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 protein S4, RNA pseudouridine synthase, and tyrosyl-tRNA synthetase.
2 DI-CMTC is not due to a catalytic defect in tyrosyl-tRNA synthetase.
3 which ATP binds to the functional subunit in tyrosyl-tRNA synthetase.
4 nitor the pre-steady state kinetics of human tyrosyl-tRNA synthetase.
5 ion step is potassium-dependent in the human tyrosyl-tRNA synthetase.
6 or tyrosine activation 260-fold in the human tyrosyl-tRNA synthetase.
7 Its genome encodes a single copy of tyrosyl-tRNA synthetase.
8 substrate in the Bacillus stearothermophilus tyrosyl-tRNA synthetase.
9 ts the non-canonical function of L. donovani tyrosyl-tRNA synthetase.
10 role in the initial binding of tRNA(Tyr) to tyrosyl-tRNA synthetase.
11 ocaldococcus jannaschii and Escherichia coli tyrosyl-tRNA synthetases.
12 ptations compared with nonsplicing bacterial tyrosyl-tRNA synthetases.
13 Notably, a variant within the mitochondrial tyrosyl-tRNA synthetase 2 (YARS2) gene exhibited a signi
15 alleles of the nuclear-encoded mitochondrial tyrosyl-tRNA synthetase (Aatm) and the mitochondrial-enc
17 ssed in Escherichia coli indicate that human tyrosyl-tRNA synthetase aminoacylates human but not B. s
18 rmore, we find that downregulation of yars-2/tyrosyl-tRNA synthetase, an NMD target transcript, by da
19 etic code, only the Methanococcus jannaschii tyrosyl tRNA synthetase and tRNA have been used extensiv
20 for both d-tyrosine activation by wild-type tyrosyl-tRNA synthetase and activation of l-tyrosine by
21 he tyrosine activation reaction in the human tyrosyl-tRNA synthetase and whether it can be replaced b
22 -terminal domain that is unique to the human tyrosyl-tRNA synthetase and whose primary structure is 4
25 synthetase and a deaminase domain, bacterial tyrosyl-tRNA synthetases, and a number of uncharacterize
27 in the Bacillus stearothermophilus and human tyrosyl-tRNA synthetases are largely conserved, several
33 ations in glycyl-tRNA synthetase (GlyRS) and tyrosyl-tRNA synthetase cause Charcot-Marie-Tooth (CMT)
34 sequenced several clones identified as human tyrosyl-tRNA synthetase cDNAs by the Human Genome Projec
35 ivation of tyrosine in B. stearothermophilus tyrosyl-tRNA synthetase (Cys-35, His-48, and Lys-233) ar
36 bifunctional Neurospora crassa mitochondrial tyrosyl-tRNA synthetase (CYT-18 protein) both aminoacyla
38 The Neurospora crassa mitochondrial (mt) tyrosyl-tRNA synthetase (CYT-18 protein) functions in sp
43 ly truncated Neurospora crassa mitochondrial tyrosyl-tRNA synthetase (CYT-18 protein) that functions
44 ility of the Neurospora crassa mitochondrial tyrosyl-tRNA synthetase (CYT-18 protein) to suppress mut
46 ed sigmoidal behavior presents a paradox, as tyrosyl-tRNA synthetase displays an extreme form of nega
47 K233A variant of Bacillus stearothermophilus tyrosyl-tRNA synthetase displays sigmoidal kinetics simi
48 , was used as a model to explore how a human tyrosyl-tRNA synthetase during evolution acquired novel
49 this technology by introducing an engineered tyrosyl-tRNA synthetase (EcTyrRS) and a tryptophanyl-tRN
50 Arc1p, the carboxyl-terminal domain of human tyrosyl-tRNA synthetase evolved from gene duplication of
52 Furthermore, as is the case for l-tyrosine, tyrosyl-tRNA synthetase exhibits "half-of-the-sites" rea
53 recombinant human and B. stearothermophilus tyrosyl-tRNA synthetases expressed in Escherichia coli i
54 synthetase are 52, 36, and 16% identical to tyrosyl-tRNA synthetases from S. cerevisiae, Methanococc
55 ora crassa CYT-18 protein, the mitochondrial tyrosyl-tRNA synthetase, functions in splicing group I i
58 h position of the 'KMSKS' signature motif in tyrosyl-tRNA synthetase have been analyzed to test the h
59 sine suggests that their side chains bind to tyrosyl-tRNA synthetase in similar orientations and that
60 e van't Hoff plots for the binding of ATP to tyrosyl-tRNA synthetase in the absence and presence of s
61 Catalysis of tRNA(Tyr) aminoacylation by tyrosyl-tRNA synthetase involves two steps: activation o
64 The Bacillus subtilis tyrS gene, encoding tyrosyl-tRNA synthetase, is a member of the T-box family
65 tant for the initial binding of tRNA(Tyr) to tyrosyl-tRNA synthetase, it does not play a catalytic ro
66 y explores the twin attributes of Leishmania tyrosyl-tRNA synthetase (LdTyrRS) namely, aminoacylation
69 and two amino acids that are present only in tyrosyl-tRNA synthetases, Lys82 and Arg86, stabilize the
