메뉴 건너뛰기




Volumn 13, Issue 4, 2003, Pages 506-512

Unnatural RNA display libraries

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; AMINO ACID; ARGININE; BETA AMINO ACID; BIOCYTIN; CARBOXYLIC ACID; CYSTEINE; FUNCTIONAL GROUP; GLYCINE; HYBRID PROTEIN; LIGAND; METICILLIN; PENICILLIN BINDING PROTEIN; PENICILLIN G; PEPTIDE LIBRARY; POLYPEPTIDE; PUROMYCIN; RNA; STREPTAVIDIN; TRYPTOPHAN; TRYPTOPHAN SYNTHASE; VALINE;

EID: 0042430533     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(03)00110-6     Document Type: Review
Times cited : (37)

References (70)
  • 3
    • 0032564346 scopus 로고    scopus 로고
    • Ribosome display efficiently selects and evolves high-affinity antibodies in vitro from immune libraries
    • Hanes J., Jermutus L., Weber-Bornhauser S., Bosshard H.R., Pluckthun A. Ribosome display efficiently selects and evolves high-affinity antibodies in vitro from immune libraries. Proc Natl Acad Sci USA. 95:1998;14130-14135.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 14130-14135
    • Hanes, J.1    Jermutus, L.2    Weber-Bornhauser, S.3    Bosshard, H.R.4    Pluckthun, A.5
  • 4
    • 0030817279 scopus 로고    scopus 로고
    • RNA-peptide fusions for the in vitro selection of peptides and proteins
    • Roberts R.W., Szostak J.W. RNA-peptide fusions for the in vitro selection of peptides and proteins. Proc Natl Acad Sci USA. 94:1997;12297-12302.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12297-12302
    • Roberts, R.W.1    Szostak, J.W.2
  • 5
    • 0000577984 scopus 로고    scopus 로고
    • The "one-bead-one-compound" combinatorial library method
    • Lam K.S., Lebl M., Krchnak V. The "one-bead-one-compound" combinatorial library method. Chem Rev. 97:1997;411-448.
    • (1997) Chem Rev , vol.97 , pp. 411-448
    • Lam, K.S.1    Lebl, M.2    Krchnak, V.3
  • 7
    • 0028592703 scopus 로고
    • An in vitro polysome display system for identifying ligands from very large peptide libraries
    • Mattheakis L.C., Bhatt R.R., Dower W.J. An in vitro polysome display system for identifying ligands from very large peptide libraries. Proc Natl Acad Sci USA. 91:1994;9022-9026.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 9022-9026
    • Mattheakis, L.C.1    Bhatt, R.R.2    Dower, W.J.3
  • 8
    • 0030974119 scopus 로고    scopus 로고
    • In vitro selection and evolution of functional proteins by using ribosome display
    • Hanes J., Pluckthun A. In vitro selection and evolution of functional proteins by using ribosome display. Proc Natl Acad Sci USA. 94:1997;4937-4942.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4937-4942
    • Hanes, J.1    Pluckthun, A.2
  • 10
    • 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
    • Nemoto N., Miyamoto-Sato E., Husimi Y., Yanagawa H. 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. 414:1997;405-408.
    • (1997) FEBS Lett , vol.414 , pp. 405-408
    • Nemoto, N.1    Miyamoto-Sato, E.2    Husimi, Y.3    Yanagawa, H.4
  • 11
    • 0036973240 scopus 로고    scopus 로고
    • The use of phage display in the study of receptors and their ligands
    • Hartley O. The use of phage display in the study of receptors and their ligands. J Recept Signal Transduct Res. 22:2002;373-392.
    • (2002) J Recept Signal Transduct Res , vol.22 , pp. 373-392
    • Hartley, O.1
  • 12
    • 0035853116 scopus 로고    scopus 로고
    • Global analysis of proteasomal substrate specificity using positional-scanning libraries of covalent inhibitors
    • Positional scanning libraries of peptide vinyl sulfones were used to create specificity profiles for proteasomal subunits, allowing the authors to design subunit-specific inhibitors
    • Nazif T., Bogyo M. Global analysis of proteasomal substrate specificity using positional-scanning libraries of covalent inhibitors. Proc Natl Acad Sci USA. 98:2001;2967-2972 Positional scanning libraries of peptide vinyl sulfones were used to create specificity profiles for proteasomal subunits, allowing the authors to design subunit-specific inhibitors.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 2967-2972
    • Nazif, T.1    Bogyo, M.2
  • 14
    • 0017705507 scopus 로고
    • Posttranslational covalent modification of proteins
    • Uy R., Wold F. Posttranslational covalent modification of proteins. Science. 198:1977;890-896.
