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1  which trypto-phan is transferred from TrpRS-tryptophanyl adenylate to tRNA.
2 l-tRNA synthetase is shown here to sequester tryptophanyl adenylate.
3 l-tRNA synthetase was solved at 2.1 A with a tryptophanyl-adenylate bound at the active site.
4 tRNA to bind the reaction intermediate TrpRS-tryptophanyl-adenylate, but predominantly affects the ra
5 diation of WT hSOD1 and bSOD1 that generated tryptophanyl and tyrosyl radicals.
6 he resulting altered translational machinery tryptophanyl (ATMW-BL21) E. coli strain as an orthogonal
7                Here we show that the E. coli tryptophanyl (EcTrp) pair is an excellent TGA-suppressor
8 o NH(2)-FMS can result in less tyrosinyl and tryptophanyl exposure OPAA molecules to aqueous environm
9                                   Changes in tryptophanyl fluorescence indicated that Ca2+ induced lo
10 ins (UFAC) induced concordant blue-shifts in tryptophanyl fluorescence spectra and a loss of beta-str
11 ace hydrophobicity and decrease in intrinsic tryptophanyl fluorescence.
12 een rho(C) and g(x) in other radicals, e.g., tryptophanyl, is discussed.
13 gal metabolite, apicidin [cyclo(N-O-methyl-L-tryptophanyl-L -isoleucinyl-D-pipecolinyl-L-2-amino-8-ox
14  to participate in biosynthetic nitration of tryptophanyl moieties in vivo.
15 ons; in Streptomyces, NOS proteins nitrate a tryptophanyl moiety in synthesis of a phytotoxin.
16 ts that the ribosomal A site occupied by the tryptophanyl moiety of the charged transfer RNA is the s
17      Here we report that the E. coli derived tryptophanyl pair can be combined with the archaeal tyro
18                                Moreover, the tryptophanyl radical detected by EPR spectroscopy of H2O
19  basis for the creation and maintenance of a tryptophanyl radical in a three-helix bundle protein maq
20 h species, and the deprotonated state of the tryptophanyl radical in the diiron(III,IV)-W* transient,
21  High field RFQ-EPR spectroscopy confirmed a tryptophanyl radical signal, and new analyses of X-band
22 This is followed by a mixture of tyrosyl and tryptophanyl radical species and finally to only a tyros
23 Both compound I and a compound II-associated tryptophanyl radical that resembles cytochrome c peroxid
24 pol, which recombines with the hSOD1-derived tryptophanyl radical, and did not occur in the absence o
25 oduct, characteristic of the generation of a tryptophanyl radical-cation (Trp(233*+)).
26  involving multiple tyrosyl (and perhaps one tryptophanyl) radical intermediates along a specific pat
27                                              Tryptophanyl radicals have been observed both in their p
28 ediates corresponding to neutral tyrosyl and tryptophanyl radicals that are formed along minor reacti
29 xidized to a similar extent to hSOD1-derived tryptophanyl radicals.
30                                          The tryptophanyl residue at the 5'-terminus packs tightly ag
31  by gel-filtration chromatography, intrinsic tryptophanyl residue fluorescence changes, titration cal
32                A 33% quench of the intrinsic tryptophanyl residue fluorescence of HD(wt) by phosphate
33  calorimetry and by changes in the intrinsic tryptophanyl residue fluorescence.
34                               Placement of a tryptophanyl residue near the serine binding site (W139F
35 xamined the fluorescence emission of the two tryptophanyl residues in the active site over the pH ran
36 lthough the quantum yield had decreased, the tryptophanyl residues remained largely buried.
37 vestigated: MPD-dependent C-mannosylation of tryptophanyl residues, and glucose-P-dolichol (GPD)-depe
38 f the synthetic peptide, which contained two tryptophanyl residues, shifted toward blue and increased
39 e near-UV circular dichroism (CD) spectra of tryptophanyl residues.
40 on (C) domain stereoselectively hydrolyzes d-tryptophanyl-S-phosphopantetheine thioester and thus rep
41 y be used as a "fingerprint" to identify the tryptophanyl side chains in situations where the benzene
42                                An orthogonal tryptophanyl-transfer RNA (tRNA) synthetase (TrpRS)-muta
43                                 An auxiliary tryptophanyl tRNA synthetase (drTrpRS II) that interacts
44 iodurans (deiNOS) associates with an unusual tryptophanyl tRNA synthetase (TrpRS).
45 ted induction of the gene encoding the human tryptophanyl tRNA synthetase (WRS) results in the produc
46 netic codes, we have developed an orthogonal tryptophanyl tRNA synthetase and tRNA pair, derived from
47  aromatic amino acids; and cells harboring a tryptophanyl tRNA synthetase mutation conferring tempera
48       Kinetoplastids encode a single nuclear tryptophanyl tRNA that contains a CCA anticodon able to
49  with an engineered Saccharomyces cerevisiae tryptophanyl tRNA-synthetase (Trp-RS):suppressor tRNA pa
50 an orthogonal promoter and to reengineer the tryptophanyl tRNA-synthetase:suppressor tRNA pair from S
51 nitial amber suppressor version of the yeast tryptophanyl tRNA.
52 tion catalyzed by wild-type Escherichia coli tryptophanyl-tRNA synthe-tase (TrpRS) have now been inve
53 UAAs) into proteins using engineered E. coli tryptophanyl-tRNA synthetase (EcTrpRS)-tRNA(Trp) pairs.
54 ered tyrosyl-tRNA synthetase (EcTyrRS) and a tryptophanyl-tRNA synthetase (EcTrpRS).