71 the archaebacterial Methanococcus jannaschii tyrosyl-tRNA synthetase may give insights into the histo
72 ne encoding the desired mutant M. jannaschii tyrosyl-tRNA synthetase (MjTyrRS) is expressed under con
73 is encoded by human YARS2 for mitochondrial tyrosyl-tRNA synthetase (mt-TyrRS), which aminoacylates
77 dy, and in vivo functional verification of a tyrosyl-tRNA synthetase mutant for the genetic encoding
78 noacyl-tRNA synthetase pair derived from the tyrosyl-tRNA synthetase of Methanococcus jannaschii can
79 of tyrosyl adenylate by the dimeric class I tyrosyl-tRNA synthetase, operates as well in this homote
80 bacterial homologues, a number of eukaryotic tyrosyl-tRNA synthetases require potassium to catalyze t
81 dy-state kinetic analyses of CHO cytoplasmic tyrosyl-tRNA synthetase revealed a 25-fold lower specifi
82 ional comparisons of mammalian and bacterial tyrosyl-tRNA synthetase revealed key differences at resi
83 re motif is absent from all known eukaryotic tyrosyl-tRNA synthetase sequences, except those of highe
84 hypothesis that the KMSSS sequence in human tyrosyl-tRNA synthetase stabilizes the transition state
85 sine activation step is higher for the human tyrosyl-tRNA synthetase than for the B. stearothermophil
86 is appears to be significantly less in human tyrosyl-tRNA synthetase than it is in the B. stearotherm
87 ora crassa CYT-18 protein is a mitochondrial tyrosyl-tRNA synthetase that also promotes self-splicing
88 the active sites of the bacterial and human tyrosyl-tRNA synthetases that could be exploited to desi
90 and "KMSKS." In Bacillus stearothermophilus tyrosyl-tRNA synthetase, the KMSKS motif (230KFGKT234) h
92 P design algorithm we then designed a mutant tyrosyl tRNA synthetase to activate O-methyl-l-tyrosine
93 DI-CMTC is due to a defect in the ability of tyrosyl-tRNA synthetase to catalyze the aminoacylation o
94 ineer an orthogonal Methanococcus jannaschii tyrosyl-tRNA synthetase/tRNA pair for encoding thioxanth
95 zed 1 and evolved a Methanococcus jannaschii tyrosyl-tRNA synthetase/tRNA(CUA) pair to genetically en
96 In this manner, a natural fragment of human tyrosyl tRNA synthetase (TyrRS), mini-TyrRS, has been sh
98 , for use in yeast, and mutants of the yeast tyrosyl-tRNA synthetase (TyrRS) along with an amber supp
99 Biological fragments of two human enzymes, tyrosyl-tRNA synthetase (TyrRS) and tryptophanyl-tRNA sy
102 nation of methods, here we showed that human tyrosyl-tRNA synthetase (TyrRS) distributes to the nucle
105 Here we show that a nuclear function of tyrosyl-tRNA synthetase (TyrRS) is implicated in a Droso
108 Structures in isolation and those bound to tyrosyl-tRNA synthetase (TyrRS) show that this ~55-kilod
109 in catalysis by Bacillus stearothermophilus tyrosyl-tRNA synthetase (TyrRS), the temperature depende
111 ecent work demonstrated that RSV facilitates tyrosyl-tRNA synthetase (TyrRS)-dependent activation of
112 We previously showed that tyrosine inhibits tyrosyl-tRNA synthetase (TyrRS)-mediated activation of p
115 protein, the Neurospora crassa mitochondrial tyrosyl-tRNA synthetase (TyrRS; CYT-18), is bifunctional
116 netic reconstruction, two types of bacterial tyrosyl-tRNA synthetases (TyrRS) form distinct clades wi
117 ing domains of the tryptophanyl (TrpRS)- and tyrosyl-tRNA synthetases (TyrRS) of Bacillus stearotherm
118 a-helix (H0), which is absent from bacterial tyrosyl-tRNA synthetases (TyrRSs), and a downstream regi
120 ytokine function of the 528-amino acid human tyrosyl-tRNA synthetase was associated with pinpointed u
121 charging of tRNA(Tyr) with noncognate Phe by tyrosyl-tRNA synthetase was responsible for mistranslati
122 ability of an amino acid binding pocket of a tyrosyl-tRNA synthetase, we identified three new variant
123 ognition differs between bacterial and human tyrosyl-tRNA synthetases, we sequenced several clones id
124 ly>Val) in YARS2 gene encoding mitochondrial tyrosyl-tRNA synthetase, which interacts with m.11778G>A
126 tal structure of an active fragment of human tyrosyl-tRNA synthetase with its cognate amino acid anal
128 f genomic sequences shows that mitochondrial tyrosyl-tRNA synthetases with structural adaptations sim
129 children homozygous for a novel mutation in tyrosyl-tRNA synthetase (YARS, c.499C > A, p.Pro167Thr)
130 Previous cellular studies have demonstrated tyrosyl-tRNA synthetase (YARS1 or TyrRS) as a stress res
132 reviously reported that an activated form of tyrosyl-tRNA synthetase (YRS(ACT)) has an extratranslati