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1
-
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0024968835
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A general method for site-specific incorporation of unnatural amino acids into proteins
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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
-
2
-
-
0000652848
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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., Diala E.S. 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
Diala, E.S.5
-
4
-
-
0030482172
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Development of improved tRNAs for in vitro biosynthesis of proteins containing unnatural amino acids
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Cload S.T., Liu D.R., Froland A.F., Schultz P.G. Development of improved tRNAs for in vitro biosynthesis of proteins containing unnatural amino acids. Chem Biol. 3:1996;1033-1038.
-
(1996)
Chem Biol
, vol.3
, pp. 1033-1038
-
-
Cload, S.T.1
Liu, D.R.2
Froland, A.F.3
Schultz, P.G.4
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5
-
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0035909080
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Incorporation of nonnatural amino acids into proteins by using various four-base codons in an Escherichia coli in vitro translation system
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Various kinds of four-base codons are developed. A highly efficient four-base codon pair for incorporation of two different non-natural amino acids into a single protein is also described.
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Hohsaka T., Ashizuka Y., Taira H., Murakami H., Sisido M. Incorporation of nonnatural amino acids into proteins by using various four-base codons in an Escherichia coli in vitro translation system. Biochemistry. 40:2001;11060-11064. Various kinds of four-base codons are developed. A highly efficient four-base codon pair for incorporation of two different non-natural amino acids into a single protein is also described.
-
(2001)
Biochemistry
, vol.40
, pp. 11060-11064
-
-
Hohsaka, T.1
Ashizuka, Y.2
Taira, H.3
Murakami, H.4
Sisido, M.5
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6
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0034793087
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Introduction of specialty functions by the position-specific incorporation of nonnatural amino acids into proteins through four-base codon/anticodon pairs
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Sisido M., Hohsaka T. Introduction of specialty functions by the position-specific incorporation of nonnatural amino acids into proteins through four-base codon/anticodon pairs. Appl Microbiol Biotechnol. 57:2001;274-281.
-
(2001)
Appl Microbiol Biotechnol
, vol.57
, pp. 274-281
-
-
Sisido, M.1
Hohsaka, T.2
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7
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0035444292
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Five-base codons for incorporation of nonnatural amino acids into proteins
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This is the first report that five-base codons are decoded by aa-tRNAs containing five-base anticodons in a translation system. Sixteen five-base codons are developed for incorporation of non-natural amino acids into proteins.
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Hohsaka T., Ashizuka Y., Murakami H., Sisido M. Five-base codons for incorporation of nonnatural amino acids into proteins. Nucleic Acids Res. 29:2001;3646-3651. This is the first report that five-base codons are decoded by aa-tRNAs containing five-base anticodons in a translation system. Sixteen five-base codons are developed for incorporation of non-natural amino acids into proteins.
-
(2001)
Nucleic Acids Res
, vol.29
, pp. 3646-3651
-
-
Hohsaka, T.1
Ashizuka, Y.2
Murakami, H.3
Sisido, M.4
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8
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0035970290
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Expanding the genetic code: Selection of efficient suppressors of four-base codons and identification of 'shifty' four-base codons with a library approach in Escherichia coli
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Magliery T.J., Anderson J.C., Schultz P.G. Expanding the genetic code: selection of efficient suppressors of four-base codons and identification of 'shifty' four-base codons with a library approach in Escherichia coli. J Mol Biol. 307:2001;755-769.
-
(2001)
J Mol Biol
, vol.307
, pp. 755-769
-
-
Magliery, T.J.1
Anderson, J.C.2
Schultz, P.G.3
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9
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0036008851
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Exploring the limits of codon and anticodon size
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Anderson J.C., Magliery T.J., Schultz P.G. Exploring the limits of codon and anticodon size. Chem Biol. 9:2002;237-244.
-
(2002)
Chem Biol
, vol.9
, pp. 237-244
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Anderson, J.C.1
Magliery, T.J.2
Schultz, P.G.3
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10
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0026523058
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Ribosome-mediated incorporation of a non-standard amino acid into a peptide through expansion of the genetic code
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Bain J.D., Switzer C., Chamberlin A.R., Benner S.A. Ribosome-mediated incorporation of a non-standard amino acid into a peptide through expansion of the genetic code. Nature. 356:1992;537-539.
