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1  cysteine codon has been replaced by the UAG amber codon.
2 ally encode this initiator in response to an amber codon.
3 the MaThg1 gene and transcript confirmed the amber codon.
4 red compared to results using the three-base amber codon.
5 rporation of N(epsilon)-Boc-lysine (BocK) at amber codon.
6 lalanines for their genetic incorporation at amber codon.
7 ural amino acid incorporation in response to amber codons.
8 ngle amber codon and from <1% to >20% on two amber codons.
9 tRNAs function efficiently in suppression of amber codons.
10 Thg1 (MaThg1) gene contains an in-frame TAG (amber) codon.
11 art and a stop that can even be a suppressed amber codon 22 nucleotides further downstream from the r
12 yl- l-phenylalanine (Bpa) in response to the amber codon allowed the biosynthesis of Bpa-substituted
13 ded this unique amino acid in response to an amber codon allowing a single 1 to be placed at any loca
14 n from approximately 20% to >60% on a single amber codon and from <1% to >20% on two amber codons.
15 mino acid incorporation, in response to both amber codons and sense codons, with an efficiency simila
16 red anticodons which bind to a UAG nonsense (amber) codon and to the Arg (AGG), Asn (AAC,AAT), Gln (C
17  cognate orthogonal tRNA that recognizes the amber codon, are encoded on the plasmid pSUPAR6-L3-3SY,
18 ne is a likely first step in translating UAG amber codons as pyrrolysine in certain methanogens.
19 media and the protein of interest with a TAG amber codon at the desired incorporation site.
20 1 gene product did not cease at the internal amber codon, but at the following ochre codon.
21 stal structure of MtmB demonstrated that the amber codon codes for pyrrolysine, the 22nd genetically
22 ns, each inserting a different amino acid at amber codons, created 12 different substitutions at the
23  addition reaction between a cysteine and an amber-codon-encoded N(e) -acryloyl-lysine (AcrK).
24 hile triplet nonsense codons, especially the amber codon, have been widely employed, quadruplet codon
25 sor tRNA gene resulted in suppression of the amber codon in a reporter chloramphenicol acetyltransfer
26 denosine to an inosine (I) within the HDAg-S amber codon in antigenomic RNA.
27 ndred ncAAs have been genetically encoded by amber codon in both prokaryotes and eukaryotes using wil
28  of unnatural amino acids in response to the amber codon in Escherichia coli.
29             Pyrrolysine is represented by an amber codon in genes encoding proteins such as the methy
30  Pyrrolysine is an amino acid encoded by the amber codon in genes required for methylamine utilizatio
31 oration of this amino acid in response to an amber codon in mammalian cells.
32 e activity in vitro is not solely due to the amber codon in ureD.
33  can incorporate noncanonical amino acids at amber codons in IVT, including the novel substrate p-cya
34 ereby, tetracycline-regulated suppression of amber codons in mammalian HeLa and COS-1 cells.
35 system that site-specifically--using the UAG amber codon--inserts Sec depending on the elongation fac
36    Expression of pylTSBCD also suppressed an amber codon introduced into the E. coli uidA gene.
37                                          The amber codon is recognized in the 30S subunit-decoding ce
38                                          The amber codon is thus read through during translation at a
39                     In nearly all cases, the amber codon is used as a sense codon, and an orthogonal
40 functionally important Lys was altered to an amber codon, or to Arg, Asn, Gln, Glu, Thr and Trp codon
41 -X) improves tRNA(CUA)-dependent decoding of amber codons placed in orthogonal mRNA.
42                                          The amber codon position corresponded to a lysyl residue usi
43 ecodes a series of quadruplet codons and the amber codon, providing several blank codons on an orthog
44  the radical trap 3-amino tyrosine (NH2Y) by amber codon suppression at positions Y731 or Y730 and in
45                                              Amber codon suppression for the insertion of non-natural
46                              Here we utilize amber codon suppression in a membrane-bound transporter
47 ite-specific incorporation into proteins via amber codon suppression in Escherichia coli and mammalia
48 vo incorporation of unnatural amino acids by amber codon suppression is limited by release factor-1-m
49 S can be redesigned to achieve high-fidelity amber codon suppression through delivery of p-bromopheny
50                                      We used amber codon suppression to generate a phosphorylated Ser
51                                      We used amber codon suppression to introduce the photoreactive u
52           This analysis was enabled by using amber codon suppression to obtain phosphorylated pS76-NA
53 site-specific introduction into proteins via amber codon suppression using the wild-type pyrrolysyl-t
54 ters and (ii) selection of tRNA for enhanced amber codon suppression.
55 e introduced into the cpTMV monomers through amber codon suppression.
56 , 4-ethynyl-l-phenylalanine (F(CC)), through amber codon suppression.
57 tem cells and mouse embryonic fibroblasts to amber codon suppression.
58          Pyrrolysine (Pyl) is encoded by the amber codon (TAG/UAG) and is widespread in archaea, wher
59 teins in Escherichia coli in response to the amber codon, TAG.
60 s possesses one naturally occurring in-frame amber codon that does not appear to act as a translation
61 nzymes are encoded by genes with an in-frame amber codon that is translated as pyrrolysine.
62 efficiently incorporated at a predefined UAG amber codon, thereby competing with RF1 rather than RF2.
63 fluoromethylphenylalanine in response to the amber codon UAG.
64 g the efficiency of suppression at a gene II amber codon upstream from the gene X start, the already
65 f the suppressor tRNA and suppression of the amber codon were reduced significantly in the presence o
66  into COS1 cells and acts as a suppressor of amber codons, whereas the same suppressor tRNA imported
67 ne dihydrofolate reductase in response to an amber codon with at least 98% fidelity.
68 ight unnatural amino acids in response to an amber codon with high yields and fidelities.
69  enable ncAA-dependent translation at single amber codons with similar efficiency as natural translat
70 creasing the efficiency of suppression at an amber codon within the gene.
71 tigate the means by which suppression of the amber codon within these genes occurs, MtmB, a methyltra