55              We identify a splice variant of tryptophanyl-tRNA synthetase (mini-WARS) as an unconvent
56 es the first step of protein synthesis-human tryptophanyl-tRNA synthetase (T2-TrpRS) has potent anti-
57 ccus radiodurans NOS (deiNOS) and an unusual tryptophanyl-tRNA synthetase (TrpRS II) catalyzes the re
58 al structures of Bacillus stearothermophilus tryptophanyl-tRNA synthetase (TrpRS) afford evidence tha
59 r example, an alternative splice fragment of tryptophanyl-tRNA synthetase (TrpRS) and a similar natur
60                           Two forms of human tryptophanyl-tRNA synthetase (TrpRS) are produced in viv
61 that competes with tryptophan for binding to tryptophanyl-tRNA synthetase (TrpRS) enzymes.
62 c.770A > G (p.His257Arg), in the cytoplasmic tryptophanyl-tRNA synthetase (TrpRS) gene (WARS) that co
63                               Binding ATP to tryptophanyl-tRNA synthetase (TrpRS) in a catalytically
64                                              Tryptophanyl-tRNA synthetase (TrpRS) is a close homologu
65                                        Human tryptophanyl-tRNA synthetase (TrpRS) is active in transl
66  by contemporary Bacillus stearothermophilus tryptophanyl-tRNA synthetase (TrpRS) over that of TrpRS
67                     We have investigated the tryptophanyl-tRNA synthetase (TrpRS) purified from six a
68                                              Tryptophanyl-tRNA Synthetase (TrpRS) Urzyme (fragments A
69                          As observed for the tryptophanyl-tRNA synthetase (TrpRS) Urzyme, these fragm
70  the aromatic amino acid permease (aroP) and tryptophanyl-tRNA synthetase (trpS) contained several am
71 nt facilitating this process, and pinpointed tryptophanyl-tRNA synthetase (WARS1) as its source.
72                                Mitochondrial tryptophanyl-tRNA synthetase (Wars2), encoding an L53F p
73            Furthermore, we show that E. coli tryptophanyl-tRNA synthetase also displays tRNA-dependen
74 We deleted the anticodon binding domain from tryptophanyl-tRNA synthetase and fused the discontinuous
75  we report the co-crystal structure of human tryptophanyl-tRNA synthetase and tRNATrp.
76 an activation by Bacillus stearothermophilus tryptophanyl-tRNA synthetase falls asymptotically to a p
77 The crystal structure of a highly homologous tryptophanyl-tRNA synthetase from Bacillus stearothermop
78 ption of the auxiliary, antibiotic-resistant tryptophanyl-tRNA synthetase gene (trpRS1) in Streptomyc
79 RNATrp, and WRS-85D is likely to be the only tryptophanyl-tRNA synthetase gene in Drosophila.
80 la embryonic salivary gland, we identified a tryptophanyl-tRNA synthetase gene that maps to cytologic
81 uss the potential noncanonical activities of tryptophanyl-tRNA synthetase in immune response and regu
82                                The bacterial tryptophanyl-tRNA synthetase inhibitor indolmycin featur
83 id activation by Bacillus stearothermophilus tryptophanyl-tRNA synthetase involves three allosteric s
84     A potential polymorphic variant of human tryptophanyl-tRNA synthetase is shown here to sequester
85 e our preliminary description of the class I tryptophanyl-tRNA synthetase minimal catalytic domain wi
86  subtilis containing a temperature-sensitive tryptophanyl-tRNA synthetase produce elevated levels of
87                While kinetic analysis of the tryptophanyl-tRNA synthetase suggests discrimination aga
88                 A crystal structure of human tryptophanyl-tRNA synthetase was solved at 2.1 A with a
89                       The structure of yeast tryptophanyl-tRNA synthetase was solved to 1.8 A by usin
90 ions were mapped to the trpS locus (encoding tryptophanyl-tRNA synthetase) have been previously isola
91 enzymes, tyrosyl-tRNA synthetase (TyrRS) and tryptophanyl-tRNA synthetase, connect protein synthesis
92 ining a temperature-sensitive mutant form of tryptophanyl-tRNA synthetase, encoded by the trpS1 allel
93 hich the HipT toxin specifically targets the tryptophanyl-tRNA synthetase, TrpS.
94 ese nucleotides for recognition by the plant tryptophanyl-tRNA synthetase.
95 Recent work suggests that human tyrosyl- and tryptophanyl-tRNA synthetases (TrpRS) link protein synth
96 he possibility that present day tyrosyl- and tryptophanyl-tRNA synthetases appeared after the separat
97   Ij particular, the eukaryotic tyrosyl- and tryptophanyl-tRNA synthetases are more related to each o
98 s shared by all tyrosyl-tRNA synthetases and tryptophanyl-tRNA synthetases for amino acid discriminat
99 ts of the closely related human tyrosyl- and tryptophanyl-tRNA synthetases were discovered to be acti
100  (another antibiotic that inhibits bacterial tryptophanyl-tRNA synthetases) and that its transcriptio
101 reptomyces coelicolor has two genes encoding tryptophanyl-tRNA synthetases, one of which (trpRS1) is
102 ycin, two antibiotics that inhibit bacterial tryptophanyl-tRNA synthetases.
103 at shows an unusual picture for tyrosyl- and tryptophanyl-tRNA synthetases.
104        Indoleamine-2,3-dioxygenase (IDO) and tryptophanyl-tRNA-synthetase (TTS) are interferon-gamma
105        The amino acid binding domains of the tryptophanyl (TrpRS)- and tyrosyl-tRNA synthetases (TyrR

 
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