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Volumn 805, Issue , 2012, Pages 349-365

Update on pure translation display with unnatural amino acid incorporation

Author keywords

In vitro directed evolution; In vitro selection; Ligand and drug discovery; mRNA display; Peptide; Peptidomimetic; Protein synthesis; Pure translation; Ribosome display; TRNA; Unnatural amino acid

Indexed keywords

AMINO ACID; PEPTIDE;

EID: 84555189972     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-61779-379-0_20     Document Type: Article
Times cited : (10)

References (44)
  • 2
    • 0028592703 scopus 로고
    • An in vitro polysome display system for identifying ligands from very large peptide libraries
    • Mattheakis LC, Bhatt RR, Dower WJ. (1994) An in vitro polysome display system for identifying ligands from very large peptide libraries. PNAS 91, 9022-9026.
    • (1994) PNAS , vol.91 , pp. 9022-9026
    • Mattheakis, L.C.1    Bhatt, R.R.2    Dower, W.J.3
  • 4
    • 33847612165 scopus 로고    scopus 로고
    • In vitro selection and evolution of protein-ligand interactions by ribosome display
    • Golemis E, Adams P, eds : Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Schaffi tzel C, Zahnd C, Amstutz P, Luginbühl B, Plückthun A. (2005) In vitro selection and evolution of protein-ligand interactions by ribosome display. In Golemis E, Adams P, eds : Protein-protein interaction: A molecular cloning manual 2nd edn. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY 517-548.
    • (2005) Protein-protein Interaction: A Molecular Cloning Manual 2nd Edn , pp. 517-548
    • Schaffi Tzel, C.1    Zahnd, C.2    Amstutz, P.3    Luginbühl, B.4    Plückthun, A.5
  • 5
    • 3142685154 scopus 로고    scopus 로고
    • In-vitro protein evolution by ribosome display and mRNA display
    • DOI 10.1016/j.jim.2004.04.008, PII S0022175904001309
    • Lipovsek D, Pluckthun A. (2004) In-vitro protein evolution by ribosome display and mRNA display. Journal of Immunological Methods 290, 51-67. (Pubitemid 38917130)
    • (2004) Journal of Immunological Methods , vol.290 , Issue.1-2 , pp. 51-67
    • Lipovsek, D.1    Pluckthun, A.2
  • 6
    • 0031559943 scopus 로고    scopus 로고
    • In vitro virus: Bonding of mRNA bearing puromycin at the 3'-terminal end to the C-terminal end of its encoded protein on the ribosome in vitro
    • DOI 10.1016/S0014-5793(97)01026-0, PII S0014579397010260
    • Nemoto N, Miyamoto-Sato E, Husimi Y, Yanagawa H. (1997) In vitro virus: Bonding of mRNA bearing puromycin at the 3 -terminal end to the C-terminal end of its encoded protein on the ribosome in vitro. FEBS Lett 414, 405-408. (Pubitemid 27389405)
    • (1997) FEBS Letters , vol.414 , Issue.2 , pp. 405-408
    • Nemoto, N.1    Miyamoto-Sato, E.2    Husimi, Y.3    Yanagawa, H.4
  • 9
    • 0035477877 scopus 로고    scopus 로고
    • A simplified reconstitution of mRNA-directed peptide synthesis: Activity of the epsilon enhancer and an unnatural amino acid
    • DOI 10.1006/abio.2001.5329
    • Forster AC, Weissbach H, Blacklow SC. (2001) A Simplifi ed Reconstitution of mRNA-Directed Peptide Synthesis: Activity of the Epsilon Enhancer and an Unnatural Amino Acid. Analytical Biochemistry 297, 60-70. (Pubitemid 32939274)
    • (2001) Analytical Biochemistry , vol.297 , Issue.1 , pp. 60-70
    • Forster, A.C.1    Weissbach, H.2    Blacklow, S.C.3
  • 11
    • 0037189891 scopus 로고    scopus 로고
