메뉴 건너뛰기




Volumn 9, Issue 11, 2014, Pages

Thermostable artificial enzyme isolated by in vitro selection

Author keywords

[No Author keywords available]

Indexed keywords

LIGASE; LIGASE 10C; MESSENGER RNA; UNCLASSIFIED DRUG; RNA;

EID: 84911887107     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0112028     Document Type: Article
Times cited : (10)

References (43)
  • 2
    • 70349901079 scopus 로고    scopus 로고
    • Stability effects of mutations and protein evolvability
    • Tokuriki N, Tawfik DS (2009) Stability effects of mutations and protein evolvability. Curr Opin Struct Biol 19: 596-604.
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 596-604
    • Tokuriki, N.1    Tawfik, D.S.2
  • 4
    • 84880120249 scopus 로고    scopus 로고
    • Stabilizing biocatalysts
    • Bommarius AS, Paye MF (2013) Stabilizing biocatalysts. Chem Soc Rev 42: 6534-6565.
    • (2013) Chem Soc Rev , vol.42 , pp. 6534-6565
    • Bommarius, A.S.1    Paye, M.F.2
  • 5
    • 84881105793 scopus 로고    scopus 로고
    • Structure- And sequence-Analysis inspired engineering of proteins for enhanced thermostability
    • Wijma HJ, Floor RJ, Janssen DB (2013) Structure- And sequence-Analysis inspired engineering of proteins for enhanced thermostability. Curr Opin Struct Biol 23: 588-594.
    • (2013) Curr Opin Struct Biol , vol.23 , pp. 588-594
    • Wijma, H.J.1    Floor, R.J.2    Janssen, D.B.3
  • 6
    • 70450242805 scopus 로고    scopus 로고
    • Exploring protein fitness landscapes by directed evolution
    • Romero PA, Arnold FH (2009) Exploring protein fitness landscapes by directed evolution. Nat Rev Mol Cell Biol 10: 866-876.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 866-876
    • Romero, P.A.1    Arnold, F.H.2
  • 8
    • 84908575740 scopus 로고    scopus 로고
    • Directed evolution of novel proteins
    • Lane MD, Seelig B (2014) Directed evolution of novel proteins. Curr Opin Chem Biol 22: 129-126.
    • (2014) Curr Opin Chem Biol , vol.22 , pp. 129-126
    • Lane, M.D.1    Seelig, B.2
  • 9
    • 0035130371 scopus 로고    scopus 로고
    • Protein solubility and folding monitored in vivo by structural complementation of a genetic marker protein
    • Wigley WC, Stidham RD, Smith NM, Hunt JF, Thomas PJ (2001) Protein solubility and folding monitored in vivo by structural complementation of a genetic marker protein. Nat Biotechnol 19: 131-136.
    • (2001) Nat Biotechnol , vol.19 , pp. 131-136
    • Wigley, W.C.1    Stidham, R.D.2    Smith, N.M.3    Hunt, J.F.4    Thomas, P.J.5
  • 11
    • 0035827175 scopus 로고    scopus 로고
    • In vitro selection of highly stabilized protein variants with optimized surface
    • Martin A, Sieber V, Schmid FX (2001) In vitro selection of highly stabilized protein variants with optimized surface. J Mol Biol 309: 717-726.
    • (2001) J Mol Biol , vol.309 , pp. 717-726
    • Martin, A.1    Sieber, V.2    Schmid, F.X.3
  • 12
    • 0031729179 scopus 로고    scopus 로고
    • Selecting proteins with improved stability by a phage-based method
    • Sieber V, Pluckthun A, Schmid FX (1998) Selecting proteins with improved stability by a phage-based method. Nat Biotechnol 16: 955-960.
    • (1998) Nat Biotechnol , vol.16 , pp. 955-960
    • Sieber, V.1    Pluckthun, A.2    Schmid, F.X.3
  • 13
    • 84886585247 scopus 로고    scopus 로고
    • Modulating protein stability - directed evolution strategies for improved protein function
    • Socha RD, Tokuriki N (2013) Modulating protein stability - directed evolution strategies for improved protein function. FEBS J 280: 5582-5595.
    • (2013) FEBS J , vol.280 , pp. 5582-5595
    • Socha, R.D.1    Tokuriki, N.2
  • 15
    • 79959733138 scopus 로고    scopus 로고
    • Lessons about protein stability from in vitro selections
    • Schmid FX (2011) Lessons about protein stability from in vitro selections. Chembiochem 12: 1501-1507.
    • (2011) Chembiochem , vol.12 , pp. 1501-1507
    • Schmid, F.X.1
  • 17
    • 34547958191 scopus 로고    scopus 로고
    • Selection and evolution of enzymes from a partially randomized non-catalytic scaffold
    • Seelig B, Szostak JW (2007) Selection and evolution of enzymes from a partially randomized non-catalytic scaffold. Nature 448: 828-831.
    • (2007) Nature , vol.448 , pp. 828-831
    • Seelig, B.1    Szostak, J.W.2
  • 18
    • 0030817279 scopus 로고    scopus 로고
    • RNA-peptide fusions for the in vitro selection of peptides and proteins