    • (1977) Science , vol.198 , pp. 890-896
    • Uy, R.1    Wold, F.2
  • 15
    • 0024968835 scopus 로고
    • A general method for site-specific incorporation of unnatural amino acids into proteins
    • Noren C.J., Anthony-Cahill S.J., Griffith M.C., Schultz P.G. A general method for site-specific incorporation of unnatural amino acids into proteins. Science. 244:1989;182-188.
    • (1989) Science , vol.244 , pp. 182-188
    • Noren, C.J.1    Anthony-Cahill, S.J.2    Griffith, M.C.3    Schultz, P.G.4
  • 16
    • 0000652848 scopus 로고
    • Biosynthetic site-specific incorporation of a non-natural amino acid into a polypeptide
    • Bain J.D., Glabe C.G., Dix T.A., Chamberlin A.R. Biosynthetic site-specific incorporation of a non-natural amino acid into a polypeptide. J Am Chem Soc. 111:1989;8013-8014.
    • (1989) J Am Chem Soc , vol.111 , pp. 8013-8014
    • Bain, J.D.1    Glabe, C.G.2    Dix, T.A.3    Chamberlin, A.R.4
  • 17
    • 0031937870 scopus 로고    scopus 로고
    • Expansion of the genetic code: Site-directed p-fluoro-phenylalanine incorporation in Escherichia coli
    • Furter R. Expansion of the genetic code: site-directed p-fluoro-phenylalanine incorporation in Escherichia coli. Protein Sci. 7:1998;419-426.
    • (1998) Protein Sci , vol.7 , pp. 419-426
    • Furter, R.1
  • 19
    • 0036890716 scopus 로고    scopus 로고
    • Expanding the natural repertoire of protein structure and function
    • This comprehensive review focuses on in vivo methods for the site-directed incorporation of unnatural amino acids into proteins via nonsense suppression, although other aspects of protein engineering are discussed
    • Anthony-Cahill S.J., Magliery T.J. Expanding the natural repertoire of protein structure and function. Curr Pharm Biotechnol. 3:2002;299-315 This comprehensive review focuses on in vivo methods for the site-directed incorporation of unnatural amino acids into proteins via nonsense suppression, although other aspects of protein engineering are discussed.
    • (2002) Curr Pharm Biotechnol , vol.3 , pp. 299-315
    • Anthony-Cahill, S.J.1    Magliery, T.J.2
  • 20
    • 0036900746 scopus 로고    scopus 로고
    • Incorporation of non-natural amino acids into proteins
    • This review describes incorporation of unnatural amino acids into proteins and discusses alternative codon-anticodon pairs for extension of the genetic code
    • Hohsaka T., Sisido M. Incorporation of non-natural amino acids into proteins. Curr Opin Chem Biol. 6:2002;809-815 This review describes incorporation of unnatural amino acids into proteins and discusses alternative codon-anticodon pairs for extension of the genetic code.
    • (2002) Curr Opin Chem Biol , vol.6 , pp. 809-815
    • Hohsaka, T.1    Sisido, M.2
  • 21
    • 0033637431 scopus 로고    scopus 로고
    • Unnatural amino acids as probes of protein structure and function
    • Dougherty D.A. Unnatural amino acids as probes of protein structure and function. Curr Opin Chem Biol. 4:2000;645-652.
    • (2000) Curr Opin Chem Biol , vol.4 , pp. 645-652
    • Dougherty, D.A.1
  • 22
    • 0033643217 scopus 로고    scopus 로고
    • Optimized synthesis of RNA-protein fusions for in vitro protein selection
    • Liu R., Barrick J.E., Szostak J.W., Roberts R.W. Optimized synthesis of RNA-protein fusions for in vitro protein selection. Methods Enzymol. 318:2000;268-293.