-
(1992)
Nature
, vol.356
, pp. 537-539
-
-
Bain, J.D.1
Switzer, C.2
Chamberlin, A.R.3
Benner, S.A.4
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11
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0036168140
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An unnatural base pair for incorporating amino acid analogs into proteins
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An artificial codon containing a non-natural base on DNA is transcribed to a mRNA, then the artificial codon on mRNA is translated to a non-natural amino acid in an E. coli extract.
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Hirao I., Ohtsuki T., Fujiwara T., Mitsui T., Yokogawa T., Okuni T., Nakayama H., Takio K., Yabuki T., Kigawa T., et al. An unnatural base pair for incorporating amino acid analogs into proteins. Nat Biotechnol. 20:2002;177-182. An artificial codon containing a non-natural base on DNA is transcribed to a mRNA, then the artificial codon on mRNA is translated to a non-natural amino acid in an E. coli extract.
-
(2002)
Nat Biotechnol
, vol.20
, pp. 177-182
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-
Hirao, I.1
Ohtsuki, T.2
Fujiwara, T.3
Mitsui, T.4
Yokogawa, T.5
Okuni, T.6
Nakayama, H.7
Takio, K.8
Yabuki, T.9
Kigawa, T.10
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12
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0035921119
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Synthesis of 6-(2-thienyl)purine nucleoside derivatives that form unnatural base pairs with pyridin-2-one nucleosides
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Fujiwara T., Kimoto M., Sugiyama H., Hirao I., Yokoyama S. Synthesis of 6-(2-thienyl)purine nucleoside derivatives that form unnatural base pairs with pyridin-2-one nucleosides. Bioorg Med Chem Lett. 11:2001;2221-2223.
-
(2001)
Bioorg Med Chem Lett
, vol.11
, pp. 2221-2223
-
-
Fujiwara, T.1
Kimoto, M.2
Sugiyama, H.3
Hirao, I.4
Yokoyama, S.5
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13
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0035942246
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Unnatural base pairs for specific transcription
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Ohtsuki T., Kimoto M., Ishikawa M., Mitsui T., Hirao I., Yokoyama S. Unnatural base pairs for specific transcription. Proc Natl Acad Sci USA. 98:2001;4922-4925.
-
(2001)
Proc Natl Acad Sci USA
, vol.98
, pp. 4922-4925
-
-
Ohtsuki, T.1
Kimoto, M.2
Ishikawa, M.3
Mitsui, T.4
Hirao, I.5
Yokoyama, S.6
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14
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0037140811
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A unique unnatural base pair between a C analogue, pseudoisocytosine, and an A analogue, 6-methoxypurine, in replication
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Hirao I., Kimoto M., Yamakage S., Ishikawa M., Kikuchi J., Yokoyama S. A unique unnatural base pair between a C analogue, pseudoisocytosine, and an A analogue, 6-methoxypurine, in replication. Bioorg Med Chem Lett. 12:2002;1391-1393.
-
(2002)
Bioorg Med Chem Lett
, vol.12
, pp. 1391-1393
-
-
Hirao, I.1
Kimoto, M.2
Yamakage, S.3
Ishikawa, M.4
Kikuchi, J.5
Yokoyama, S.6
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15
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0034835786
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Efforts toward expansion of the genetic alphabet: Replication of DNA with three base pairs
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Tae E.L., Wu Y., Xia G., Schultz P.G., Romesberg F.E. Efforts toward expansion of the genetic alphabet: replication of DNA with three base pairs. J Am Chem Soc. 123:2001;7439-7440.
-
(2001)
J Am Chem Soc
, vol.123
, pp. 7439-7440
-
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Tae, E.L.1
Wu, Y.2
Xia, G.3
Schultz, P.G.4
Romesberg, F.E.5
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16
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0034255553
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Universal bases for hybridization, replication and chain termination
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Berger M., Wu Y., Ogawa A.K., McMinn D.L., Schultz P.G., Romesberg F.E. Universal bases for hybridization, replication and chain termination. Nucleic Acids Res. 28:2000;2911-2914.
-
(2000)
Nucleic Acids Res
, vol.28
, pp. 2911-2914
-
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Berger, M.1
Wu, Y.2
Ogawa, A.K.3
McMinn, D.L.4
Schultz, P.G.5
Romesberg, F.E.6
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17
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0034682919
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Stable and selective hybridization of oligonucleotides with unnatural hydrophobic bases
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Berger M., Ogawa A.K., McMinn D.L., Wu Y., Schultz P.G., Romesberg F.E. Stable and selective hybridization of oligonucleotides with unnatural hydrophobic bases. Angew Chem Int Ed Engl. 39:2000;2940-2942.