    • Roberts RW, Szostak JW (1997) RNA-peptide fusions for the in vitro selection of peptides and proteins. Proc Natl Acad Sci USA 94: 12297-12302.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12297-12302
    • Roberts, R.W.1    Szostak, J.W.2
  • 19
    • 0031559943 scopus 로고    scopus 로고
    • In vitro virus: Bonding of mRNA bearing puromycin at the 39-Terminal end to the C-Terminal end of its encoded protein on the ribosome in vitro
    • Nemoto N, MiyamotoSato E, Husimi Y, Yanagawa H (1997) In vitro virus: Bonding of mRNA bearing puromycin at the 39-Terminal end to the C-Terminal end of its encoded protein on the ribosome in vitro. FEBS Lett 414: 405-408.
    • (1997) FEBS Lett , vol.414 , pp. 405-408
    • Nemoto, N.1    MiyamotoSato, E.2    Husimi, Y.3    Yanagawa, H.4
  • 20
    • 84872684145 scopus 로고    scopus 로고
    • Structure and dynamics of a primordial catalytic fold generated by in vitro evolution
    • Chao F-A, Morelli A, Haugner JC, III, Churchfield L, Hagmann LN, et al. (2013) Structure and dynamics of a primordial catalytic fold generated by in vitro evolution. Nat Chem Biol 9: 81-83.
    • (2013) Nat Chem Biol , vol.9 , pp. 81-83
    • Chao, F.-A.1    Morelli, A.2    Haugner, J.C.3    Churchfield, L.4    Hagmann, L.N.5
  • 21
    • 84883510320 scopus 로고    scopus 로고
    • Universal labeling of 59-Triphosphate RNAs by artificial RNA ligase enzyme with broad substrate specificity
    • Haugner III JC, Seelig B (2013) Universal labeling of 59-Triphosphate RNAs by artificial RNA ligase enzyme with broad substrate specificity. Chem Commun 49: 7322-7324.
    • (2013) Chem Commun , vol.49 , pp. 7322-7324
    • Haugner, J.C.1    Seelig, B.2
  • 22
    • 79960062888 scopus 로고    scopus 로고
    • MRNA display for the selection and evolution of enzymes from in vitro-Translated protein libraries
    • Seelig B (2011) mRNA display for the selection and evolution of enzymes from in vitro-Translated protein libraries. Nat Protocols 6: 540-552.
    • (2011) Nat Protocols , vol.6 , pp. 540-552
    • Seelig, B.1
  • 23
    • 0026680843 scopus 로고
    • Site-specific modification of pre-mRNA: The 29- hydroxyl groups at the splice sites
    • Moore MJ, Sharp PA (1992) Site-specific modification of pre-mRNA: The 29- hydroxyl groups at the splice sites. Science 256: 992-997.
    • (1992) Science , vol.256 , pp. 992-997
    • Moore, M.J.1    Sharp, P.A.2
  • 24
    • 34548819311 scopus 로고    scopus 로고
    • Using circular dichroism collected as a function of temperature to determine the thermodynamics of protein unfolding and binding interactions
    • Greenfield NJ (2006) Using circular dichroism collected as a function of temperature to determine the thermodynamics of protein unfolding and binding interactions. Nat Protoc 1: 2527-2535.
    • (2006) Nat Protoc , vol.1 , pp. 2527-2535
    • Greenfield, N.J.1
  • 25
    • 84860389087 scopus 로고    scopus 로고
    • Computational design and selections for an engineered, thermostable terpene synthase
    • Diaz JE, Lin C-S, Kunishiro K, Feld BK, Avrantinis SK, et al. (2011) Computational design and selections for an engineered, thermostable terpene synthase. Protein Sci 20: 1597-1606.
    • (2011) Protein Sci , vol.20 , pp. 1597-1606
    • Diaz, J.E.1    Lin, C.-S.2    Kunishiro, K.3    Feld, B.K.4    Avrantinis, S.K.5
  • 26
    • 70350110646 scopus 로고    scopus 로고
    • Creation of an amino acid network of structurally coupled residues in the directed evolution of a thermostable enzyme
    • Reetz MT, Soni P, Acevedo JP, Sanchis J (2009) Creation of an amino acid network of structurally coupled residues in the directed evolution of a thermostable enzyme. Angew Chem Int Ed Engl 48: 8268-8272.
    • (2009) Angew Chem Int Ed Engl , vol.48 , pp. 8268-8272
    • Reetz, M.T.1    Soni, P.2    Acevedo, J.P.3    Sanchis, J.4
  • 28
    • 37249032102 scopus 로고    scopus 로고
    • Dynamic personalities of proteins
    • Henzler-Wildman K, Kern D (2007) Dynamic personalities of proteins. Nature 450: 964-972.
    • (2007) Nature , vol.450 , pp. 964-972
    • Henzler-Wildman, K.1    Kern, D.2
  • 30
    • 82455175792 scopus 로고    scopus 로고
    • Evolutionarily conserved linkage between enzyme fold, flexibility, and catalysis
    • Ramanathan A, Agarwal PK (2011) Evolutionarily conserved linkage between enzyme fold, flexibility, and catalysis. PLoS Biol 9.
