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1 ransient overexpression of editing-defective valyl-tRNA synthetase (ValRS(ED)) activated DNA break-re
2 actions between Escherichia coli tRNAVal and valyl-tRNA synthetase (ValRS) by enzymatic footprinting
3 mologs isoleucyl-tRNA synthetase (IleRS) and valyl-tRNA synthetase (ValRS) deacylate Val-tRNA(Ile) an
6 uRS), isoleucyl-tRNA synthetase (IleRS), and valyl-tRNA synthetase (ValRS) have evolved a discrete ed
7 uRS), isoleucyl-tRNA synthetase (IleRS), and valyl-tRNA synthetase (ValRS) share a common insertion,
8 n Escherichia coli tRNAValfor recognition by valyl-tRNA synthetase (ValRS), nucleotides in the accept
10 wo previously reported biallelic variants in valyl-tRNA synthetase (VARS) in ten patients with a deve
12 NMR also shows that formation of the tRNAVal-valyl-tRNA synthetase complex does not disrupt the first
14 the homologous isoleucyl-tRNA synthetase and valyl-tRNA synthetase editing active sites, play a centr
16 tive peptide 1; CP1 domain), LeuRS resembles valyl-tRNA synthetase in its reliance on post-transfer e
20 es, are abolished in a temperature-sensitive valyl-tRNA synthetase mutant (un-3(ts)) that has high le
22 hing the identity of the human mitochondrial valyl-tRNA synthetase then inducing its overexpression i
24 tic analyses of beta-tubulin, chaperonin 60, valyl-tRNA synthetase, and EF-1alpha, suggests a sister-
25 or analyses of isoleucyl-tRNA synthetase and valyl-tRNA synthetase, these experiments provide the bas
28 mportant for proper recognition of tRNAValby valyl-tRNA synthetase.19F NMR also shows that formation
30 the evolutionary-related IleRS, leucyl- and valyl-tRNA synthetases (I/L/VRSs), all efficiently hydro