 scopus 로고    scopus 로고
    • A real-time fluorescence method for enzymatic characterization of specialized humn DNA polymerases
    • Dorjsuren D., et al. A real-time fluorescence method for enzymatic characterization of specialized humn DNA polymerases. Nucleic Acids Res. 37, e128 (2009
    • (2009) Nucleic Acids Res , vol.37 , pp. e128
    • Dorjsuren, D.1
  • 24
    • 36049004653 scopus 로고    scopus 로고
    • Selection of fluorophore and quencher pairs for fluorescent nucleic acid hybridization probes
    • Marras S. Selection of fluorophore and quencher pairs for fluorescent nucleic acid hybridization probes. Methods Mol. Biol. 335, 3-16 (2006
    • (2006) Methods Mol. Biol , vol.335 , pp. 3-16
    • Marras, S.1
  • 25
    • 84971232016 scopus 로고    scopus 로고
    • Improving polymerase activity with unnatural substrates by sampling mutations in homologous protein architectures
    • Dunn M. R., Otto C., Fenton K. E., & Chaput J. C. Improving polymerase activity with unnatural substrates by sampling mutations in homologous protein architectures. ACS Chem. Biol. doi: 10.1021/acshembio.5b00949 (2016
    • (2016) ACS Chem. Biol
    • Dunn, M.R.1    Otto, C.2    Fenton, K.E.3    Chaput, J.C.4
  • 26
    • 79951620951 scopus 로고    scopus 로고
    • Unlocking the sugar 'steric gate' of DNA polymerases
    • Brown J. A., & Suo Z. Unlocking the sugar 'steric gate' of DNA polymerases. Biochemistry 50, 1135-1142 (2011
    • (2011) Biochemistry , vol.50 , pp. 1135-1142
    • Brown, J.A.1    Suo, Z.2
  • 27
    • 84900653348 scopus 로고    scopus 로고
    • One in a million: Flow cytometric sorting of single cell-lysate assays in monodisperse picoliter double emulsion droplets for directed evolution
    • Zinchenko A., et al. One in a million: flow cytometric sorting of single cell-lysate assays in monodisperse picoliter double emulsion droplets for directed evolution. Anal. Chem. 86, 2526-2533 (2014
    • (2014) Anal. Chem , vol.86 , pp. 2526-2533
    • Zinchenko, A.1
  • 28
    • 0034680801 scopus 로고    scopus 로고
    • Chemical etiology of nucleic acid structure: The alpha-threofuranosyl-(3'-42′) oligonucleotide system
    • Schoning K. U., et al. Chemical etiology of nucleic acid structure: the alpha-threofuranosyl-(3'-42′) oligonucleotide system. Science 290, 1347-1351 (2000
    • (2000) Science , vol.290 , pp. 1347-1351
    • Schoning, K.U.1
  • 29
    • 84926355512 scopus 로고    scopus 로고
    • Therminator-mediated synthesis of unbiased TNA polymers requires 7-deazaguanine to suppress G-G mispairing during TNA transcription
    • Dunn M. R., et al. Therminator-mediated synthesis of unbiased TNA polymers requires 7-deazaguanine to suppress G-G mispairing during TNA transcription. J. Am. Chem. Soc. 137, 4014-4017 (2015
    • (2015) J. Am. Chem. Soc , vol.137 , pp. 4014-4017
    • Dunn, M.R.1
  • 30
    • 0006962619 scopus 로고
    • Effect of manganese ions on the incorporation of dideoxynucleotides by bacteriophage T7 DNA polymerase and Escherichia coli DNA polymerase i
    • Tabor S., & Richardson C. C. Effect of manganese ions on the incorporation of dideoxynucleotides by bacteriophage T7 DNA polymerase and Escherichia coli DNA polymerase I. Proc. Natl Acad. Sci. USA 86, 4076-4080 (1989
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 4076-4080
    • Tabor, S.1    Richardson, C.C.2
  • 32
    • 84961636998 scopus 로고    scopus 로고
    • A scalable synthesis of a-L-threose nucleic acid monomers
    • Sau S. P., Fahmi N. E., Liao J.-Y., Bala S., & Chaput J. C. A scalable synthesis of a-L-threose nucleic acid monomers. J. Org. Chem 81, 2302-2307 (2016
    • (2016) J. Org. Chem , vol.81 , pp. 2302-2307
    • Sau, S.P.1    Fahmi, N.E.2    Liao, J.-Y.3    Bala, S.4    Chaput, J.C.5
  • 33
    • 84880733476 scopus 로고    scopus 로고
    • Synthesis of threose nucleic acid (TNA) triphosphates and oligonucleotides by polymerase-mediated primer extension
    • Zhang S., Yu H., & Chaput J. C. Synthesis of threose nucleic acid (TNA) triphosphates and oligonucleotides by polymerase-mediated primer extension. Curr. Protoc. Nucleic Acid Chem. 52 4.54 (2013
    • (2013) Curr. Protoc. Nucleic Acid Chem , vol.52 , pp. 454
    • Zhang, S.1    Yu, H.2    Chaput, J.C.3
  • 35
    • 0033581011 scopus 로고    scopus 로고
    • DNA polymerases: Structural diversity and common mechanisms
    • Steitz T. A. DNA polymerases: structural diversity and common mechanisms. J. Biol. Chem. 274, 17395-17398 (1999
    • (1999) J. Biol. Chem , vol.274 , pp. 17395-17398
    • Steitz, T.A.1
  • 36
    • 84931291559 scopus 로고    scopus 로고
    • Dissecting enzyme function with microfluidic-based deep mutational scanning
    • Romero P. A., Tran T. M., & Abate A. R. Dissecting enzyme function with microfluidic-based deep mutational scanning. Proc. Natl Acad. Sci. USA 112, 7159-7164 (2015
    • (2015) Proc. Natl Acad. Sci. USA , vol.112 , pp. 7159-7164
    • Romero, P.A.1    Tran, T.M.2    Abate, A.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.