    • (2011) PLoS Biol , vol.9
    • Ramanathan, A.1    Agarwal, P.K.2
  • 31
    • 0032526414 scopus 로고    scopus 로고
    • Lactate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima: The crystal structure at 2.1 A resolution reveals strategies for intrinsic protein stabilization
    • Auerbach G, Ostendorp R, Prade L, Korndorfer I, Dams T, et al. (1998) Lactate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima: The crystal structure at 2.1 A resolution reveals strategies for intrinsic protein stabilization. Structure 6: 769-781.
    • (1998) Structure , vol.6 , pp. 769-781
    • Auerbach, G.1    Ostendorp, R.2    Prade, L.3    Korndorfer, I.4    Dams, T.5
  • 32
    • 0032521220 scopus 로고    scopus 로고
    • Structural adaptations of the cold-Active citrate synthase from an Antarctic bacterium
    • Russell RJ, Gerike U, Danson MJ, Hough DW, Taylor GL (1998) Structural adaptations of the cold-Active citrate synthase from an Antarctic bacterium. Structure 6: 351-361.
    • (1998) Structure , vol.6 , pp. 351-361
    • Russell, R.J.1    Gerike, U.2    Danson, M.J.3    Hough, D.W.4    Taylor, G.L.5
  • 34
    • 0030589056 scopus 로고    scopus 로고
    • Small structural changes account for the high thermostability of 1[4Fe-4S] ferredoxin from the hyperthermophilic bacterium Thermotoga maritima
    • Macedo-Ribeiro S, Darimont B, Sterner R, Huber R (1996) Small structural changes account for the high thermostability of 1[4Fe-4S] ferredoxin from the hyperthermophilic bacterium Thermotoga maritima. Structure 4: 1291-1301.
    • (1996) Structure , vol.4 , pp. 1291-1301
    • Macedo-Ribeiro, S.1    Darimont, B.2    Sterner, R.3    Huber, R.4
  • 37
    • 77953911271 scopus 로고    scopus 로고
    • De novo enzymes: From computational design to mRNA display
    • Golynskiy MV, Seelig B (2010) De novo enzymes: From computational design to mRNA display. Trends Biotechnol 28: 340-345.
    • (2010) Trends Biotechnol , vol.28 , pp. 340-345
    • Golynskiy, M.V.1    Seelig, B.2
  • 38
    • 84883164633 scopus 로고    scopus 로고
    • Highly diverse protein library based on the ubiquitous (b/a)8 enzyme fold yields well-structured proteins through in vitro folding selection
    • Golynskiy MV, Haugner JC, Seelig B (2013) Highly diverse protein library based on the ubiquitous (b/a)8 enzyme fold yields well-structured proteins through in vitro folding selection. ChemBioChem 14: 1553-1563.
    • (2013) ChemBioChem , vol.14 , pp. 1553-1563
    • Golynskiy, M.V.1    Haugner, J.C.2    Seelig, B.3
  • 39
    • 3042693137 scopus 로고    scopus 로고
    • Evolutionary optimization of a nonbiological ATP binding protein for improved folding stability
    • Chaput JC, Szostak JW (2004) Evolutionary optimization of a nonbiological ATP binding protein for improved folding stability. Chem Biol 11: 865-874.
    • (2004) Chem Biol , vol.11 , pp. 865-874
    • Chaput, J.C.1    Szostak, J.W.2
  • 40
    • 55849103128 scopus 로고    scopus 로고
    • Structural insights into the evolution of a non-biological protein: Importance of surface residues in protein fold optimization
    • Smith MD, Rosenow MA, Wang MT, Allen JP, Szostak JW, et al. (2007) Structural insights into the evolution of a non-biological protein: Importance of surface residues in protein fold optimization. PLoS ONE 2.
    • (2007) PLoS ONE , vol.2
    • Smith, M.D.1    Rosenow, M.A.2    Wang, M.T.3    Allen, J.P.4    Szostak, J.W.5
  • 41
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit: A user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT
    • Hall TA (1999) BioEdit: A user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucleic Acids Symp Ser 41: 95-98.
    • (1999) Nucleic Acids Symp Ser , vol.41 , pp. 95-98
    • Hall, T.A.1
  • 42
    • 0027968068 scopus 로고
    • CLUSTAL-W - improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ (1994) CLUSTAL-W - improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22: 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 43
    • 32844460390 scopus 로고    scopus 로고
    • Directed evolution of ATP binding proteins from a zinc finger domain by using mRNA display
    • Cho GS, Szostak JW (2006) Directed evolution of ATP binding proteins from a zinc finger domain by using mRNA display. Chem Biol 13: 139-147.
    • (2006) Chem Biol , vol.13 , pp. 139-147
    • Cho, G.S.1    Szostak, J.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.