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1 tes diacetyl-[14C]lysyl-tRNA and acetyl-[14C]phenylalanyl-tRNA.
3 ize aminoacyl-tRNA recognition by the leucyl/phenylalanyl-tRNA-protein transferase (L/Ftransferase).
4 ares 45% identity with the yeast cytoplasmic phenylalanyl tRNA synthetase (PheRS) regulatory alpha-su
5 ug resistance was engineered using a mutated phenylalanyl tRNA synthetase gene and marking strains wi
8 ficity in AcKRS and in a PylRS variant [iodo-phenylalanyl-tRNA synthetase (IFRS)] that displays both
10 the amino acid binding and recognition step, phenylalanyl-tRNA synthetase (PheRS) faces the challenge
15 olutionary divergence of tyrosine editing by phenylalanyl-tRNA synthetase (PheRS) was used as a model
16 n its acceptor stem that prevents editing by phenylalanyl-tRNA synthetase (PheRS), leading to the acc
23 or tRNA (ytRNA(Phe)(CUA)) and a mutant yeast phenylalanyl-tRNA synthetase (yPheRS (T415G)) into an Es
24 -acetyllysyl-tRNA synthetase [AcKRS], 3-iodo-phenylalanyl-tRNA synthetase [IFRS], a broad specific Py
25 and the aminoacyl-tRNA hydrolytic domain of phenylalanyl-tRNA synthetase are functionally and evolut
26 we have engineered a Caenorhabditis elegans phenylalanyl-tRNA synthetase capable of tagging proteins
27 e we report that wild-type E. coli EF-Tu and phenylalanyl-tRNA synthetase collaborate with these muta
28 c azetidines targeting Plasmodium falciparum phenylalanyl-tRNA synthetase comprise one promising new
30 crimination in vivo revealed that editing by phenylalanyl-tRNA synthetase is essential for faithful t
35 nthesized in nature (by Thermus thermophilus phenylalanyl-tRNA synthetase), and many disubstituted tR
36 n of the nucleus-encoded human mitochondrial phenylalanyl-tRNA synthetase, which aminoacylates hmt-tR
41 a proofreading ("editing") activity, such as phenylalanyl-tRNA synthetases (PheRS) that hydrolyze mis
42 tivity of aminoacyl-tRNA synthetases such as phenylalanyl-tRNA synthetases (PheRS), which edit misact