戻る
「早戻しボタン」を押すと検索画面に戻ります。 [閉じる]

コーパス検索結果 (1語後でソート)

通し番号をクリックするとPubMedの該当ページを表示します
1 ion from fars-3, an essential subunit of the phenylalanyl tRNA synthetase.
2  from the active site of human mitochondrial phenylalanyl-tRNA synthetase.
3 lanyl-tRNA is formed by Thermus thermophilus phenylalanyl-tRNA synthetase.
4 lyclonal antibodies raised against mammalian phenylalanyl-tRNA synthetase.
5 ines that inhibit a new antimalarial target, phenylalanyl-tRNA synthetase.
6 erminal module that resembles the OB-fold of phenylalanyl-tRNA synthetases.
7 nthesized in nature (by Thermus thermophilus phenylalanyl-tRNA synthetase), and many disubstituted tR
8  and the aminoacyl-tRNA hydrolytic domain of phenylalanyl-tRNA synthetase are functionally and evolut
9  we have engineered a Caenorhabditis elegans phenylalanyl-tRNA synthetase capable of tagging proteins
10 e we report that wild-type E. coli EF-Tu and phenylalanyl-tRNA synthetase collaborate with these muta
11 c azetidines targeting Plasmodium falciparum phenylalanyl-tRNA synthetase comprise one promising new
12                                          The phenylalanyl-tRNA synthetase editing mechanism is also a
13                 Inhibition of purified yeast phenylalanyl-tRNA synthetase (FRS) catalyzed aminoacylat
14 ug resistance was engineered using a mutated phenylalanyl tRNA synthetase gene and marking strains wi
15 ficity in AcKRS and in a PylRS variant [iodo-phenylalanyl-tRNA synthetase (IFRS)] that displays both
16 -acetyllysyl-tRNA synthetase [AcKRS], 3-iodo-phenylalanyl-tRNA synthetase [IFRS], a broad specific Py
17 crimination in vivo revealed that editing by phenylalanyl-tRNA synthetase is essential for faithful t
18                                 We show that phenylalanyl-tRNA synthetase misactivates tyrosine and t
19                          Human mitochondrial phenylalanyl-tRNA synthetase (mtPheRS) has been identifi
20  computationally designed mutant form of the phenylalanyl-tRNA synthetase of the host.
21 ares 45% identity with the yeast cytoplasmic phenylalanyl tRNA synthetase (PheRS) regulatory alpha-su
22 the amino acid binding and recognition step, phenylalanyl-tRNA synthetase (PheRS) faces the challenge
23                                              Phenylalanyl-tRNA synthetase (PheRS) is a multidomain (a
24                                              Phenylalanyl-tRNA synthetase (PheRS) maintains specifici
25                                              Phenylalanyl-tRNA synthetase (PheRS) preferentially liga
26                                  For example phenylalanyl-tRNA synthetase (PheRS) proofreads the non-
27 olutionary divergence of tyrosine editing by phenylalanyl-tRNA synthetase (PheRS) was used as a model
28 n its acceptor stem that prevents editing by phenylalanyl-tRNA synthetase (PheRS), leading to the acc
29  translation by the proofreading activity of phenylalanyl-tRNA synthetase (PheRS).
30  that of the heterotetrameric (alphabeta)(2) phenylalanyl-tRNA synthetase (PheRS).
31 ies of binding of phenylalanine analogues to phenylalanyl-tRNA synthetase (PheRS).
32 molog of one subunit of prokaryote and yeast phenylalanyl-tRNA synthetase (PheRS).
33 ynthetase (PylRS) is structurally related to phenylalanyl-tRNA synthetase (PheRS).
34 a proofreading ("editing") activity, such as phenylalanyl-tRNA synthetases (PheRS) that hydrolyze mis
35 tivity of aminoacyl-tRNA synthetases such as phenylalanyl-tRNA synthetases (PheRS), which edit misact
36                      In addition, seryl- and phenylalanyl-tRNA synthetases that are only marginally r
37                                          The phenylalanyl-tRNA synthetase variants S57C and N280S bot
38          To define the mechanism of editing, phenylalanyl-tRNA synthetase was used to investigate dif
39 n of the nucleus-encoded human mitochondrial phenylalanyl-tRNA synthetase, which aminoacylates hmt-tR
40                             A designed yeast phenylalanyl-tRNA synthetase (yPheRS (T415G)) activates
41 or tRNA (ytRNA(Phe)(CUA)) and a mutant yeast phenylalanyl-tRNA synthetase (yPheRS (T415G)) into an Es