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1 hat different mode of recognition of the two tyrosyl-tRNAs.
2 has a mutation in the gene (dtd) encoding D-tyrosyl-tRNA deacylase, an enzyme that prevents the misi
3 this is kinetic, based on relative rates of tyrosyl-tRNA formation and tyrosine degradation and expo
4 We also show that the RNAP III-transcribed tyrosyl tRNA gene, SUP4-o, is subject to position effect
5 derived from a Methanocaldococcus jannaschii tyrosyl-tRNA (MjtRNATyrCUA) are expressed under control
6 In this manner, a natural fragment of human tyrosyl tRNA synthetase (TyrRS), mini-TyrRS, has been sh
7 etic code, only the Methanococcus jannaschii tyrosyl tRNA synthetase and tRNA have been used extensiv
8 P design algorithm we then designed a mutant tyrosyl tRNA synthetase to activate O-methyl-l-tyrosine
10 alleles of the nuclear-encoded mitochondrial tyrosyl-tRNA synthetase (Aatm) and the mitochondrial-enc
11 ivation of tyrosine in B. stearothermophilus tyrosyl-tRNA synthetase (Cys-35, His-48, and Lys-233) ar
12 bifunctional Neurospora crassa mitochondrial tyrosyl-tRNA synthetase (CYT-18 protein) both aminoacyla
14 The Neurospora crassa mitochondrial (mt) tyrosyl-tRNA synthetase (CYT-18 protein) functions in sp
19 ly truncated Neurospora crassa mitochondrial tyrosyl-tRNA synthetase (CYT-18 protein) that functions
20 ility of the Neurospora crassa mitochondrial tyrosyl-tRNA synthetase (CYT-18 protein) to suppress mut
21 y explores the twin attributes of Leishmania tyrosyl-tRNA synthetase (LdTyrRS) namely, aminoacylation
23 ne encoding the desired mutant M. jannaschii tyrosyl-tRNA synthetase (MjTyrRS) is expressed under con
26 , for use in yeast, and mutants of the yeast tyrosyl-tRNA synthetase (TyrRS) along with an amber supp
27 Biological fragments of two human enzymes, tyrosyl-tRNA synthetase (TyrRS) and tryptophanyl-tRNA sy
30 nation of methods, here we showed that human tyrosyl-tRNA synthetase (TyrRS) distributes to the nucle
35 in catalysis by Bacillus stearothermophilus tyrosyl-tRNA synthetase (TyrRS), the temperature depende
39 protein, the Neurospora crassa mitochondrial tyrosyl-tRNA synthetase (TyrRS; CYT-18), is bifunctional
41 ssed in Escherichia coli indicate that human tyrosyl-tRNA synthetase aminoacylates human but not B. s
42 for both d-tyrosine activation by wild-type tyrosyl-tRNA synthetase and activation of l-tyrosine by
43 he tyrosine activation reaction in the human tyrosyl-tRNA synthetase and whether it can be replaced b
44 -terminal domain that is unique to the human tyrosyl-tRNA synthetase and whose primary structure is 4
50 ations in glycyl-tRNA synthetase (GlyRS) and tyrosyl-tRNA synthetase cause Charcot-Marie-Tooth (CMT)
51 sequenced several clones identified as human tyrosyl-tRNA synthetase cDNAs by the Human Genome Projec
53 ed sigmoidal behavior presents a paradox, as tyrosyl-tRNA synthetase displays an extreme form of nega
54 K233A variant of Bacillus stearothermophilus tyrosyl-tRNA synthetase displays sigmoidal kinetics simi
55 , was used as a model to explore how a human tyrosyl-tRNA synthetase during evolution acquired novel
56 Arc1p, the carboxyl-terminal domain of human tyrosyl-tRNA synthetase evolved from gene duplication of
58 Furthermore, as is the case for l-tyrosine, tyrosyl-tRNA synthetase exhibits "half-of-the-sites" rea
61 h position of the 'KMSKS' signature motif in tyrosyl-tRNA synthetase have been analyzed to test the h
62 sine suggests that their side chains bind to tyrosyl-tRNA synthetase in similar orientations and that
63 e van't Hoff plots for the binding of ATP to tyrosyl-tRNA synthetase in the absence and presence of s
64 Catalysis of tRNA(Tyr) aminoacylation by tyrosyl-tRNA synthetase involves two steps: activation o
