ライフサイエンスコーパス: tyrosyl

1 -[N,O-bis(5-isoquinolinesulfonyl)-N-methyl-l-tyrosyl]-4-phenylpiperazine (KN-62) blocks MOR-mediated

2 [N,O-bis(5-isoquinolinesulphonyl)-N-methyl-L-tyrosyl]-4-phenylpiperazine)] rescues VP gene transcript

3 rentially modulated SHP-2 phosphorylation at tyrosyl 542 and 580 residues, which may regulate Erk1/2

4 blocked in vivo by a resveratrol-displacing tyrosyl adenylate analogue.

5 eviously described for synthesis of 1 mol of tyrosyl adenylate by the dimeric class I tyrosyl-tRNA sy

6 ivity," with respect to tyrosine binding and tyrosyl-adenylate formation.

7 tly affect the kinetics for formation of the tyrosyl-adenylate intermediate and actually increases th

8 ATP results in formation of an enzyme-bound tyrosyl-adenylate intermediate and is accompanied by a b

9 ep, tyrosine is activated by ATP to form the tyrosyl-adenylate intermediate.

10 by a "hopping" mechanism involving multiple tyrosyl (and perhaps one tryptophanyl) radical intermedi

11 Both the Escherichia coli tyrosyl- and leucyl-RS/tRNA(CUA) pairs were shown to be

12 nucleotide reductase (RNR) houses a diferric tyrosyl cofactor (Fe2(III)-Y(*)) that initiates nucleoti

13 ), with decreased phosphorylation of various tyrosyl-containing proteins, EphB4, and its downstream t

14 xerts a unique regulatory fingerprint of RTK tyrosyl dephosphorylation and suggest a complex signalin

15 the involvement of the RPTP subfamily in RTK tyrosyl dephosphorylation has not been established.

16 phosphorylated, much less is known about RTK tyrosyl dephosphorylation.

17 actin binding activity of ACTN4 by inducing tyrosyl-directed phosphorylation.

18 afeguards genome integrity by hydrolyzing 5'-tyrosyl DNA adducts formed by abortive topoisomerase II

19 DP2; aka TTRAP/EAPII) that possesses weak 3'-tyrosyl DNA phosphodiesterase (3'-TDP) activity, in vitr

20 Recently, we identified a second tyrosyl DNA phosphodiesterase (TDP2; aka TTRAP/EAPII) th

21 Tyrosyl DNA phosphodiesterase 1 (TDP1) and human AP-endo

22 We recently showed that tyrosyl DNA phosphodiesterase 1 (Tdp1) regulates the acc

23 Here, we report that depletion of Tyrosyl DNA phosphodiesterase 1 (TDP1) sensitizes human

24 This is typified by defects in tyrosyl DNA phosphodiesterase 1 (TDP1), which removes st

25 Tyrosyl DNA phosphodiesterase 2 (TDP2) is a multifunctio

26 Tyrosyl DNA phosphodiesterase 2 (Tdp2) is a recently dis

27 Tyrosyl DNA phosphodiesterase 2 (TDP2), a newly discover

28 ural compounds in the presence or absence of tyrosyl DNA phosphodiesterase I (TDP1); a key TOP1-media

29 Tyrosyl DNA phosphodiesterase II (TDP2) is a recently di

30 Importantly, we identified TDP2, a 5'-tyrosyl DNA phosphodiesterase involved in the repair of

31 e 2 (Tdp2) is a recently discovered human 5'-tyrosyl DNA phosphodiesterase that repairs this topoisom

32 RAP is, to our knowledge, the first human 5'-tyrosyl DNA phosphodiesterase to be identified, and we s

33 Tyrosyl DNA phosphodiesterase-1 protects cells from abor

34 , and we suggest that this enzyme is denoted tyrosyl DNA phosphodiesterase-2 (TDP2).

35 mozygous mutations in the TDP2 gene encoding tyrosyl DNA phosphodiesterase-2, an enzyme that repairs

36 o the viral polymerase (P protein) through a tyrosyl-DNA phosphodiester bond.

37 (PLD), phosphatidylserine synthase (PSS) and tyrosyl-DNA phosphodiesterase (TDP), and conserved catal

38 Human tyrosyl-DNA phosphodiesterase (TDP1) hydrolyzes the phos

39 Human tyrosyl-DNA phosphodiesterase (TDP1) hydrolyzes the phos

40 Tyrosyl-DNA phosphodiesterase (TDP1) is a phylogenetical

41 Human tyrosyl-DNA phosphodiesterase (Tdp1) processes 3'-blocki

42 hodiester bond at the 3'-ends of DNA breaks, tyrosyl-DNA phosphodiesterase (Tdp1) repairs topoisomera

43 ssess moderate inhibitory activities against tyrosyl-DNA phosphodiesterase 1 (TDP1) and tyrosyl-DNA p

44 Tyrosyl-DNA phosphodiesterase 1 (Tdp1) catalyzes the hyd

45 vity of the potential anticancer drug target tyrosyl-DNA phosphodiesterase 1 (TDP1) in a very simple,