    • In vitro selection of mRNA display libraries containing an unnatural amino acid
    • DOI 10.1021/ja026789q
    • Li S, Millward S, Roberts R. (2002) In Vitro Selection of mRNA Display Libraries Containing an Unnatural Amino Acid. JACS 124, 9972-9973. (Pubitemid 34919718)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.34 , pp. 9972-9973
    • Li, S.1    Millward, S.2    Roberts, R.3
  • 12
    • 0345531149 scopus 로고    scopus 로고
    • Encodamers: Unnatural peptide oligomers encoded in RNA
    • DOI 10.1016/j.chembiol.2003.11.004
    • Frankel A, Millward SW, Roberts RW. (2003) Encodamers: Unnatural Peptide Oligomers Encoded in RNA. Chemistry and Biology 10, 1043-1050. (Pubitemid 37496434)
    • (2003) Chemistry and Biology , vol.10 , Issue.11 , pp. 1043-1050
    • Frankel, A.1    Millward, S.W.2    Roberts, R.W.3
  • 13
    • 4644254373 scopus 로고    scopus 로고
    • Pure translation display
    • DOI 10.1016/j.ab.2004.06.028, PII S0003269704005457
    • Forster AC, Cornish VW, Blacklow SC. (2004) Pure Translation Display. Analytical Biochemistry 333, 358-364. (Pubitemid 39278060)
    • (2004) Analytical Biochemistry , vol.333 , Issue.2 , pp. 358-364
    • Forster, A.C.1    Cornish, V.W.2    Blacklow, S.C.3
  • 15
    • 77957345108 scopus 로고    scopus 로고
    • Update on designing and building minimal cells
    • Jewett MC, Forster AC. (2010) Update on designing and building minimal cells. Curr. Op. Biotech. 21, 697-703.
    • (2010) Curr. Op. Biotech. , vol.21 , pp. 697-703
    • Jewett, M.C.1    Forster, A.C.2
  • 16
    • 33745727452 scopus 로고    scopus 로고
    • Highly Efficient ribosome display selection by use of purifi ed components for in vitro translation
    • Villemagne D, Jackson R, Douthwaite JA. (2006) Highly Efficient ribosome display selection by use of purifi ed components for in vitro translation. Journal of Immunological Methods 313, 140-148.
    • (2006) Journal of Immunological Methods , vol.313 , pp. 140-148
    • Villemagne, D.1    Jackson, R.2    Douthwaite, J.A.3
  • 17
    • 33751410139 scopus 로고    scopus 로고
    • Efficient protein selection based on ribosome display system with purified components
    • DOI 10.1016/j.bbrc.2006.11.017, PII S0006291X06024867
    • Ohashi H, Shimizu Y, Ying BW, Ueda T. (2007) Efficient protein selection based on ribosome display system with purifi ed components. Biochemical and Biophysical Research Communications 352, 270-276. (Pubitemid 44821125)
    • (2007) Biochemical and Biophysical Research Communications , vol.352 , Issue.1 , pp. 270-276
    • Ohashi, H.1    Shimizu, Y.2    Ying, B.-W.3    Ueda, T.4
  • 18
    • 66749151526 scopus 로고    scopus 로고
    • Epitope Mapping Using Ribosome Display in a Reconstituted Cell-Free Protein Synthesis System
    • Osada E, Shimizu Y, Akbar BK, Kanamori T, Ueda T. (2009) Epitope Mapping Using Ribosome Display in a Reconstituted Cell-Free Protein Synthesis System. Journal of Biochemistry 145, 693-700.
    • (2009) Journal of Biochemistry , vol.145 , pp. 693-700
    • Osada, E.1    Shimizu, Y.2    Akbar, B.K.3    Kanamori, T.4    Ueda, T.5
  • 19
    • 38649143198 scopus 로고    scopus 로고
    • Compensatory Evolution of a WW Domain Variant Lacking the Strictly Conserved Trp Residue
    • Yanagida H, Matsuura T, Yomo T. (2007) Compensatory Evolution of a WW Domain Variant Lacking the Strictly Conserved Trp Residue. Journal of Molecular Evolution 66, 61-71.
