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1 ein A) and LysN (anticodon binding domain of lysyl tRNA synthetase).
2 base pair reduces mischarging by the E. coli lysyl-tRNA synthetase.
3 he synthesis of asparaginyl-tRNA and a novel lysyl-tRNA synthetase.
4 n shown to contain an unrelated class I-type lysyl-tRNA synthetase.
5 rgdorferi contains a functional class I-type lysyl-tRNA synthetase.
6 (Trp)(CCA) to be aminoacylated by A.thaliana lysyl-tRNA synthetase.
7 n the mammalian cells by S207-phosphorylated Lysyl-tRNA synthetase.
8 RS1 and LysRS2, the two different M. barkeri lysyl-tRNA synthetases.
9 h lysine but is not closely related to known lysyl-tRNA synthetases.
10 bases indicated high homology to a family of lysyl-tRNA synthetases.
11 he amino acid level to archaeal class I-type lysyl-tRNA synthetases.
19 69 base pair to G4:C69 and overproduction of lysyl-tRNA synthetase and methionyl-tRNA transformylase
20 jeK, encoding truncated homologs of class II lysyl-tRNA synthetase and of lysine-2,3-aminomutase, res
21 r results on recognition of tRNAs by E. coli lysyl-tRNA synthetase and on competition in cells among
23 stem eliminated misacylation by the E. coli lysyl tRNA synthetase, and led to the development of a f
24 molar inhibitor of the Plasmodium falciparum lysyl-tRNA synthetase, and exhibits activity against bot
29 ination factor Rho, bacterial and eukaryotic lysyl-tRNA synthetases, bacteriophage T4 endonuclease VI
31 , our analysis points to the extant forms of lysyl-tRNA synthetase being preceded in evolution by the
33 lso encode G73, the motif 2 loop sequence of lysyl-tRNA synthetase differs at multiple positions from
34 r, the capacity of tRNA3Lys to interact with lysyl-tRNA synthetase does not entirely explain the enha
36 lysis of B. burgdorferi mRNA showed that the lysyl-tRNA synthetase-encoding gene is highly expressed,
40 gene lies immediately adjacent to the cKARS (lysyl-tRNA synthetase) gene with the two genes in a head
44 hydrolyze lysyl-adenylate generated by human lysyl-tRNA synthetase (hLysRS) by proceeding through an
49 udies have demonstrated that the presence of lysyl-tRNA synthetase in HIV-1 virions might account for
50 this knowledge gap, a diverse set of potent lysyl-tRNA synthetase inhibitors was profiled to identif
53 ases, we report here that the class II human lysyl-tRNA synthetase is relatively insensitive to the n
54 is, p.Tyr173SerfsX7, and p.Ile302Met) in the lysyl-tRNA synthetase (KARS) gene in two patients from t
57 e identified at highly conserved residues of lysyl-tRNA synthetase (KARS): the c.1129G>A (p.Asp377Asn
59 an methionyl-tRNA synthetase (MRS) and human lysyl-tRNA synthetase (KRS) were expressed in human-deri
60 d a trans pQTL relationship between the KARS lysyl-tRNA synthetase locus and levels of the DIDO1 prot
63 s has been developed against M. tuberculosis lysyl-tRNA synthetase (LysRS) and cellular studies suppo
64 nscription primer via an interaction between lysyl-tRNA synthetase (LysRS) and the HIV-1 Gag polyprot
65 f the transcription factors MITF or USF2 and lysyl-tRNA synthetase (LysRS) are associated with human
66 into two unrelated structural classes, with lysyl-tRNA synthetase (LysRS) being the only enzyme repr
67 previously shown that the essential protein lysyl-tRNA synthetase (LysRS) exists in two unrelated fo
69 unrelated aminoacyl-tRNA synthetase classes, lysyl-tRNA synthetase (LysRS) is the only example known
73 s a mutation in the KARS gene, which encodes lysyl-tRNA synthetase (LysRS), a moonlight protein with
74 s a mutation in the KARS gene, which encodes lysyl-tRNA synthetase (LysRS), a moonlight protein with
75 Gag and GagPol, as well as host cell factor lysyl-tRNA synthetase (LysRS), are required for specific
78 tion in the C. capitata lysine--tRNA ligase (Lysyl-tRNA synthetase, LysRS) gene responsible for the t
81 The crystal structure of the constitutive lysyl-tRNA synthetase (LysS) from Escherichia coli has b
82 Crystals of the thermo-inducible E. coli lysyl-tRNA synthetase LysU which diffract to 2.1 A resol
87 the sequence of the loop of motif 2 of human lysyl-tRNA synthetase specifies a structural variation t
88 RNA, we discovered that the Escherichia coli lysyl tRNA synthetase was responsible for misacylating t
89 syl-AMP generated by either E. coli or human lysyl-tRNA synthetase were partially transferable by C-t
91 ural classes, the only known exception being lysyl-tRNA synthetase which exists in both classes I (Ly