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1 tes diacetyl-[14C]lysyl-tRNA and acetyl-[14C]phenylalanyl-tRNA.
2                                   The leucyl/phenylalanyl-tRNA-protein transferase (L/F-transferase)
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
6 ion from fars-3, an essential subunit of the phenylalanyl tRNA synthetase.
7                 Inhibition of purified yeast phenylalanyl-tRNA synthetase (FRS) catalyzed aminoacylat
8 ficity in AcKRS and in a PylRS variant [iodo-phenylalanyl-tRNA synthetase (IFRS)] that displays both
9                          Human mitochondrial phenylalanyl-tRNA synthetase (mtPheRS) has been identifi
10 the amino acid binding and recognition step, phenylalanyl-tRNA synthetase (PheRS) faces the challenge
11                                              Phenylalanyl-tRNA synthetase (PheRS) is a multidomain (a
12                                              Phenylalanyl-tRNA synthetase (PheRS) maintains specifici
13                                              Phenylalanyl-tRNA synthetase (PheRS) preferentially liga
14                                  For example phenylalanyl-tRNA synthetase (PheRS) proofreads the non-
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
17  translation by the proofreading activity of phenylalanyl-tRNA synthetase (PheRS).
18  that of the heterotetrameric (alphabeta)(2) phenylalanyl-tRNA synthetase (PheRS).
19 ies of binding of phenylalanine analogues to phenylalanyl-tRNA synthetase (PheRS).
20 molog of one subunit of prokaryote and yeast phenylalanyl-tRNA synthetase (PheRS).
21 ynthetase (PylRS) is structurally related to phenylalanyl-tRNA synthetase (PheRS).
22                             A designed yeast phenylalanyl-tRNA synthetase (yPheRS (T415G)) activates
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
29                                          The phenylalanyl-tRNA synthetase editing mechanism is also a
30 crimination in vivo revealed that editing by phenylalanyl-tRNA synthetase is essential for faithful t
31                                 We show that phenylalanyl-tRNA synthetase misactivates tyrosine and t
32  computationally designed mutant form of the phenylalanyl-tRNA synthetase of the host.
33                                          The phenylalanyl-tRNA synthetase variants S57C and N280S bot
34          To define the mechanism of editing, phenylalanyl-tRNA synthetase was used to investigate dif
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
37  from the active site of human mitochondrial phenylalanyl-tRNA synthetase.
38 lanyl-tRNA is formed by Thermus thermophilus phenylalanyl-tRNA synthetase.
39 lyclonal antibodies raised against mammalian phenylalanyl-tRNA synthetase.
40 ines that inhibit a new antimalarial target, phenylalanyl-tRNA synthetase.
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
43                      In addition, seryl- and phenylalanyl-tRNA synthetases that are only marginally r
44 erminal module that resembles the OB-fold of phenylalanyl-tRNA synthetases.