-
(2000)
Angew Chem Int Ed Engl
, vol.39
, pp. 2940-2942
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Berger, M.1
Ogawa, A.K.2
McMinn, D.L.3
Wu, Y.4
Schultz, P.G.5
Romesberg, F.E.6
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18
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0037039298
-
Incorporation of azides into recombinant proteins for chemoselective modification by the Staudinger ligation
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An azidohomoalanine is incorporated into a protein as a methionine analogue in E. coli. The resulting protein is ligated with phosphine-labeled peptides.
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Kiick K.L., Saxon E., Tirrell D.A., Bertozzi C.R. Incorporation of azides into recombinant proteins for chemoselective modification by the Staudinger ligation. Proc Natl Acad Sci USA. 99:2002;19-24. An azidohomoalanine is incorporated into a protein as a methionine analogue in E. coli. The resulting protein is ligated with phosphine-labeled peptides.
-
(2002)
Proc Natl Acad Sci USA
, vol.99
, pp. 19-24
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Kiick, K.L.1
Saxon, E.2
Tirrell, D.A.3
Bertozzi, C.R.4
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19
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0034709379
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A new functional suppressor tRNA/aminoacyl-tRNA synthetase pair for the in vivo incorporation of unnatural amino acids into proteins
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Wang L., Magliery T.J., Liu D.R., Schultz P.G. A new functional suppressor tRNA/aminoacyl-tRNA synthetase pair for the in vivo incorporation of unnatural amino acids into proteins. J Am Chem Soc. 122:2000;5010-5011.
-
(2000)
J Am Chem Soc
, vol.122
, pp. 5010-5011
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Wang, L.1
Magliery, T.J.2
Liu, D.R.3
Schultz, P.G.4
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20
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0034833416
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A general approach for the generation of orthogonal tRNAs
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Wang L., Schultz P.G. A general approach for the generation of orthogonal tRNAs. Chem Biol. 8:2001;883-890.
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(2001)
Chem Biol
, vol.8
, pp. 883-890
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Wang, L.1
Schultz, P.G.2
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21
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0035917812
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Expanding the genetic code of Escherichia coli
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A breakthrough report describing the incorporation of a 21st amino acid into a protein in a growing E. coli. A mutated TyrRS that exclusively recognizes an amber suppressor tRNA and O-methyl-tyrosine is developed, and expressed in an E. coli together with a DHFR gene containing an amber codon. The produced DHFR contains O-methyl-tyrosine at the directed position.
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Wang L., Brock A., Herberich B., Schultz P.G. Expanding the genetic code of Escherichia coli. Science. 292:2001;498-500. A breakthrough report describing the incorporation of a 21st amino acid into a protein in a growing E. coli. A mutated TyrRS that exclusively recognizes an amber suppressor tRNA and O-methyl-tyrosine is developed, and expressed in an E. coli together with a DHFR gene containing an amber codon. The produced DHFR contains O-methyl-tyrosine at the directed position.
-
(2001)
Science
, vol.292
, pp. 498-500
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Wang, L.1
Brock, A.2
Herberich, B.3
Schultz, P.G.4
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22
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0037028931
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Adding l-3-(2-naphthyl)alanine to the genetic code of E. coli
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Wang L., Brock A., Schultz P.G. Adding l-3-(2-naphthyl)alanine to the genetic code of E. coli. J Am Chem Soc. 124:2002;1836-1837.
-
(2002)
J Am Chem Soc
, vol.124
, pp. 1836-1837
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Wang, L.1
Brock, A.2
Schultz, P.G.3
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23
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0037036727
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Addition of p-azido-l-phenylalanine to the genetic code of Escherichia coli
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Chin J.W., Santoro S.W., Martin A.B., King D.S., Wang L., Schultz P.G. Addition of p-azido-l-phenylalanine to the genetic code of Escherichia coli. J Am Chem Soc. 124:2002;9026-9027.
