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1 crimination were functionally independent in valyl-tRNA synthetase.
2 case of inner mitochondrial membrane 50, and valyl-tRNA synthetase.
3 in all known LeuRSs and also isoleucyl- and valyl-tRNA synthetases.
4 mportant for proper recognition of tRNAValby valyl-tRNA synthetase.19F NMR also shows that formation
6 tic analyses of beta-tubulin, chaperonin 60, valyl-tRNA synthetase, and EF-1alpha, suggests a sister-
8 NMR also shows that formation of the tRNAVal-valyl-tRNA synthetase complex does not disrupt the first
10 the homologous isoleucyl-tRNA synthetase and valyl-tRNA synthetase editing active sites, play a centr
12 the evolutionary-related IleRS, leucyl- and valyl-tRNA synthetases (I/L/VRSs), all efficiently hydro
13 tive peptide 1; CP1 domain), LeuRS resembles valyl-tRNA synthetase in its reliance on post-transfer e
17 es, are abolished in a temperature-sensitive valyl-tRNA synthetase mutant (un-3(ts)) that has high le
19 hing the identity of the human mitochondrial valyl-tRNA synthetase then inducing its overexpression i
20 or analyses of isoleucyl-tRNA synthetase and valyl-tRNA synthetase, these experiments provide the bas
21 ransient overexpression of editing-defective valyl-tRNA synthetase (ValRS(ED)) activated DNA break-re
22 actions between Escherichia coli tRNAVal and valyl-tRNA synthetase (ValRS) by enzymatic footprinting
23 mologs isoleucyl-tRNA synthetase (IleRS) and valyl-tRNA synthetase (ValRS) deacylate Val-tRNA(Ile) an
26 uRS), isoleucyl-tRNA synthetase (IleRS), and valyl-tRNA synthetase (ValRS) have evolved a discrete ed
27 uRS), isoleucyl-tRNA synthetase (IleRS), and valyl-tRNA synthetase (ValRS) share a common insertion,
28 n Escherichia coli tRNAValfor recognition by valyl-tRNA synthetase (ValRS), nucleotides in the accept
32 wo previously reported biallelic variants in valyl-tRNA synthetase (VARS) in ten patients with a deve