    • (2000) Methods Enzymol , vol.318 , pp. 268-293
    • Liu, R.1    Barrick, J.E.2    Szostak, J.W.3    Roberts, R.W.4
  • 23
    • 0037333841 scopus 로고    scopus 로고
    • MRNA display: Ligand discovery, interaction analysis and beyond
    • Takahashi T.T., Austin R.J., Roberts R.W. mRNA display: ligand discovery, interaction analysis and beyond. Trends Biochem Sci. 28:2003;159-165.
    • (2003) Trends Biochem Sci , vol.28 , pp. 159-165
    • Takahashi, T.T.1    Austin, R.J.2    Roberts, R.W.3
  • 24
    • 0034708337 scopus 로고    scopus 로고
    • Constructing high complexity synthetic libraries of long ORFs using in vitro selection
    • Cho G., Keefe A.D., Liu R., Wilson D.S., Szostak J.W. Constructing high complexity synthetic libraries of long ORFs using in vitro selection. J Mol Biol. 297:2000;309-319.
    • (2000) J Mol Biol , vol.297 , pp. 309-319
    • Cho, G.1    Keefe, A.D.2    Liu, R.3    Wilson, D.S.4    Szostak, J.W.5
  • 26
    • 0037189891 scopus 로고    scopus 로고
    • In vitro selection of mRNA display libraries containing an unnatural amino acid
    • The authors demonstrate for the first time that nonsense suppression and mRNA display can be united. An acylated amber suppressor tRNA is used to incorporate the unnatural amino acid biocytin in an mRNA display library and streptavidin purification is used to select for the presence of the unnatural residue with high efficiency
    • Li S., Millward S., Roberts R. In vitro selection of mRNA display libraries containing an unnatural amino acid. J Am Chem Soc. 124:2002;9972-9973 The authors demonstrate for the first time that nonsense suppression and mRNA display can be united. An acylated amber suppressor tRNA is used to incorporate the unnatural amino acid biocytin in an mRNA display library and streptavidin purification is used to select for the presence of the unnatural residue with high efficiency.
    • (2002) J Am Chem Soc , vol.124 , pp. 9972-9973
    • Li, S.1    Millward, S.2    Roberts, R.3
  • 27
    • 0029661426 scopus 로고    scopus 로고
    • An engineered Tetrahymena tRNAGln for in vivo incorporation of unnatural amino acids into proteins by nonsense suppression
    • Saks M.E., Sampson J.R., Nowak M.W., Kearney P.C., Du F., Abelson J.N., Lester H.A., Dougherty D.A. An engineered Tetrahymena tRNAGln for in vivo incorporation of unnatural amino acids into proteins by nonsense suppression. J Biol Chem. 271:1996;23169-23175.
    • (1996) J Biol Chem , vol.271 , pp. 23169-23175
    • Saks, M.E.1    Sampson, J.R.2    Nowak, M.W.3    Kearney, P.C.4    Du, F.5    Abelson, J.N.6    Lester, H.A.7    Dougherty, D.A.8
  • 28
    • 0037348840 scopus 로고    scopus 로고
    • A novel strategy for in vitro selection of peptide-drug conjugates
    • This paper describes construction of hybrid drug-peptide mRNA display libraries by conjugation at a fixed cysteine with a reactive penicillin sidechain. The resulting library is used to target S. aureus penicillin-binding protein PBP2a, resulting in a ligand with a 100-fold enhancement in activity compared to the drug alone
    • Li S., Roberts R.W. A novel strategy for in vitro selection of peptide-drug conjugates. Chem Biol. 10:2003;233-239 This paper describes construction of hybrid drug-peptide mRNA display libraries by conjugation at a fixed cysteine with a reactive penicillin sidechain. The resulting library is used to target S. aureus penicillin-binding protein PBP2a, resulting in a ligand with a 100-fold enhancement in activity compared to the drug alone.
    • (2003) Chem Biol , vol.10 , pp. 233-239
    • Li, S.1    Roberts, R.W.2
  • 29
    • 0033580616 scopus 로고    scopus 로고
    • Penicillin-binding protein 2a from methicillin-resistant Staphylococcus aureus: Kinetic characterization of its interactions with β-lactams using electrospray mass spectrometry
    • Lu W.-P., Sun Y., Bauer M.D., Paule S., Koenigs P.M., Kraft W.G. Penicillin-binding protein 2a from methicillin-resistant Staphylococcus aureus: kinetic characterization of its interactions with β-lactams using electrospray mass spectrometry. Biochemistry. 38:1999;6537-6546.