    • (2007) Journal of Molecular Evolution , vol.66 , pp. 61-71
    • Yanagida, H.1    Matsuura, T.2    Yomo, T.3
  • 20
    • 23044489674 scopus 로고    scopus 로고
    • De novo genetic codes and pure translation display
    • DOI 10.1016/j.ymeth.2005.04.011, PII S1046202305000873, Engineering Translation
    • Tan Z, Blacklow SC, Cornish VW, Forster AC. (2005) De novo genetic codes and pure translation display. Methods 36, 279-290. (Pubitemid 41074959)
    • (2005) Methods , vol.36 , Issue.3 , pp. 279-290
    • Tan, Z.1    Blacklow, S.C.2    Cornish, V.W.3    Forster, A.C.4
  • 21
    • 0000932115 scopus 로고
    • A general and efficient route for chemical aminoacylation of transfer RNAs
    • Robertson SA, Ellman JA, Schultz PG. (1991) A General and Efficient Route for Chemical Aminoacylation of Transfer RNAs. JACS 113, 2722-2729.
    • (1991) JACS , vol.113 , pp. 2722-2729
    • Robertson, S.A.1    Ellman, J.A.2    Schultz, P.G.3
  • 22
    • 33646044708 scopus 로고    scopus 로고
    • A highly fl exible tRNA acylation method for non-natural polypeptide synthesis
    • Murakami H, Ohta A, Ashigai H, Suga H. (2006) A highly fl exible tRNA acylation method for non-natural polypeptide synthesis. Nature Methods 3, 357-359.
    • (2006) Nature Methods , vol.3 , pp. 357-359
    • Murakami, H.1    Ohta, A.2    Ashigai, H.3    Suga, H.4
  • 23
    • 1942445134 scopus 로고    scopus 로고
    • Transformation of aminoacyl tRNAs for the in vitro selection of "drug-like" molecules
    • DOI 10.1016/j.chembiol.2004.03.009, PII S1074552104000857
    • Merryman C, Green R. (2004) Transformation of Aminoacyl tRNAs for the In Vitro Selection of "Drug-like" Molecules. Chemistry and Biology 11, 575-582. (Pubitemid 38503589)
    • (2004) Chemistry and Biology , vol.11 , Issue.4 , pp. 575-582
    • Merryman, C.1    Green, R.2
  • 24
    • 33645298531 scopus 로고    scopus 로고
    • Enzymatic aminoacylation of tRNA with unnatural amino acids
    • Hartman MCT, Josephson K, Szostak JW. (2006) Enzymatic aminoacylation of tRNA with unnatural amino acids. PNAS 103, 4356-4361.
    • (2006) PNAS , vol.103 , pp. 4356-4361
    • Hartman, M.C.T.1    Josephson, K.2    Szostak, J.W.3
  • 25
    • 43049128964 scopus 로고    scopus 로고
    • An expanded set of amino acid analogs for the ribosomal translation of unnatural peptides
    • Hartman MCT, Josephson K, Lin CW, Szostak JW. (2007) An Expanded Set of Amino Acid Analogs for the Ribosomal Translation of Unnatural Peptides. PLoS ONE 2, e972.
    • (2007) PLoS ONE , vol.2
    • Hartman, M.C.T.1    Josephson, K.2    Lin, C.W.3    Szostak, J.W.4
  • 26
    • 77954943220 scopus 로고    scopus 로고
    • Aminoacyl transfer rate dictates choice of editing pathway in threonyl-tRNA synthetase
    • Minajigi A, Francklyn CS. (2010) Aminoacyl Transfer Rate Dictates Choice of Editing Pathway in Threonyl-tRNA Synthetase. Journal of Biological Chemistry 285, 23810-23817.
