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1 by RRF (ribosome recycling factor) and EF-G (elongation factor G).
2 compensated by mutations in the translation elongation factor G.
3 mbled by ribosome recycling factor (RRF) and elongation factor G.
6 on change in Efl1 equivalent to changes that elongation factor G and eEF2 undergo during translocatio
7 he two release factors is as good as between elongation factor G and elongation factor Tu-guanosine-5
9 osomes at a site that coincides with that of elongation factor G and has a GTPase activity that is se
11 st our method on the experimental cryo-EM of elongation factor G and show that the model obtained is
13 ver, the antibiotic has negligible effect on elongation factor G catalyzed translocation of tRNA and
15 e single-dimer ribosomal particles supported elongation factor G dependent GTP hydrolysis and protein
16 scribe a new sensitive method for monitoring elongation factor G-dependent translocation of the mRNA
17 of this base-pair in peptide bond formation, elongation factor G-dependent translocation, and peptide
19 iostrepton, which inhibits the activities of elongation factor G (EF-G) and EF-Tu by binding to the r
21 enger RNA (mRNA), in a reaction catalyzed by elongation factor G (EF-G) and guanosine triphosphate (G
22 The antibiotic fusidic acid (FA) targets elongation factor G (EF-G) and inhibits ribosomal peptid
24 ion (ALC) is formed between the G' domain of elongation factor G (EF-G) and the L7/L12-stalk base of
27 nt crystal structures of G proteins, such as elongation factor G (EF-G) bound to the ribosome, as wel
28 bits bacterial protein synthesis by blocking elongation factor G (EF-G) catalyzed translocation of me
31 ibosome recycling factor (RRF) together with elongation factor G (EF-G) disassembles the post- termin
32 complex through the ribosome is promoted by elongation factor G (EF-G) during the translation cycle.
33 ction of ribosome recycling factor (RRF) and elongation factor G (EF-G) in a guanosine 5'-triphosphat
34 ersally conserved ribosome-dependent GTPase [elongation factor G (EF-G) in prokaryotes and elongation
40 the ribosomal translocation, the binding of elongation factor G (EF-G) to the pretranslocational rib
43 ociation of elongation factor Tu (EF-Tu) and elongation factor G (EF-G) with the ribosome during prot
44 ation step of prokaryotic protein synthesis, elongation factor G (EF-G), a guanosine triphosphatase (
45 tion of the ribosome-recycling factor (RRF), elongation factor G (EF-G), and GTP to prepare the ribos
46 bosome-recycling factor (RRF), together with elongation factor G (EF-G), disassembles this posttermin
47 Tet(M) protein, which displays homology to elongation factor G (EF-G), interacts with the protein b
49 rotated state is not a proper substrate for elongation factor G (EF-G), thus inhibiting translocatio
50 elivers aminoacyl tRNAs to the ribosome, and elongation factor G (EF-G), which catalyzes translocatio
62 presence of the antibiotic thiostrepton and elongation factor-G (EF-G) rigorously localized the bind
63 ogenic bacteria Staphylococcus aureus, locks elongation factor-G (EF-G) to the ribosome after GTP hyd
65 ional ribosome complexes and to compete with elongation factor G for interaction with pretranslocatio
67 domains could facilitate the association of elongation factor-G into lipid rafts in living bacteria,
73 m the A to the P-site upon GTP hydrolysis by elongation factor G, shifting approximately 8 A toward t
74 domain (L11-NTD) may variously interact with elongation factor G, the antibiotic thiostrepton, and rR
76 recycling factor (RRF) is used together with elongation factor G to recycle the 30S and 50S ribosomal
77 mal protein S5 and the ribosomal translocase elongation factor G, which suggests evolution from a com
78 d also shows time-dependent enhancement when elongation factor G with GTP is added to 70S ribosomes.
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