    • (1999) Biochemistry , vol.38 , pp. 6537-6546
    • Lu, W.-P.1    Sun, Y.2    Bauer, M.D.3    Paule, S.4    Koenigs, P.M.5    Kraft, W.G.6
  • 30
    • 0024722501 scopus 로고
    • Errors and alternatives in reading the universal genetic code
    • Parker J. Errors and alternatives in reading the universal genetic code. Microbiol Rev. 53:1989;273-298.
    • (1989) Microbiol Rev , vol.53 , pp. 273-298
    • Parker, J.1
  • 31
    • 0023977682 scopus 로고
    • EFTu provides an internal kinetic standard for translational accuracy
    • Thompson R.C. EFTu provides an internal kinetic standard for translational accuracy. Trends Biochem Sci. 13:1988;91-93.
    • (1988) Trends Biochem Sci , vol.13 , pp. 91-93
    • Thompson, R.C.1
  • 32
    • 0034961959 scopus 로고    scopus 로고
    • Analysis of codon:anticodon interactions within the ribosome provides new insights into codon reading and the genetic code structure
    • Lim V.I., Curran J.F. Analysis of codon:anticodon interactions within the ribosome provides new insights into codon reading and the genetic code structure. RNA. 7:2001;942-957.
    • (2001) RNA , vol.7 , pp. 942-957
    • Lim, V.I.1    Curran, J.F.2
  • 33
    • 0016596282 scopus 로고
    • Informational suppression of missense mutations
    • Hill C.W. Informational suppression of missense mutations. Cell. 6:1975;419-427.
    • (1975) Cell , vol.6 , pp. 419-427
    • Hill, C.W.1
  • 34
    • 0013935886 scopus 로고
    • Studies of missense suppression of the tryptophan synthetase A-protein mutant A36
    • Carbon J., Berg P., Yanofsky C. Studies of missense suppression of the tryptophan synthetase A-protein mutant A36. Proc Natl Acad Sci USA. 56:1966;764-771.
    • (1966) Proc Natl Acad Sci USA , vol.56 , pp. 764-771
    • Carbon, J.1    Berg, P.2    Yanofsky, C.3
  • 37
    • 0014966259 scopus 로고
    • Glycine transfer RNA of Escherichia coli. I. Structural genes for two glycine tRNA species
    • Squires C., Carbon J., Hill C.W. Glycine transfer RNA of Escherichia coli. I. Structural genes for two glycine tRNA species. J Mol Biol. 52:1970;557-569.
    • (1970) J Mol Biol , vol.52 , pp. 557-569
    • Squires, C.1    Carbon, J.2    Hill, C.W.3
  • 38
    • 0014966266 scopus 로고
    • Glycine transfer RNA of Escherichia coli. II. Impaired GGA-recognition in strains containing a genetically altered transfer RNA reversal by a secondary suppressor mutation
    • Carbon J., Squires C., Hill C.W. Glycine transfer RNA of Escherichia coli. II. Impaired GGA-recognition in strains containing a genetically altered transfer RNA reversal by a secondary suppressor mutation. J Mol Biol. 52:1970;571-584.
    • (1970) J Mol Biol , vol.52 , pp. 571-584
    • Carbon, J.1    Squires, C.2    Hill, C.W.3
  • 39
    • 0028200375 scopus 로고
    • Site-specific incorporation of photofunctional nonnatural amino acids into a polypeptide through in vitro protein biosynthesis
    • Hohsaka T., Sato K., Sisido M., Takai K., Yokoyama S. Site-specific incorporation of photofunctional nonnatural amino acids into a polypeptide through in vitro protein biosynthesis. FEBS Lett. 344:1994;171-174.
    • (1994) FEBS Lett , vol.344 , pp. 171-174
    • Hohsaka, T.1    Sato, K.2    Sisido, M.3    Takai, K.4    Yokoyama, S.5
  • 40
    • 0025283965 scopus 로고
    • Role of GC-biased mutation pressure on synonymous codon choice in Micrococcus luteus, a bacterium with a high genomic GC-content
    • Ohama T., Muto A., Osawa S. Role of GC-biased mutation pressure on synonymous codon choice in Micrococcus luteus, a bacterium with a high genomic GC-content. Nucleic Acids Res. 18:1990;1565-1569.
