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1 ing of uncharged tRNA to a domain related to histidyl tRNA synthetase.
2 ation of mutants in the gene (hisS) encoding histidyl-tRNA synthetase.
3 f G(-1) to allows efficient histidylation by histidyl-tRNA synthetase.
4 four HisZ regulatory subunits that resemble histidyl-tRNA synthetases.
5 four HisZ regulatory subunits that resemble histidyl-tRNA synthetases.
7 catalytic domain and a domain homologous to histidyl-tRNA synthetase and by the ability of dGCN2 to
8 necessary for the proper functioning of the histidyl-tRNA synthetase, and suggests a novel mechanism
9 as a risk factor for the development of anti-histidyl tRNA synthetase antibodies, and HLA-DRB1*11:01
10 ystal structure of the Staphylococcus aureus histidyl-tRNA synthetase apoprotein has been determined
12 Gcn2p has a regulatory region homologous to histidyl tRNA synthetase enzymes that binds uncharged tR
13 to isolate secondary site revertants in the histidyl-tRNA synthetase from E. coli which restore hist
15 ozygosity for mutations in the mitochondrial histidyl tRNA synthetase HARS2 at two highly conserved a
16 ture of the closely related Escherichia coli histidyl-tRNA synthetase (HisRS) as a guide, two mutants
17 exhibits significant sequence identity with histidyl-tRNA synthetase (HisRS) but does not aminoacyla
18 ion binds to sequences in GCN2 homologous to histidyl-tRNA synthetase (HisRS) enzymes, leading to enh
21 hia coli, the aminoacylation of tRNA(His) by histidyl-tRNA synthetase (HisRS) is highly dependent upo
24 GCN2 contains a regulatory domain related to histidyl-tRNA synthetase (HisRS) postulated to bind mult
26 This is the major recognition element for histidyl-tRNA synthetase (HisRS) to permit acylation of
27 domains of the homodimeric Escherichia coli histidyl-tRNA synthetase (HisRS) were separately express
29 noacyl transfer in class II Escherichia coli histidyl-tRNA synthetase (HisRS), we devised a rapid que
30 CN2, requires binding of uncharged tRNA to a histidyl-tRNA synthetase (HisRS)-like domain in GCN2.
32 domains, including a pseudokinase domain, a histidyl-tRNA synthetase (HisRS)-related region, and a C
34 d that GCN2 sequences containing homology to histidyl-tRNA synthetases (HisRS) bind uncharged tRNA th
35 ministration of bacterially expressed murine histidyl-tRNA synthetase (HRS) triggers florid muscle in
37 Thg1p-depleted cells is uncharged, although histidyl tRNA synthetase is active and the 3' end of the
38 at the level of binding by Escherichia coli histidyl-tRNA synthetase is addressed by filter binding,
39 The Gcn2p regulatory domain homologous to histidyl-tRNA synthetases is proposed to bind to uncharg
41 has expanded; antibodies to the autoantigen histidyl-tRNA synthetase (Jo1) being the commonest and b
42 yeast, GCN2, contains a region homologous to histidyl-tRNA synthetases juxtaposed to the kinase catal
44 f mutations in HARS2, encoding mitochondrial histidyl-tRNA synthetase, mutations in CLPP expose dysfu
45 lls having a temperature-sensitive mutant of histidyl tRNA synthetase, p70(s6k) was suppressed by a t
48 ent chemical modification experiments in the histidyl-tRNA synthetase system, emphasizes that substra
49 d sequence of tRNA(His) and at many sites in histidyl-tRNA synthetase that might be expected to affec
50 , including, in some mice, autoantibodies to histidyl-tRNA synthetase, the most common specificity fo
51 and essential for recognition by the cognate histidyl-tRNA synthetase to allow efficient His-tRNA(His
52 c interaction between MA and HO3, a putative histidyl-tRNA synthetase, was demonstrated in this syste
53 site fragments of Escherichia coli Class II histidyl-tRNA synthetase were constructed, expressed as
54 catalytic core of the contemporary class II histidyl-tRNA synthetase whose members lack aminoacylati
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