    • (2010) Journal of Biological Chemistry , vol.285 , pp. 23810-23817
    • Minajigi, A.1    Francklyn, C.S.2
  • 28
    • 67649888367 scopus 로고    scopus 로고
    • Low modularity of aminoacyl-tRNA substrates in polymerization by the ribosome
    • Forster AC. (2009) Low modularity of aminoacyl-tRNA substrates in polymerization by the ribosome. Nucleic Acids Research 37, 3747-3755.
    • (2009) Nucleic Acids Research , vol.37 , pp. 3747-3755
    • Forster, A.C.1
  • 29
    • 58049219079 scopus 로고    scopus 로고
    • Ribosomal synthesis of polypeptoids and peptoid-peptide hybrids
    • Kawakami T, Murakami H, Suga H. (2008) Ribosomal Synthesis of Polypeptoids and Peptoid-Peptide Hybrids. JACS 130, 16861-16863.
    • (2008) JACS , vol.130 , pp. 16861-16863
    • Kawakami, T.1    Murakami, H.2    Suga, H.3
  • 30
    • 38349062552 scopus 로고    scopus 로고
    • Messenger RNA-programmed incorporation of multiple n-methyl-amino acids into linear and cyclic peptides
    • Kawakami T, Murakami H, Suga H. (2008) Messenger RNA-Programmed Incorporation of Multiple N-Methyl-Amino Acids into Linear and Cyclic Peptides. Chemistry and Biology 15, 32-42.
    • (2008) Chemistry and Biology , vol.15 , pp. 32-42
    • Kawakami, T.1    Murakami, H.2    Suga, H.3
  • 31
    • 37149000703 scopus 로고    scopus 로고
    • Synthesis of Polyester by Means of Genetic Code Reprogramming
    • DOI 10.1016/j.chembiol.2007.10.015, PII S1074552107003705
    • Ohta A, Murakami H, Higashimura E, Suga H. (2007) Synthesis of Polyester by Means of Genetic Code Reprogramming. Chemistry and Biology 14, 1315-1322. (Pubitemid 350257006)
    • (2007) Chemistry and Biology , vol.14 , Issue.12 , pp. 1315-1322
    • Ohta, A.1    Murakami, H.2    Higashimura, E.3    Suga, H.4
  • 32
    • 0035986704 scopus 로고    scopus 로고
    • A bifunctional tRNA for in vitro selection
    • DOI 10.1016/S1074-5521(02)00161-8, PII S1074552102001618
    • Merryman C, Weinstein E, Wnuk SF, Bartel DP. (2002) A Bifunctional tRNA for In Vitro Selection. Chemistry and Biology 9, 741-746. (Pubitemid 34653069)
    • (2002) Chemistry and Biology , vol.9 , Issue.6 , pp. 741-746
    • Merryman, C.1    Weinstein, E.2    Wnuk, S.F.3    Bartel, D.P.4
  • 33
    • 33747130345 scopus 로고    scopus 로고
    • Miniaturising the laboratory in emulsion droplets
    • Griffi ths AD, Tawfi k DS. (2006) Miniaturising the laboratory in emulsion droplets. Trends in Biotechnology 24, 395-402.
    • (2006) Trends in Biotechnology , vol.24 , pp. 395-402
    • Griffi Ths, A.D.1    Tawfi, K.D.S.2
  • 34
    • 0031543396 scopus 로고    scopus 로고
    • The role of cysteinyl residues in the activity of bacterial elongation factor Ts, a guanosine nucleotide dissociation protein
    • DOI 10.1006/abbi.1997.0375
    • Hwang YW, Sanchez A, Hwang MCC, Miller DL. (1997) The Role of Cysteinyl Residues in the Activity of Bacterial Elongation Factor Ts, a Guanosine Nucleotide Dissociation Protein. Arch. Biochem. Biophys. 348, 157-162. (Pubitemid 27514682)
    • (1997) Archives of Biochemistry and Biophysics , vol.348 , Issue.1 , pp. 157-162
    • Hwang, Y.-W.1    Sanchez, A.2    Hwang, M.-C.C.3    Miller, D.L.4
  • 35
    • 0029959815 scopus 로고    scopus 로고
    • The "allosteric three-site model" of elongation cannot be confi rmed in a welldefi ned ribosome system from Escherichia coli
    • Semenkov YP, Rodnina MV, Wintermeyer W. (1996) The "allosteric three-site model" of elongation cannot be confi rmed in a welldefi ned ribosome system from Escherichia coli. PNAS 93, 12183-12188.
