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1 in binding also prevented readthrough of the UGA codon.
2 factor and tRNA(Sec) needed to reassign the UGA codon.
3 ts specific incorporation is directed by the UGA codon.
4 ational incorporation of selenocysteine at a UGA codon.
5 al and collaborated in Sec insertion at each UGA codon.
6 he compounding effect of termination at each UGA codon.
7 a provided that it is spatially close to the UGA codon.
8 ial of the SECIS flanking region and the Sec UGA codon.
9 stem loop starting six nucleotides 3' of the UGA codon.
10 ementary to the region downstream of the Sec UGA codon.
11 ination at UAA and UAG codons but not at the UGA codon.
12 dant enzyme by promoting substitution at the UGA codon.
13 mino acid selenocysteine, as directed by the UGA codon.
14 er polypeptide chain, encoded by an in-frame UGA codon.
15 carboxyl terminus and which is encoded by a UGA codon.
16 and facilitates its misincorporation at Sec UGA codons.
17 terminate at the second, third, and seventh UGA codons.
18 itive to antibiotics due to its ten in frame UGA codons.
19 proximately 10-fold at subsequent downstream UGA codons.
20 ynthesis but cannot decode the mitochondrial UGA codons.
21 ptide release at UAA and UAG codons, but not UGA codons.
22 and distinct roles for SECIS1 and SECIS2 at UGA codons.
23 the coding regions immediately downstream of UGA codons.
24 in vertebrates may contain up to 22 in-frame UGA codons.
25 ife by dynamic translational redefinition of UGA codons.
26 any of these are followed with nearby UAA or UGA codons.
27 l insertion of selenocysteine in response to UGA codons.
29 n initiation, structures located adjacent to UGA codons, additional coding sequence regions necessary
32 as most selenoprotein mRNAs contain a single UGA codon and a single SECIS element, selenoprotein P ge
33 nation of translation at the second in-frame UGA codon and all of the 10 in-frame UGA codons being re
34 loop RNA structure immediately following the UGA codon and forms part of the coding sequence in bacte
36 to the primary sequence arrangement between UGA codons and SECIS elements, their proximity within th
37 nthesis and insertion of Cys into protein at UGA codons and suggest new biological functions for thio
39 tion RNA structures, the coding potential of UGA codons, and the presence of cysteine-containing homo
40 teine Insertion Sequence (SECIS) element and UGA codon are sufficient for selenocysteine (Sec) insert
41 n the 3'-untranslated region and an in-frame UGA codon are the requisite cis-acting elements for the
43 s by translational recoding whereby in-frame UGA codons are redefined to encode the selenium containi
44 of selenoproteins requires the decoding of a UGA codon as selenocysteine (Sec) instead of translation
46 that the percentage of ribosomes decoding a UGA codon as selenocysteine rather than termination can
47 ncorporation (i.e., after decoding the first UGA codon as selenocysteine) are fully competent to term
49 ral mRNAs, they instruct ribosomes to decode UGA codons as selenocysteine (Sec, U) codons instead of
52 ntain a selenocysteine residue, encoded by a UGA codon, as the penultimate carboxyl-terminal amino ac
53 on model that incorporated Sec at non-native UGA codons at rates equal to those of endogenous glutath
55 -nucleotide-long fragments representing each UGA codon context into a luciferase reporter construct h
56 verexpressing eRF1 and eRF3, and of altering UGA codon context, on the efficiency of selenoprotein sy
58 the inefficient incorporation of Sec at the UGA codon during mRNA translation augments the nonsense-
59 Sec or Cys in MsrBs, whereas the three other UGA codons evolved recently and had no homologs with Sec
60 chain as compared with selenocysteine at the UGA codon, expression of the catalytically inactive Gpx4
62 -kDa GFP/GPX1 proteins, Sec incorporation at UGA codons, formerly close to the 5' or 3' ends, was inc
67 They raise the possibility that the second UGA codon in selenoprotein P mRNA can have alternative f
68 uence element approximately 4.8 kb 3' to the UGA codon in the active center and three short open read
70 first is a conserved, inefficiently decoded UGA codon in the N-terminal region, which appears to ser
76 djacent to, or near, selenocysteine-encoding UGA codons in the Sps2, SelH, SelO, and SelT selenoprote
77 e conductance regulator (CFTR) W1282X PTC (a UGA codon) in the context of its three upstream and down
78 ocysteine incorporation element along with a UGA codon into a reporter construct allows for read-thro
79 Selenocysteine incorporation at the first UGA codon is inefficient but increases by approximately
80 on of selenocysteine (Sec) into protein, the UGA codon is transformed from one that signals translati
81 ocysteine (Sec) into proteins in response to UGA codons is directed by selenocysteine insertion seque
82 steine incorporation as the distance between UGA codons is increased, and that efficient selenocystei
83 he inefficiently decoded GPX4 selenocysteine UGA codon, leading to ribosome collisions, early transla
84 rected by translational recoding of specific UGA codons located upstream of a stem-loop structure kno
86 ec incorporation at the first and downstream UGA codons occurs with variable efficiencies to control
87 D helix in ribosomes stalled at the in-frame UGA codon of prfB generates tension on the mRNA that des
89 G read-through element upstream of the first UGA codon or by providing a competing messenger RNA in t
91 that Sec is more efficiently incorporated at UGA codons positioned in the middle of the coding region
93 ts direct incorporation of selenocysteine at UGA codons, provided the SECIS element lies a sufficient
95 he stem (G1922) is specifically critical for UGA codon recognition by the class 1 release factor RF2.
96 ocysteine (Sec) into proteins in response to UGA codons requires a cis-acting RNA structure, Sec inse
99 t immediately upstream and downstream of the UGA codon significantly affects termination to incorpora
100 75)Se labeling showed that all four in-frame UGA codons supported Sec insertion and that both SECIS e
102 nic amino acid encoded by a recoded in-frame UGA codon that does not operate as the canonical opal st
103 lutathione peroxidase 1 (Se-GPx1) contains a UGA codon that is recognized as a codon for the nonstand
104 ec-tRNA(Sec)) to the ribosome and suppresses UGA codons that are upstream of Sec insertion sequence (
105 diated decay due to the presence of in-frame UGA codons that can be decoded as either selenocysteine
106 co-translationally incorporated at specific UGA codons that normally serve as termination signals.
107 fic expansion of the genetic code allows for UGA codons to specify the amino acid selenocysteine (Sec
109 on in eukaryotes occurs cotranslationally at UGA codons via the interactions of RNA-protein complexes
111 Although the major readthrough event at the UGA codon was insertion of tryptophan, Sec was also inco
112 n immediately downstream of the Sec-encoding UGA codon, whereas in eukaryotes a completely different
113 e the unusual amino acid selenocysteine at a UGA codon, which conventionally serves as a termination
114 of selenoprotein messages by redefinition of UGA codons, which normally specify termination of transl
117 n, we used a reporter gene system that has a UGA codon within the protein-coding region of the lucife
118 is inserted cotranslationally in response to UGA codons within selenoprotein mRNAs in a process requi