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1 e mechanochemical motions in T. thermophilus leucyl-tRNA synthetase.
2 nate amino acids that can be misactivated by leucyl-tRNA synthetase.
3 he ser-tRNACAG and preventing binding of the leucyl-tRNA synthetase.
4 editing of mischarged tRNA similar to other leucyl-tRNA synthetases.
5 out mischarging by glycyl-, glutaminyl-, and leucyl-tRNA synthetases.
6 use HSPE71, Rat RhoGAP protein, S cerevisiae leucyl tRNA synthetase and S cerevisiae chromosome II OR
8 y a constitutive protein complex composed of leucyl-tRNA-synthetase and folliculin, which regulates m
9 ein, different mutations in Escherichia coli leucyl-tRNA synthetase are combined to unmask the pretra
10 of onychomycosis, inhibits yeast cytoplasmic leucyl-tRNA synthetase by formation of a stable tRNA(Leu
11 he collective motion in Thermus thermophilus leucyl-tRNA synthetase by studying the low frequency nor
14 These mutations that altered or abolished leucyl-tRNA synthetase editing were introduced into comp
15 overcome this limitation, we have adapted a leucyl-tRNA synthetase from Methanobacterium thermoautot
16 n identified a mutation in the mitochondrial leucyl-tRNA synthetase gene (lrs-2) that impaired mitoch
18 d mutations in LARS2, encoding mitochondrial leucyl-tRNA synthetase: homozygous c.1565C>A (p.Thr522As
23 rving cells of leucine or treating them with leucyl-tRNA synthetase inhibitors did not elicit nuclear
24 ted that the transfer of human mitochondrial leucyl-tRNA synthetase into the cybrid cells carrying th
25 er the overexpression of human mitochondrial leucyl-tRNA synthetase (LARS2) in the cytoplasmic hybrid
28 c and editing activities of Escherichia coli leucyl-tRNA synthetase (LeuRS) demonstrate that the enzy
38 this biocontrol agent targets A. tumefaciens leucyl-tRNA synthetase (LeuRS), an essential enzyme for
42 a unique tRNA-dependent mechanism to inhibit leucyl-tRNA synthetase (LeuRS), while the TM84-producer
47 cluding a complex between prolyl-(ProRS) and leucyl-tRNA synthetases (LeuRS) in Methanothermobacter t
52 ulting from cancer-associated MTOR mutations.Leucyl-tRNA synthetase (LRS) is a leucine sensor of the
54 carboxy-terminal domain (Cterm) of human mt-leucyl tRNA synthetase rescues the pathologic phenotype
55 cid editing active site for Escherichia coli leucyl-tRNA synthetase resides within the CP1 domain tha
56 hreonine-rich region of the Escherichia coli leucyl-tRNA synthetase's CP1 domain that is hypothesized
57 tational analysis within yeast mitochondrial leucyl-tRNA synthetase showed that the enzyme has mainta
59 ed conformational changes of T. thermophilus leucyl-tRNA synthetase upon substrate binding and analyz
60 red the refolding of the human mitochondrial leucyl-tRNA synthetase variant H324Q to that of wild typ
61 be aminoacylated by the human mitochondrial leucyl-tRNA synthetase, we examined the aminoacylation k
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