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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.
4                            This implies that elongation factor G actively pushes both the decoding si
5 ent translational GTPase factors, along with elongation factor G and BPI-inducible protein A.
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
8                        Subsequent binding of elongation factor G and GTP hydrolysis results in a cloc
9 osomes at a site that coincides with that of elongation factor G and has a GTPase activity that is se
10                     The translation factors, elongation factor G and ribosome recycling factor, are k
11 st our method on the experimental cryo-EM of elongation factor G and show that the model obtained is
12 ational GTPase (trGTPase) factors along with elongation factors G and 4 (EF-G and EF4).
13 ver, the antibiotic has negligible effect on elongation factor G catalyzed translocation of tRNA and
14                                              Elongation factor-G-catalyzed translocation of mRNA 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
18 inked ribosomes were specifically blocked in elongation factor G-dependent translocation.
19 iostrepton, which inhibits the activities of elongation factor G (EF-G) and EF-Tu by binding to the r
20             Ribosome recycling factor (RRF), elongation factor G (EF-G) and GTP split 70S ribosomes i
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
23                                              Elongation factor G (EF-G) and ribosome recycling factor
24 ion (ALC) is formed between the G' domain of elongation factor G (EF-G) and the L7/L12-stalk base of
25                    During protein synthesis, elongation factor G (EF-G) binds to the ribosome and pro
26                After peptide-bond formation, elongation factor G (EF-G) binds to the ribosome, trigge
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
29        The guanosine triphosphatase (GTPase) elongation factor G (EF-G) catalyzes the subsequent move
30             The universally conserved GTPase elongation factor G (EF-G) catalyzes the translocation o
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
35 coding region, resulting from the binding of elongation factor G (EF-G) in various forms.
36                Initiation factor 2 (IF2) and elongation factor G (EF-G) induce similar changes in rib
37                                              Elongation factor G (EF-G) is a guanosine triphosphatase
38                                              Elongation factor G (EF-G) is a universally conserved tr
39                                   Binding of elongation factor G (EF-G) shifts this equilibrium towar
40  the ribosomal translocation, the binding of elongation factor G (EF-G) to the pretranslocational rib
41                                              Elongation factor G (EF-G) was identified as one possibl
42                 In contrast, the activity of elongation factor G (EF-G) was strongly impaired in alph
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
48                       These proteins bind to elongation factor G (EF-G), the target of FA, and rescue
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
51             We observed significantly slower elongation factor G (EF-G)-catalyzed translocation throu
52           Cryo-EM reconstructions of certain elongation factor G (EF-G)-containing complexes have led
53 zed by the guanosine triphosphatase (GTPase) elongation factor G (EF-G).
54 drolysis on elongation factor Tu (EF-Tu) and elongation factor G (EF-G).
55 nslation by interfering with the function of elongation factor G (EF-G).
56 n of the ribosome-recycling factor (RRF) and elongation factor G (EF-G).
57 nslocation through the ribosome catalyzed by elongation factor G (EF-G).
58 anied by large interdomain rearrangements of elongation factor G (EF-G).
59                This reaction is catalyzed by elongation factor-G (EF-G) and is associated with riboso
60          Ribosome recycling factor (RRF) and elongation factor-G (EF-G) are jointly essential for rec
61      The ribosome-recycling factor (RRF) and elongation factor-G (EF-G) disassemble the 70S post-term
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
64 R) of an orthologue of bacterial translation elongation factor G (EFG).
65 ional ribosome complexes and to compete with elongation factor G for interaction with pretranslocatio
66  of the small subunit head domain within the elongation factor G (GDP)-bound ribosome complex.
67  domains could facilitate the association of elongation factor-G into lipid rafts in living bacteria,
68                              As a homolog of elongation factor G, it contains three domains (III-V) p
69 o observe aa-tRNA accommodation coupled with elongation factor G-mediated translocation.
70                     Mitochondria possess two elongation factor Gs: one with translocation activity (E
71                       We can position either elongation factor G or elongation factor Tu complexed wi
72                        The overproduction of elongation factor G or initiation factor 3 did not have
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
75                            In the absence of elongation factor G, the entire pretranslocation ribosom
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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