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1 It was identified to be plastid ribosome recycling factor.
2 the ribosomal A site that contacts tRNA and ribosome recycling factor.
3 n these models, at least in part through the ribosome recycling factor ABCE1, ribosome-associated qua
4 actors known to induce drop-off reveals that ribosome recycling factor accounts for a small fraction
5 ond, a fully rotated state, is stabilized by ribosome recycling factor and binds tRNA in a highly ben
6 n eubacteria, recycling is catalyzed by RRF (ribosome recycling factor) and EF-G (elongation factor G
7 coiled-coil domains of the STAT protein, the ribosome-recycling factor, and structural proteins like
8 translation factors, elongation factor G and ribosome recycling factor, are known to be required for
9 cross the improvement process, including the ribosome recycling factor (BnRRF) gene for seed weight.
11 limited by mRNA cleavage, and that RF-3 and ribosome recycling factor do not constitute a tmRNA-inde
12 nd a mass of density corresponding to chloro-ribosome recycling factor; domain II of this factor appe
13 scent chain complexes are dissociated by the ribosome recycling factors Hbs1/Pelota/ABCE1 to a unique
14 3 in 50 S subunit and 25 in 30 S subunit and ribosome recycling factor in 70 S), of which 53 are E. c
19 treating cells with kasugamycin, decreasing ribosome recycling factor (RRF) activity or increasing i
20 to its 30S and 50S subunits by the action of ribosome recycling factor (RRF) and elongation factor G
21 ination ribosomal complex is disassembled by ribosome recycling factor (RRF) and elongation factor G.
23 acking a tnaC plasmid, the overproduction of ribosome recycling factor (RRF) and release factor 3 (RF
27 iling to characterize the biological role of ribosome recycling factor (RRF) in Escherichia coli.
31 lent mutations of frr (the gene encoding for ribosome recycling factor (RRF)) of Escherichia coli are
35 the ribosome by the concerted action of the ribosome-recycling factor (RRF) and elongation factor G
37 ence that two essential translation factors, ribosome-recycling factor (RRF) and GTPase elongation fa
38 is processed by the concerted action of the ribosome-recycling factor (RRF), elongation factor G (EF