    • (1990) Nucleic Acids Res , vol.18 , pp. 1565-1569
    • Ohama, T.1    Muto, A.2    Osawa, S.3
  • 41
    • 0025742784 scopus 로고
    • Novel anticodon composition of transfer RNAs in Micrococcus luteus, a bacterium with a high genomic G + C content. Correlation with codon usage
    • Kano A., Andachi Y., Ohama T., Osawa S. Novel anticodon composition of transfer RNAs in Micrococcus luteus, a bacterium with a high genomic G + C content. Correlation with codon usage. J Mol Biol. 221:1991;387-401.
    • (1991) J Mol Biol , vol.221 , pp. 387-401
    • Kano, A.1    Andachi, Y.2    Ohama, T.3    Osawa, S.4
  • 42
    • 0025831680 scopus 로고
    • Protein synthesis in vitro by Micrococcus luteus
    • Farwell M.A., Rabinowitz J.C. Protein synthesis in vitro by Micrococcus luteus. J Bacteriol. 173:1991;3514-3522.
    • (1991) J Bacteriol , vol.173 , pp. 3514-3522
    • Farwell, M.A.1    Rabinowitz, J.C.2
  • 43
    • 0030784822 scopus 로고    scopus 로고
    • Exploiting unassigned codons in Micrococcus luteus for tRNA-based amino acid mutagenesis
    • Kowal A.K., Oliver J.S. Exploiting unassigned codons in Micrococcus luteus for tRNA-based amino acid mutagenesis. Nucleic Acids Res. 25:1997;4685-4689.
    • (1997) Nucleic Acids Res , vol.25 , pp. 4685-4689
    • Kowal, A.K.1    Oliver, J.S.2
  • 44
    • 0020262659 scopus 로고
    • Codon usage and transfer RNA content: Organism-specific codon-choice patterns in reference to the isoacceptor contents
    • Ikemura T., Ozeki H. Codon usage and transfer RNA content: organism-specific codon-choice patterns in reference to the isoacceptor contents. Cold Spring Harb Symp Quant Biol. 47:1983;1087-1097.
    • (1983) Cold Spring Harb Symp Quant Biol , vol.47 , pp. 1087-1097
    • Ikemura, T.1    Ozeki, H.2
  • 45
    • 0038044525 scopus 로고    scopus 로고
    • In vitro selection for sense codon suppression
    • This work uses mRNA display to select sense codons that can be easily suppressed. In standard reticulocyte lysate extracts, sense codon suppression is found to occur predominantly at a GUA valine codon with equal efficiency to UAG-mediated nonsense suppression. The authors go on to show that sense suppression can occur at arbitrarily chosen codons with equal efficiency if the tRNA concentration is controlled
    • Frankel A., Roberts R.W. In vitro selection for sense codon suppression. RNA. 9:2003;780-786 This work uses mRNA display to select sense codons that can be easily suppressed. In standard reticulocyte lysate extracts, sense codon suppression is found to occur predominantly at a GUA valine codon with equal efficiency to UAG-mediated nonsense suppression. The authors go on to show that sense suppression can occur at arbitrarily chosen codons with equal efficiency if the tRNA concentration is controlled.
    • (2003) RNA , vol.9 , pp. 780-786
    • Frankel, A.1    Roberts, R.W.2
  • 46
    • 0035043155 scopus 로고    scopus 로고
    • Development of a tRNA-dependent in vitro translation system
    • Jackson R.J., Napthine S., Brierley I. Development of a tRNA-dependent in vitro translation system. RNA. 7:2001;765-773.