-
(2002)
J Am Chem Soc
, vol.124
, pp. 9026-9027
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-
Chin, J.W.1
Santoro, S.W.2
Martin, A.B.3
King, D.S.4
Wang, L.5
Schultz, P.G.6
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24
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0037143649
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Addition of a photocrosslinking amino acid to the genetic code of Escherichia coli
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This report describes a novel mutated aaRS that catalyzes an aminoacylation of tRNA with p-benzoylphenylalanine. The result raises the possibility that non-natural amino acids with large side chains may be accepted by ARSs after appropriate mutations.
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Chin J.W., Martin A.B., King D.S., Wang L., Schultz P.G. Addition of a photocrosslinking amino acid to the genetic code of Escherichia coli. Proc Natl Acad Sci USA. 99:2002;11020-11024. This report describes a novel mutated aaRS that catalyzes an aminoacylation of tRNA with p-benzoylphenylalanine. The result raises the possibility that non-natural amino acids with large side chains may be accepted by ARSs after appropriate mutations.
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(2002)
Proc Natl Acad Sci USA
, vol.99
, pp. 11020-11024
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Chin, J.W.1
Martin, A.B.2
King, D.S.3
Wang, L.4
Schultz, P.G.5
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25
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0037033377
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Expanding the genetic code
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This is a review of expanded translation systems for introducing non-natural amino acids into proteins. Recent work of author's group are described.
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Wang L., Schultz P.G. Expanding the genetic code. Chem Commun. 7:2002;1-11. This is a review of expanded translation systems for introducing non-natural amino acids into proteins. Recent work of author's group are described.
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(2002)
Chem Commun
, vol.7
, pp. 1-11
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Wang, L.1
Schultz, P.G.2
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26
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0037162453
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An engineered Escherichia coli tyrosyl-tRNA synthetase for site-specific incorporation of an unnatural amino acid into proteins in eukaryotic translation and its application in a wheat germ cell-free system
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A mutated TyrRS catalyzes an aminoacylation of a nonsense suppressor tRNA with a non-natural amino acid, m-iodotyrosine. The resulting aminoacyl-tRNA introduces iodotyrosine into a desired position of proteins in a wheat germ translation system. This system, enabling the introduction of iodine into specific positions of proteins, will be useful for X-ray structure analyses.
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Kiga D., Sakamoto K., Kodama K., Kigawa T., Matsuda T., Yabuki T., Shirouzu M., Harada Y., Nakayama H., Takio K., et al. An engineered Escherichia coli tyrosyl-tRNA synthetase for site-specific incorporation of an unnatural amino acid into proteins in eukaryotic translation and its application in a wheat germ cell-free system. Proc Natl Acad Sci USA. 99:2002;9715-9720. A mutated TyrRS catalyzes an aminoacylation of a nonsense suppressor tRNA with a non-natural amino acid, m-iodotyrosine. The resulting aminoacyl-tRNA introduces iodotyrosine into a desired position of proteins in a wheat germ translation system. This system, enabling the introduction of iodine into specific positions of proteins, will be useful for X-ray structure analyses.
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(2002)
Proc Natl Acad Sci USA
, vol.99
, pp. 9715-9720
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Kiga, D.1
Sakamoto, K.2
Kodama, K.3
Kigawa, T.4
Matsuda, T.5
Yabuki, T.6
Shirouzu, M.7
Harada, Y.8
Nakayama, H.9
Takio, K.10
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27
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0035807914
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Import of amber and ochre suppressor tRNAs into mammalian cells: A general approach to site-specific insertion of amino acid analogues into proteins
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Kohrer C., Xie L., Kellerer S., Varshney U., RajBhandary U.L. Import of amber and ochre suppressor tRNAs into mammalian cells: a general approach to site-specific insertion of amino acid analogues into proteins. Proc Natl Acad Sci USA. 98:2001;14310-14315.
-
(2001)
Proc Natl Acad Sci USA
, vol.98
, pp. 14310-14315
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Kohrer, C.1
Xie, L.2
Kellerer, S.3
Varshney, U.4
RajBhandary, U.L.5
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28
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0035956903
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Twenty-first aminoacyl-tRNA synthetase-suppressor tRNA pairs for possible use in site-specific incorporation of amino acid analogues into proteins in eukaryotes and in eubacteria
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Kowal A.K., Kohrer C., RajBhandary U.L. Twenty-first aminoacyl-tRNA synthetase-suppressor tRNA pairs for possible use in site-specific incorporation of amino acid analogues into proteins in eukaryotes and in eubacteria. Proc Natl Acad Sci USA. 98:2001;2268-2273.
