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1 eriments between the five captured wild-type leucyl-tRNAs and their synthetic counterparts, revealing
3 rom Methanobacterium thermoautotrophicum and leucyl tRNA derived from Halobacterium sp. NRC-1 as an o
4 sma KIC enrichment most accurately predicted leucyl-tRNA enrichment, whereas plasma Leu enrichment wa
5 f E. coli TruA in complex with two different leucyl tRNAs in conjunction with functional assays and c
7 lytic turnover, thus inhibiting synthesis of leucyl-tRNA(Leu) and consequentially blocking protein sy
9 use HSPE71, Rat RhoGAP protein, S cerevisiae leucyl tRNA synthetase and S cerevisiae chromosome II OR
10 carboxy-terminal domain (Cterm) of human mt-leucyl tRNA synthetase rescues the pathologic phenotype
11 roach exploits an engineered E. coli-derived leucyl tRNA synthetase-tRNA pair that incorporates a pho
14 re we report the surprising observation that leucyl-tRNA synthetase (LARS) becomes repressed during m
16 er the overexpression of human mitochondrial leucyl-tRNA synthetase (LARS2) in the cytoplasmic hybrid
19 c and editing activities of Escherichia coli leucyl-tRNA synthetase (LeuRS) demonstrate that the enzy
20 rmatics analyses, we identified two distinct leucyl-tRNA synthetase (LeuRS) genes within all genomes
31 this biocontrol agent targets A. tumefaciens leucyl-tRNA synthetase (LeuRS), an essential enzyme for
33 targeting an unprecedented Wolbachia enzyme, leucyl-tRNA synthetase (LeuRS), effectively inhibiting i
34 n-based compounds (benzoxaboroles) targeting leucyl-tRNA synthetase (LeuRS), including an antibiotic
37 a unique tRNA-dependent mechanism to inhibit leucyl-tRNA synthetase (LeuRS), while the TM84-producer
41 ulting from cancer-associated MTOR mutations.Leucyl-tRNA synthetase (LRS) is a leucine sensor of the
44 Binding of gold-labeled tRNA(Leu) places leucyl-tRNA synthetase and the bifunctional glutamyl-/pr
45 ein, different mutations in Escherichia coli leucyl-tRNA synthetase are combined to unmask the pretra
46 of onychomycosis, inhibits yeast cytoplasmic leucyl-tRNA synthetase by formation of a stable tRNA(Leu
47 he collective motion in Thermus thermophilus leucyl-tRNA synthetase by studying the low frequency nor
49 These mutations that altered or abolished leucyl-tRNA synthetase editing were introduced into comp
50 overcome this limitation, we have adapted a leucyl-tRNA synthetase from Methanobacterium thermoautot
51 n identified a mutation in the mitochondrial leucyl-tRNA synthetase gene (lrs-2) that impaired mitoch
55 rving cells of leucine or treating them with leucyl-tRNA synthetase inhibitors did not elicit nuclear
56 ted that the transfer of human mitochondrial leucyl-tRNA synthetase into the cybrid cells carrying th
58 cid editing active site for Escherichia coli leucyl-tRNA synthetase resides within the CP1 domain tha
59 tational analysis within yeast mitochondrial leucyl-tRNA synthetase showed that the enzyme has mainta
60 ed conformational changes of T. thermophilus leucyl-tRNA synthetase upon substrate binding and analyz
61 red the refolding of the human mitochondrial leucyl-tRNA synthetase variant H324Q to that of wild typ
62 hreonine-rich region of the Escherichia coli leucyl-tRNA synthetase's CP1 domain that is hypothesized
64 be aminoacylated by the human mitochondrial leucyl-tRNA synthetase, we examined the aminoacylation k
70 d mutations in LARS2, encoding mitochondrial leucyl-tRNA synthetase: homozygous c.1565C>A (p.Thr522As
71 y a constitutive protein complex composed of leucyl-tRNA-synthetase and folliculin, which regulates m
73 cluding a complex between prolyl-(ProRS) and leucyl-tRNA synthetases (LeuRS) in Methanothermobacter t
82 pared the ability of wild-type and synthetic leucyl-tRNA to break the degeneracy of the leucine codon