    • (2001) RNA , vol.7 , pp. 765-773
    • Jackson, R.J.1    Napthine, S.2    Brierley, I.3
  • 47
    • 0034904102 scopus 로고    scopus 로고
    • Cell-free translation reconstituted with purified components
    • The authors describe a fully reconstituted E. coli translation system from purified components. This system or similar systems will be important in creating unnatural RNA display libraries. Omission of release factor 1 results in efficient unnatural amino acid incorporation into nascent polypeptides
    • Shimizu Y., Inoue A., Tomari Y., Suzuki T., Yokogawa T., Nishikawa K., Ueda T. Cell-free translation reconstituted with purified components. Nat Biotechnol. 19:2001;751-755 The authors describe a fully reconstituted E. coli translation system from purified components. This system or similar systems will be important in creating unnatural RNA display libraries. Omission of release factor 1 results in efficient unnatural amino acid incorporation into nascent polypeptides.
    • (2001) Nat Biotechnol , vol.19 , pp. 751-755
    • Shimizu, Y.1    Inoue, A.2    Tomari, Y.3    Suzuki, T.4    Yokogawa, T.5    Nishikawa, K.6    Ueda, T.7
  • 48
    • 0035477877 scopus 로고    scopus 로고
    • A simplified reconstitution of mRNA-directed peptide synthesis: Activity of the epsilon enhancer and an unnatural amino acid
    • Lys in a reconstituted E. coli translation system
    • Lys in a reconstituted E. coli translation system.
    • (2001) Anal Biochem , vol.297 , pp. 60-70
    • Forster, A.C.1    Weissbach, H.2    Blacklow, S.C.3
  • 49
    • 0038652110 scopus 로고    scopus 로고
    • Programming peptidomimetic syntheses by translating genetic codes designed de novo
    • This work demonstrates that short unnatural oligopeptides can be created using a reconstituted bacterial translation system. If long enough molecules can be created, this work may provide a basis for unnatural library selection via ribosome display
    • Forster A.C., Tan Z., Nalam M.N., Lin H., Qu H., Cornish V.W., Blacklow S.C. Programming peptidomimetic syntheses by translating genetic codes designed de novo. Proc Natl Acad Sci USA. 100:2003;6353-6357 This work demonstrates that short unnatural oligopeptides can be created using a reconstituted bacterial translation system. If long enough molecules can be created, this work may provide a basis for unnatural library selection via ribosome display.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 6353-6357
    • Forster, A.C.1    Tan, Z.2    Nalam, M.N.3    Lin, H.4    Qu, H.5    Cornish, V.W.6    Blacklow, S.C.7
  • 50
    • 0001412985 scopus 로고
    • Structural requirements for puromycin inhibition of protein synthesis
    • Nathans D., Neidle A. Structural requirements for puromycin inhibition of protein synthesis. Nature. 197:1963;1076-1077.
    • (1963) Nature , vol.197 , pp. 1076-1077
    • Nathans, D.1    Neidle, A.2
  • 51
    • 0024293249 scopus 로고
    • Ribosomal binding and dipeptide formation by misacylated tRNA(Phe),S
    • Heckler T.G., Roesser J.R., Xu C., Chang P.I., Hecht S.M. Ribosomal binding and dipeptide formation by misacylated tRNA(Phe),S. Biochemistry. 27:1988;7254-7262.
    • (1988) Biochemistry , vol.27 , pp. 7254-7262
    • Heckler, T.G.1    Roesser, J.R.2    Xu, C.3    Chang, P.I.4    Hecht, S.M.5
  • 53
    • 0014219393 scopus 로고
    • Ribosome-catalysed reaction of puromycin with a formylmethionine-containing oligonucleotide
    • Monro R.E., Marcker K.A. Ribosome-catalysed reaction of puromycin with a formylmethionine-containing oligonucleotide. J Mol Biol. 25:1967;347-350.
    • (1967) J Mol Biol , vol.25 , pp. 347-350
    • Monro, R.E.1    Marcker, K.A.2
  • 54
    • 0036077695 scopus 로고    scopus 로고
    • Puromycin oligonucleotides reveal steric restrictions for ribosome entry and multiple modes of translation inhibition
    • Starck S.R., Roberts R.W. Puromycin oligonucleotides reveal steric restrictions for ribosome entry and multiple modes of translation inhibition. RNA. 8:2002;890-903.
