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1 from the active site of human mitochondrial phenylalanyl-tRNA synthetase.
2 lanyl-tRNA is formed by Thermus thermophilus phenylalanyl-tRNA synthetase.
3 lyclonal antibodies raised against mammalian phenylalanyl-tRNA synthetase.
4 ines that inhibit a new antimalarial target, phenylalanyl-tRNA synthetase.
5 erminal module that resembles the OB-fold of phenylalanyl-tRNA synthetases.
6 nthesized in nature (by Thermus thermophilus phenylalanyl-tRNA synthetase), and many disubstituted tR
7 we have engineered a Caenorhabditis elegans phenylalanyl-tRNA synthetase capable of tagging proteins
8 e we report that wild-type E. coli EF-Tu and phenylalanyl-tRNA synthetase collaborate with these muta
9 c azetidines targeting Plasmodium falciparum phenylalanyl-tRNA synthetase comprise one promising new
12 ficity in AcKRS and in a PylRS variant [iodo-phenylalanyl-tRNA synthetase (IFRS)] that displays both
13 -acetyllysyl-tRNA synthetase [AcKRS], 3-iodo-phenylalanyl-tRNA synthetase [IFRS], a broad specific Py
14 crimination in vivo revealed that editing by phenylalanyl-tRNA synthetase is essential for faithful t
18 ares 45% identity with the yeast cytoplasmic phenylalanyl tRNA synthetase (PheRS) regulatory alpha-su
19 the amino acid binding and recognition step, phenylalanyl-tRNA synthetase (PheRS) faces the challenge
23 olutionary divergence of tyrosine editing by phenylalanyl-tRNA synthetase (PheRS) was used as a model
24 n its acceptor stem that prevents editing by phenylalanyl-tRNA synthetase (PheRS), leading to the acc
28 a proofreading ("editing") activity, such as phenylalanyl-tRNA synthetases (PheRS) that hydrolyze mis
29 tivity of aminoacyl-tRNA synthetases such as phenylalanyl-tRNA synthetases (PheRS), which edit misact
33 n of the nucleus-encoded human mitochondrial phenylalanyl-tRNA synthetase, which aminoacylates hmt-tR
35 or tRNA (ytRNA(Phe)(CUA)) and a mutant yeast phenylalanyl-tRNA synthetase (yPheRS (T415G)) into an Es
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