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1 e 2) and a gene from the plastid genome (the elongation factor Tu).
2 ibosomal peptidyl transferase center and the elongation factor Tu.
3 t is unable to substitute for either EF-G or elongation factor Tu.
4 d the Ser-tRNA(Thr) level in the presence of elongation factor Tu.
5 gests a common GTPase mechanism for EF-G and elongation factor Tu.
6 d further ensured through collaboration with elongation factor Tu.
7 ding to either the 50 S ribosomal subunit or elongation factor Tu.
8 and the presence and the absence of AMP and elongation factor Tu.
9 nd presence of inorganic pyrophosphatase and elongation factor Tu.
10 second domain in the eukaryotic translation elongation factor-Tu.
11 y cleaves the host translation factor EF-Tu (elongation factor Tu) after it has formed a weak complex
12 e tmRNA enters the ribosome with the help of elongation factor Tu and a protein factor called small p
14 n of aminoacyl-tRNAs in ternary complex with elongation factor Tu and GTP on messenger RNA-programmed
16 yl-tRNA (aa-tRNA), in a ternary complex with elongation factor-Tu and GTP, enters the aminoacyl (A) s
19 ture of the complex between Escherichia coli elongation factors Tu and Ts (EF-Tu.Ts) and subsequent m
20 d include type IV secretion system proteins, elongation factor Tu, and members of the MSP2 superfamil
21 associated with the S1 subunit, site II with elongation factor Tu, and polymerization with the viral
22 stal structure of a tmRNA fragment, SmpB and elongation factor Tu bound to the ribosome at 3.2 angstr
23 ts decoding site, to accelerate the rates of elongation factor-Tu-catalyzed GTP hydrolysis and riboso
24 e can position either elongation factor G or elongation factor Tu complexed with an aminoacylated tra
26 earlier that surface-localized M. pneumoniae elongation factor Tu (EF-Tu(Mp)) mediates binding to the
28 In plants, the bacterial MAMPs flagellin and elongation factor Tu (EF-Tu) activate distinct, phylogen
29 s as a nucleotide-exchange factor by binding elongation factor Tu (EF-Tu) and accelerating the GDP di
31 is critical for triggering GTP hydrolysis on elongation factor Tu (EF-Tu) and elongation factor G (EF
32 lying the orderly, sequential association of elongation factor Tu (EF-Tu) and elongation factor G (EF
33 programmed ribosome in ternary complex with elongation factor Tu (EF-Tu) and GTP and then, again, in
36 receptor (EFR) recognizes the bacterial PAMP elongation factor Tu (EF-Tu) and its derived peptide elf
37 5 and the 30 kDa proteins identified them as elongation factor Tu (EF-Tu) and pyruvate dehydrogenase
45 ydroxyl groups in stabilizing a complex with elongation factor Tu (EF-Tu) from Thermus thermophilus.
46 Recent evidence indicates that translation elongation factor Tu (EF-Tu) has a role in the cell in a
50 rvations of cross-reactivity with the 45-kDa elongation factor Tu (EF-Tu) protein from Chlamydia trac
51 cerevisiae tRNA Phe to Thermus thermophilus elongation factor Tu (EF-Tu) revealed that much of the s
53 ontained within a similar PGH motif found in elongation factor Tu (EF-Tu) that is required for GTP hy
56 As (aa-tRNAs) have evolved to bind bacterial elongation factor Tu (EF-Tu) with uniform affinities, mu
57 d for their affinity to Thermus thermophilus elongation factor Tu (EF-Tu)*GTP by using a ribonuclease
60 he cellular levels of alanine synthetase and elongation factor TU (EF-Tu), the amount of tRNA and the
61 e ribosome is limited by its poor binding to elongation factor Tu (EF-Tu), the yield of incorporation
62 ein synthesis is promoted by two G proteins, elongation factor Tu (EF-Tu), which delivers aminoacyl t
63 e triphosphatase (GTPase) factors, including elongation factor Tu (EF-Tu), which delivers aminoacyl-t
64 inoacyl-tRNA is delivered to the ribosome by elongation factor Tu (EF-Tu), which hydrolyzes guanosine
65 ne cluster responsible for production of the elongation factor Tu (EF-Tu)-targeting 29-member thiazol
75 e misacylated tRNAs for Thermus thermophilus elongation factor Tu (EF-Tu).GTP were determined using a
76 ported that surface-associated M. pneumoniae elongation factor Tu (EF-Tu, also called MPN665) serves
77 at overexpressed Hsp33 specifically binds to elongation factor-Tu (EF-Tu) and targets it for degradat
79 s GTPase activating protein (RasGAP) and the elongation factor-Tu (EF-Tu) with a 1 W mechanism is sti
81 ith peptides derived from flagellin (flg22), elongation factor-Tu (elf18), or an endogenous protein (
82 '-yl imidodiphosphate) but not [14C]Phe-tRNA.elongation factor Tu.GDP.kirromycin increased labeling o
84 s as good as between elongation factor G and elongation factor Tu-guanosine-5'(beta,gamma-imido)triph
85 he co-crystal structure of Thermus aquaticus elongation factor Tu.guanosine 5'- [beta,gamma-imido]tri
86 Binding of the ternary complex [14C]Phe-tRNA-elongation factor Tu.guanyl-5'-yl imidodiphosphate) but
88 tation, driven by a conformational change in elongation factor Tu involving GTP hydrolysis, transorie
89 eEF1A, the eukaryotic homologue of bacterial elongation factor Tu, is a well characterized translatio
90 ves the elf18 peptide derived from bacterial elongation factor Tu, is activated upon ligand binding b
92 Glucose 6-phospatase, alcohol dehydrogenase, elongation factor-TU, methylglutaryl coenzyme A (CoA), a
93 major antigenic outer membrane protein MgPa, elongation factor Tu, pyruvate dehydrogenase E1alpha, an
94 Previous studies have shown that bacterial elongation factor Tu receptor (EFR), a pattern-recogniti
95 A similar approach with swaps between the Elongation factor-Tu receptor and BAK1 also resulted in
97 -kDa protein was 100% identical to bacterial elongation factor Tu, suggesting a role as a possible ch
98 mpete for aminoacyl-tRNAs in the presence of elongation factor Tu, suggesting that YbaK acts before r
99 Cleavage of SRL slightly affected binding of elongation factor Tu ternary complex (EF-Tu*GTP*tRNA) to
101 70-80% in levels of mRNA for the chloroplast elongation factor Tu (tufA) in asynchronously growing Ch
102 Levels of mRNA for the chloroplast-encoded elongation factor Tu (tufA) showed a dramatic daily osci
103 e of the most abundant proteins in the cell, elongation factor Tu, was found to be more oxidatively m
104 1, glutamate dehydrogenase, gamma-actin, and elongation factor Tu were identified as increasingly car
105 identify amino acids in Thermus thermophilus elongation factor Tu which contribute to its specificity
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