    • (2002) RNA , vol.8 , pp. 890-903
    • Starck, S.R.1    Roberts, R.W.2
  • 56
    • 0016749809 scopus 로고
    • Synthesis of thiol-containing analogues of puromycin and a study of their interaction with N-acetylphenylalanyl-transfer ribonucleic acid on ribosomes to form thioesters
    • Gooch J., Hawtrey A.O. Synthesis of thiol-containing analogues of puromycin and a study of their interaction with N-acetylphenylalanyl-transfer ribonucleic acid on ribosomes to form thioesters. Biochem J. 149:1975;209-220.
    • (1975) Biochem J , vol.149 , pp. 209-220
    • Gooch, J.1    Hawtrey, A.O.2
  • 57
    • 0037668349 scopus 로고    scopus 로고
    • The puromycin route to assess stereo- and regiochemical constraints on peptide bond formation in eukaryotic ribosomes
    • This paper demonstrates that the stereoselectivity of the eukaryotic ribosome depends on the size and nature of the pendant sidechain. Interestingly, some unnatural enantiomers (e.g. [D] O-methyltyrosine) are found to be more efficiently incorporated than natural [L] residues. Incorporation of β-amino acids is also demonstrated
    • Starck S.R., Olsen B., Roberts R.W. The puromycin route to assess stereo- and regiochemical constraints on peptide bond formation in eukaryotic ribosomes. J Am Chem Soc. 125:2003;8090-8091 This paper demonstrates that the stereoselectivity of the eukaryotic ribosome depends on the size and nature of the pendant sidechain. Interestingly, some unnatural enantiomers (e.g. [D] O-methyltyrosine) are found to be more efficiently incorporated than natural [L] residues. Incorporation of β-amino acids is also demonstrated.
    • (2003) J Am Chem Soc , vol.125 , pp. 8090-8091
    • Starck, S.R.1    Olsen, B.2    Roberts, R.W.3
  • 58
    • 0029108642 scopus 로고
    • Probing protein structure and function with an expanded genetic code
    • Cornish V.W., Mendel D., Schultz P.G. Probing protein structure and function with an expanded genetic code. Angew Chem Int Ed Engl. 34:1995;621-633.
    • (1995) Angew Chem Int Ed Engl , vol.34 , pp. 621-633
    • Cornish, V.W.1    Mendel, D.2    Schultz, P.G.3
  • 59
    • 0003104160 scopus 로고    scopus 로고
    • Incorporation of noncoded amino acids by in vitro protein biosynthesis
    • Gilmore M.A., Steward L.E., Chamberlin A.R. Incorporation of noncoded amino acids by in vitro protein biosynthesis. Top Curr Chem. 202:1999;77-99.
    • (1999) Top Curr Chem , vol.202 , pp. 77-99
    • Gilmore, M.A.1    Steward, L.E.2    Chamberlin, A.R.3
  • 60
    • 0035823759 scopus 로고    scopus 로고
    • Protein-based materials, towards a new level of structural control
    • A comprehensive review pertaining to protein engineering using unnatural amino acid insertion
    • van Hest J.C.M., Tirrell D.A. Protein-based materials, towards a new level of structural control. Chem Commun. 19:2001;1897-1904 A comprehensive review pertaining to protein engineering using unnatural amino acid insertion.
    • (2001) Chem Commun , vol.19 , pp. 1897-1904
    • Van Hest, J.C.M.1    Tirrell, D.A.2
  • 61
    • 0026082859 scopus 로고
    • Site-specific incorporation of non-natural residues into peptides: Effect of residue structure on suppression and translation efficiencies
    • Bain J.D., Wacjer D.A., Kuo E.E., Chamberlin A.R., Diala E.S. Site-specific incorporation of non-natural residues into peptides: effect of residue structure on suppression and translation efficiencies. Tetrahedron. 47:1991;2389-2400.
    • (1991) Tetrahedron , vol.47 , pp. 2389-2400
    • Bain, J.D.1    Wacjer, D.A.2    Kuo, E.E.3    Chamberlin, A.R.4    Diala, E.S.5
  • 62
    • 0026567563 scopus 로고
    • Site-specific incorporation of novel backbone structures into proteins
    • Ellman J.A., Mendel D., Schultz P.G. Site-specific incorporation of novel backbone structures into proteins. Science. 255:1992;197-200.