-
(2001)
Proc Natl Acad Sci USA
, vol.98
, pp. 2268-2273
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Kowal, A.K.1
Kohrer, C.2
RajBhandary, U.L.3
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29
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0035674323
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Concurrent molecular recognition of the amino acid and tRNA by a ribozyme
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Saito H., Watanabe K., Suga H. Concurrent molecular recognition of the amino acid and tRNA by a ribozyme. RNA. 7:2001;1867-1878.
-
(2001)
RNA
, vol.7
, pp. 1867-1878
-
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Saito, H.1
Watanabe, K.2
Suga, H.3
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30
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0034838173
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A ribozyme exclusively aminoacylates the 3′-hydroxyl group of the tRNA terminal adenosine
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Saito H., Suga H. A ribozyme exclusively aminoacylates the 3′-hydroxyl group of the tRNA terminal adenosine. J Am Chem Soc. 123:2001;7178-7179.
-
(2001)
J Am Chem Soc
, vol.123
, pp. 7178-7179
-
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Saito, H.1
Suga, H.2
-
31
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0037134798
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Aminoacyl-tRNA synthesis by a resin-immobilized ribozyme
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Murakami H., Bonzagni N.J., Suga H. Aminoacyl-tRNA synthesis by a resin-immobilized ribozyme. J Am Chem Soc. 124:2002;6834-6835.
-
(2002)
J Am Chem Soc
, vol.124
, pp. 6834-6835
-
-
Murakami, H.1
Bonzagni, N.J.2
Suga, H.3
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32
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0035989650
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A tRNA aminoacylation system for non-natural amino acids based on a programmable ribozyme
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This paper describes the ribozyme-mediated aminoacylation of tRNAs. Addition of a tRNA recognition domain selected from a random pool to a previously developed acyl-transfer ribozyme gives a novel ribozyme that aminoacylates specific tRNAs with α- or ε-biotinylated amino acids.
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Bessho Y., Hodgson D.R., Suga H. A tRNA aminoacylation system for non-natural amino acids based on a programmable ribozyme. Nat Biotechnol. 20:2002;723-728. This paper describes the ribozyme-mediated aminoacylation of tRNAs. Addition of a tRNA recognition domain selected from a random pool to a previously developed acyl-transfer ribozyme gives a novel ribozyme that aminoacylates specific tRNAs with α- or ε-biotinylated amino acids.
-
(2002)
Nat Biotechnol
, vol.20
, pp. 723-728
-
-
Bessho, Y.1
Hodgson, D.R.2
Suga, H.3
-
33
-
-
0033637431
-
Unnatural amino acids as probes of protein structure and function
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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
-
34
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0034816479
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Incorporation of caged cysteine and caged tyrosine into a transmembrane segment of the nicotinic ACh receptor
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Philipson K.D., Gallivan J.P., Brandt G.S., Dougherty D.A., Lester H.A. Incorporation of caged cysteine and caged tyrosine into a transmembrane segment of the nicotinic ACh receptor. Am J Physiol Cell Physiol. 281:2001;C195-C206.
-
(2001)
Am J Physiol Cell Physiol
, vol.281
-
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Philipson, K.D.1
Gallivan, J.P.2
Brandt, G.S.3
Dougherty, D.A.4
Lester, H.A.5
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35
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0035003359
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Tyrosine decaging leads to substantial membrane trafficking during modulation of an inward rectifier potassium channel
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Tong Y., Brandt G.S., Li M., Shapovalov G., Slimko E., Karschin A., Dougherty D.A., Lester H.A. Tyrosine decaging leads to substantial membrane trafficking during modulation of an inward rectifier potassium channel. J Gen Physiol. 117:2001;103-118.
-
(2001)
J Gen Physiol
, vol.117
, pp. 103-118
-
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Tong, Y.1
Brandt, G.S.2
Li, M.3
Shapovalov, G.4
Slimko, E.5
Karschin, A.6
Dougherty, D.A.7
Lester, H.A.8
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36
-
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0035113738
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The tethered agonist approach to mapping ion channel proteins - Toward a structural model for the agonist binding site of the nicotinic acetylcholine receptor
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Incorporation of agonist-linked amino acids into an acetylcholine receptor gives a constitutively active receptor. The result provides a useful tool for probing structures of ligand-binding sites of proteins.