68 the archaebacterial Methanococcus jannaschii tyrosyl-tRNA synthetase may give insights into the histo
69 noacyl-tRNA synthetase pair derived from the tyrosyl-tRNA synthetase of Methanococcus jannaschii can
70 dy-state kinetic analyses of CHO cytoplasmic tyrosyl-tRNA synthetase revealed a 25-fold lower specifi
71 ional comparisons of mammalian and bacterial tyrosyl-tRNA synthetase revealed key differences at resi
72 re motif is absent from all known eukaryotic tyrosyl-tRNA synthetase sequences, except those of highe
73 hypothesis that the KMSSS sequence in human tyrosyl-tRNA synthetase stabilizes the transition state
74 sine activation step is higher for the human tyrosyl-tRNA synthetase than for the B. stearothermophil
75 is appears to be significantly less in human tyrosyl-tRNA synthetase than it is in the B. stearotherm
76 ora crassa CYT-18 protein is a mitochondrial tyrosyl-tRNA synthetase that also promotes self-splicing
77 DI-CMTC is due to a defect in the ability of tyrosyl-tRNA synthetase to catalyze the aminoacylation o
78 ytokine function of the 528-amino acid human tyrosyl-tRNA synthetase was associated with pinpointed u
79 charging of tRNA(Tyr) with noncognate Phe by tyrosyl-tRNA synthetase was responsible for mistranslati
80 tal structure of an active fragment of human tyrosyl-tRNA synthetase with its cognate amino acid anal
81 rmore, we find that downregulation of yars-2/tyrosyl-tRNA synthetase, an NMD target transcript, by da
83 ora crassa CYT-18 protein, the mitochondrial tyrosyl-tRNA synthetase, functions in splicing group I i
84 The Bacillus subtilis tyrS gene, encoding tyrosyl-tRNA synthetase, is a member of the T-box family
85 tant for the initial binding of tRNA(Tyr) to tyrosyl-tRNA synthetase, it does not play a catalytic ro
86 of tyrosyl adenylate by the dimeric class I tyrosyl-tRNA synthetase, operates as well in this homote
88 and "KMSKS." In Bacillus stearothermophilus tyrosyl-tRNA synthetase, the KMSKS motif (230KFGKT234) h
90 ability of an amino acid binding pocket of a tyrosyl-tRNA synthetase, we identified three new variant
91 ly>Val) in YARS2 gene encoding mitochondrial tyrosyl-tRNA synthetase, which interacts with m.11778G>A
103 zed 1 and evolved a Methanococcus jannaschii tyrosyl-tRNA synthetase/tRNA(CUA) pair to genetically en
106 netic reconstruction, two types of bacterial tyrosyl-tRNA synthetases (TyrRS) form distinct clades wi
107 ing domains of the tryptophanyl (TrpRS)- and tyrosyl-tRNA synthetases (TyrRS) of Bacillus stearotherm
108 a-helix (H0), which is absent from bacterial tyrosyl-tRNA synthetases (TyrRSs), and a downstream regi
109 This insertion is shared with all other tyrosyl-tRNA synthetases and is needed for a critical mi
111 in the Bacillus stearothermophilus and human tyrosyl-tRNA synthetases are largely conserved, several
112 recombinant human and B. stearothermophilus tyrosyl-tRNA synthetases expressed in Escherichia coli i
113 synthetase are 52, 36, and 16% identical to tyrosyl-tRNA synthetases from S. cerevisiae, Methanococc
114 bacterial homologues, a number of eukaryotic tyrosyl-tRNA synthetases require potassium to catalyze t
115 the active sites of the bacterial and human tyrosyl-tRNA synthetases that could be exploited to desi
117 f genomic sequences shows that mitochondrial tyrosyl-tRNA synthetases with structural adaptations sim
118 synthetase and a deaminase domain, bacterial tyrosyl-tRNA synthetases, and a number of uncharacterize
120 and two amino acids that are present only in tyrosyl-tRNA synthetases, Lys82 and Arg86, stabilize the
122 ognition differs between bacterial and human tyrosyl-tRNA synthetases, we sequenced several clones id
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