    • (1992) Science , vol.255 , pp. 197-200
    • Ellman, J.A.1    Mendel, D.2    Schultz, P.G.3
  • 63
    • 0001100635 scopus 로고
    • Protein biosynthesis with conformationally restricted amino acids
    • Mendel D., Ellman J., Schultz P.G. Protein biosynthesis with conformationally restricted amino acids. J Am Chem Soc. 115:1993;4359-4360.
    • (1993) J Am Chem Soc , vol.115 , pp. 4359-4360
    • Mendel, D.1    Ellman, J.2    Schultz, P.G.3
  • 64
    • 0032495762 scopus 로고    scopus 로고
    • Ribosome-mediated incorporation of hydrazinophenylalanine into modified peptide and protein analogues
    • Killian J.A., Van Cleve M.D., Shayo Y.F., Hecht S.M. Ribosome-mediated incorporation of hydrazinophenylalanine into modified peptide and protein analogues. J Am Chem Soc. 120:1998;3032-3042.
    • (1998) J Am Chem Soc , vol.120 , pp. 3032-3042
    • Killian, J.A.1    Van Cleve, M.D.2    Shayo, Y.F.3    Hecht, S.M.4
  • 65
    • 0037167581 scopus 로고    scopus 로고
    • Site-specific incorporation of (aminooxy)acetic acid into proteins
    • This work demonstrates that the ribosome can incorporate (aminooxy) acetic acid into different sites within the DHFR protein via nonsense suppression. The monomer has a chain length similar to β-amino acids, but has the sidechain positioned similar to a typical natural residue. The hydrazino-amino acids of Killian et al. [64] show a similar overall geometry
    • Eisenhauer B.M., Hecht S.M. Site-specific incorporation of (aminooxy)acetic acid into proteins. Biochemistry. 41:2002;11472-11478 This work demonstrates that the ribosome can incorporate (aminooxy)acetic acid into different sites within the DHFR protein via nonsense suppression. The monomer has a chain length similar to β-amino acids, but has the sidechain positioned similar to a typical natural residue. The hydrazino-amino acids of Killian et al. [64] show a similar overall geometry.
    • (2002) Biochemistry , vol.41 , pp. 11472-11478
    • Eisenhauer, B.M.1    Hecht, S.M.2
  • 67
    • 0018945995 scopus 로고
    • Aminoacyl transfer ribonucleic acid binding site of the bacterial elongation factor Tu
    • Pingoud A., Urbanke C. Aminoacyl transfer ribonucleic acid binding site of the bacterial elongation factor Tu. Biochemistry. 19:1980;2108-2112.
    • (1980) Biochemistry , vol.19 , pp. 2108-2112
    • Pingoud, A.1    Urbanke, C.2
  • 68
    • 0035812828 scopus 로고    scopus 로고
    • Uniform binding of aminoacyl-tRNAs to elongation factor Tu by thermodynamic compensation
    • LaRiviere F.J., Wolfson A.D., Uhlenbeck O.C. Uniform binding of aminoacyl-tRNAs to elongation factor Tu by thermodynamic compensation. Science. 294:2001;165-168.
    • (2001) Science , vol.294 , pp. 165-168
    • LaRiviere, F.J.1    Wolfson, A.D.2    Uhlenbeck, O.C.3
  • 69
    • 85031075312 scopus 로고    scopus 로고
    • In vitro ribosome evolution. US Patent 2002 6,358,713
    • Green R: In vitro ribosome evolution. US Patent 2002 6,358,713.
    • Green, R.1
  • 70
    • 0038547955 scopus 로고    scopus 로고
    • Enhanced D-amino acid incorporation into protein by modified ribosome
    • A demonstration that mutant ribosomes can have relaxed stereospecificity, allowing the incorporation (acceptor and donor function) of [D] amino acids into protein chains via in vitro nonsense suppression
    • Dedkova L.M., Fahmi N.E., Golovine S.Y., Hecht S.M. Enhanced D-amino acid incorporation into protein by modified ribosome. J Am Chem Soc. 125:2003;6616-6617 A demonstration that mutant ribosomes can have relaxed stereospecificity, allowing the incorporation (acceptor and donor function) of [D] amino acids into protein chains via in vitro nonsense suppression.
    • (2003) J Am Chem Soc , vol.125 , pp. 6616-6617
    • Dedkova, L.M.1    Fahmi, N.E.2    Golovine, S.Y.3    Hecht, S.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.