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Li L., Zhong W., Zacharias N., Gibbs C., Lester H.A., Dougherty D.A. The tethered agonist approach to mapping ion channel proteins - toward a structural model for the agonist binding site of the nicotinic acetylcholine receptor. Chem Biol. 8:2001;47-58. Incorporation of agonist-linked amino acids into an acetylcholine receptor gives a constitutively active receptor. The result provides a useful tool for probing structures of ligand-binding sites of proteins.
-
(2001)
Chem Biol
, vol.8
, pp. 47-58
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Li, L.1
Zhong, W.2
Zacharias, N.3
Gibbs, C.4
Lester, H.A.5
Dougherty, D.A.6
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37
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0037176865
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Chemically mediated site-specific proteolysis. Alteration of protein-protein interaction
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This paper describes a useful strategy to cleave a polypeptide chain internally through an iodination of allylglycine incorporated at desired positions of proteins.
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Wang B., Brown K.C., Lodder M., Craik C.S., Hecht S.M. Chemically mediated site-specific proteolysis. Alteration of protein-protein interaction. Biochemistry. 41:2002;2805-2813. This paper describes a useful strategy to cleave a polypeptide chain internally through an iodination of allylglycine incorporated at desired positions of proteins.
-
(2002)
Biochemistry
, vol.41
, pp. 2805-2813
-
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Wang, B.1
Brown, K.C.2
Lodder, M.3
Craik, C.S.4
Hecht, S.M.5
-
38
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0034711375
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Generation of active trypsin by chemical cleavage
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Baird T. Jr, Wang B., Lodder M., Hecht S.M., Craik C.S. Generation of active trypsin by chemical cleavage. Tetrahedoron. 56:2000;9477-9485.
-
(2000)
Tetrahedoron
, vol.56
, pp. 9477-9485
-
-
Baird T., Jr.1
Wang, B.2
Lodder, M.3
Hecht, S.M.4
Craik, C.S.5
-
39
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0035969932
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Studies toward the site specific incorporation of sugars into proteins: Synthesis of glycosylated aminoacyl-tRNAs
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Fahmi N.E., Golovine S., Wang B., Hecht S.M. Studies toward the site specific incorporation of sugars into proteins: synthesis of glycosylated aminoacyl-tRNAs. Carbohydr Res. 330:2001;149-164.
-
(2001)
Carbohydr Res
, vol.330
, pp. 149-164
-
-
Fahmi, N.E.1
Golovine, S.2
Wang, B.3
Hecht, S.M.4
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40
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0037005999
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Photoswitching of peroxidase activity by position-specific incorporation of a photoisomerizable non-natural amino acid into horseradish peroxidase
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Muranaka N., Hohsaka T., Sisido M. Photoswitching of peroxidase activity by position-specific incorporation of a photoisomerizable non-natural amino acid into horseradish peroxidase. FEBS Lett. 510:2002;10-12.
-
(2002)
FEBS Lett
, vol.510
, pp. 10-12
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-
Muranaka, N.1
Hohsaka, T.2
Sisido, M.3
-
41
-
-
0034157693
-
Site-directed incorporation of fluorescent nonnatural amino acids into streptavidin for highly sensitive detection of biotin
-
Murakami H., Hohsaka T., Ashizuka Y., Hashimoto K., Sisido M. Site-directed incorporation of fluorescent nonnatural amino acids into streptavidin for highly sensitive detection of biotin. Biomacromolecules. 1:2000;118-125.
-
(2000)
Biomacromolecules
, vol.1
, pp. 118-125
-
-
Murakami, H.1
Hohsaka, T.2
Ashizuka, Y.3
Hashimoto, K.4
Sisido, M.5
-
42
-
-
0035914118
-
A non-natural amino acid for efficient incorporation into proteins as a sensitive fluorescent probe
-
Taki M., Hohsaka T., Murakami H., Taira K., Sisido M. A non-natural amino acid for efficient incorporation into proteins as a sensitive fluorescent probe. FEBS Lett. 507:2001;35-38.
-
(2001)
FEBS Lett
, vol.507
, pp. 35-38
-
-
Taki, M.1
Hohsaka, T.2
Murakami, H.3
Taira, K.4
Sisido, M.5
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