    • (1996) PNAS , vol.93 , pp. 12183-12188
    • Semenkov, Y.P.1    Rodnina, M.V.2    Wintermeyer, W.3
  • 36
    • 71549163430 scopus 로고    scopus 로고
    • Changeability of individual domains of an aminoacyl-tRNA in polymerization by the ribosome
    • Gao R, Forster AC. (2010) Changeability of individual domains of an aminoacyl-tRNA in polymerization by the ribosome. FEBS Letters 584, 99-105.
    • (2010) FEBS Letters , vol.584 , pp. 99-105
    • Gao, R.1    Forster, A.C.2
  • 37
    • 58549114677 scopus 로고    scopus 로고
    • Slow peptide bond formation by proline and other N-alkylamino acids in translation
    • Pavlov MY, Watts RE, Tan Z, Cornish VW, Ehrenberg M, Forster AC. (2008) Slow peptide bond formation by proline and other N-alkylamino acids in translation. PNAS 106, 50-54.
    • (2008) PNAS , vol.106 , pp. 50-54
    • Pavlov, M.Y.1    Watts, R.E.2    Tan, Z.3    Cornish, V.W.4    Ehrenberg, M.5    Forster, A.C.6
  • 39
    • 77949404685 scopus 로고    scopus 로고
    • Chemical models of peptide formation in translation
    • Watts RE, Forster AC. (2010) Chemical Models of Peptide Formation in Translation. Biochemistry 49, 2177-2185.
    • (2010) Biochemistry , vol.49 , pp. 2177-2185
    • Watts, R.E.1    Forster, A.C.2
  • 40
    • 33745071762 scopus 로고    scopus 로고
    • Peptide bond formation does not involve acid-base catalysis by ribosomal residues
    • DOI 10.1038/nsmb1091, PII N1091
    • Bieling P, Beringer M, Adio S, Rodnina MV. (2006) Peptide bond formation does not involve acid-base catalysis by ribosomal residues. Nature Structural and Molecular Biology 13, 423-428. (Pubitemid 43881582)
    • (2006) Nature Structural and Molecular Biology , vol.13 , Issue.5 , pp. 423-428
    • Bieling, P.1    Beringer, M.2    Adio, S.3    Rodnina, M.V.4
  • 41
    • 59649098288 scopus 로고    scopus 로고
    • A single-step method for purifi cation of active His-tagged ribosomes from a genetically engineered Escherichia coli
    • Ederth J, Mandava CS, Dasgupta S, Sanyal S. (2009) A single-step method for purifi cation of active His-tagged ribosomes from a genetically engineered Escherichia coli . Nucleic Acids Research 37, e15.
    • (2009) Nucleic Acids Research , vol.37
    • Ederth, J.1    Mandava, C.S.2    Dasgupta, S.3    Sanyal, S.4
  • 42
    • 0035812714 scopus 로고    scopus 로고
    • A posttermination ribosomal complex is the guanine nucleotide exchange factor for peptide release factor RF3
    • DOI 10.1016/S0092-8674(01)00508-6
    • Zavialov AV, Buckingham RH, Ehrenberg M. (2001) A Posttermination Ribosomal Complex Is the Guanine Nucleotide Exchange Factor for Peptide Release Factor RF3. Cell 107, 115-124. (Pubitemid 32972042)
    • (2001) Cell , vol.107 , Issue.1 , pp. 115-124
    • Zavialov, A.V.1    Buckingham, R.H.2    Ehrenberg, M.3


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