46 Here, we reveal the importance of tyrosyl-DNA phosphodiesterase 1 (TDP1) in the repair of

47 Tyrosyl-DNA phosphodiesterase 1 (TDP1) is a key enzyme i

48 Tyrosyl-DNA phosphodiesterase 1 (Tdp1) is an enzyme that

49 Tyrosyl-DNA phosphodiesterase 1 (TDP1), a key repair enz

50 rved in individuals containing a mutation in tyrosyl-DNA phosphodiesterase 1 (TDP1), an enzyme that c

51 d the involvement of topoisomerase 1 (TOP1), tyrosyl-DNA phosphodiesterase 1 (TDP1), and single-stran

52 ir cross-complementing protein 1 (XRCC1) and tyrosyl-DNA phosphodiesterase 1 (TDP1), using fluorescen

53 mal cells, suggesting a significant role for tyrosyl-DNA phosphodiesterase 1 in removing 3'-PG blocki

54 human spinocerebellar ataxias-aprataxin and tyrosyl-DNA phosphodiesterase 1-implicating SSBR in prot

55 osphate termini, and were more persistent in tyrosyl-DNA phosphodiesterase 1-mutant SCAN1 than in nor

56 ntermediates, e.g. polynucleotide kinase and tyrosyl-DNA phosphodiesterase 1.

57 nd were further increased by inactivation of tyrosyl-DNA phosphodiesterase 1.

58 mage as an alternative pathway from PARP and tyrosyl-DNA phosphodiesterase 1.

59 The recently discovered enzyme tyrosyl-DNA phosphodiesterase 2 (TDP2) has been implicat

60 TOP2cc facilitates a proteasome-independent tyrosyl-DNA phosphodiesterase 2 (TDP2) hydrolase activit

61 Mammalian Tyrosyl-DNA phosphodiesterase 2 (Tdp2) reverses Topoisom

62 t tyrosyl-DNA phosphodiesterase 1 (TDP1) and tyrosyl-DNA phosphodiesterase 2 (TDP2), two enzymes that

63 double-strand breaks are rejoined in part by tyrosyl-DNA phosphodiesterase 2 (TDP2)-dependent non-hom

64 TDP2 possesses both 3'- and 5'-tyrosyl-DNA phosphodiesterase activity, which is general

65 Tyrosyl-DNA phosphodiesterase I (Tdp1) catalyzes the rep

66 Tyrosyl-DNA phosphodiesterase I (Tdp1) is a cellular enz

67 Tyrosyl-DNA phosphodiesterase I (Tdp1) is a member of th

68 Tyrosyl-DNA phosphodiesterase I (Tdp1) plays a key role

69 Tyrosyl-DNA phosphodiesterase I (TDP1) repairs stalled t

70 Substances with dual tyrosyl-DNA phosphodiesterase I-topoisomerase I inhibito

71 ingle-strand break repair factors, including tyrosyl-DNA phosphodiesterase-1 or XRCC1, resulted in in

72 f VPg unlinkase as the DNA repair enzyme, 5'-tyrosyl-DNA phosphodiesterase-2 (TDP2).

73 Tdp1 and Tdp2 are two tyrosyl-DNA phosphodiesterases that can repair damaged D

74 We show that two genes, TDP1, a tyrosyl-DNA-phosphdiesterase, and TAF12, an RNA polymera

75 merase-DNA adducts and their known repair by tyrosyl-DNA-phosphodiesterase (TDP) 1 or TDP2 suggested

76 Tyrosyl-DNA-phosphodiesterase 1 (Tdp1) can disjoin pepti

77 was attributed to the reduced expression of tyrosyl-DNA-phosphodiesterase 1 (TDP1), a DNA repair enz

78 covalent complexes are excised (in part) by tyrosyl-DNA-phosphodiesterase 2 (TDP2/TTRAP/EAP2/VPg unl

79 s(-1)M(-1) for TDP2 using single-stranded 5'-tyrosyl-DNA.

80 sulting in a Y --> H substitution in the tri-tyrosyl domain of the enamel extracellular matrix protei

81 rromagnetically coupled iron centers and one tyrosyl free radical, Y122*/beta2.

82 In tyrosyl-glycine and Leu-enkephalin, which have N-termina

83 onically coupled along dynamics to the Tyr-Z tyrosyl group, releases a proton from the nearby W1 wate

84 The cleaved MeP-tyrosyl intermediate formed by Flp(R191A) can be targete

85 nt for understanding redox chains relying on tyrosyl intermediates.

86 most efficient when the DNA attached to the tyrosyl is in a single-stranded configuration and that T

87 A transient tyrosyl-like radical with a narrow doublet X-band EPR si

88 sphodiester bond at a DNA 3'-end linked to a tyrosyl moiety and has been implicated in the repair of

89 In the second step, the tyrosyl moiety is transferred to the 3' end of tRNA.

90 and actually increases the rate at which the tyrosyl moiety is transferred to tRNA(Tyr).

91 sphodiester bond at a DNA 3' end linked to a tyrosyl moiety.

92 ter bond between the DNA 3'-end and the Top1 tyrosyl moiety.

93 interactions mediated via the amelogenin tri-tyrosyl motif are a key mechanistic factor underpinning

94 The scaffold protein Gab2 is a major tyrosyl phosphoprotein in the CSF-1R signaling network.

95 mutant PI3K remained associated with several tyrosyl phosphoproteins, potentially explaining the disp

96 Here, we further investigate the role of the tyrosyl phosphorylated PAK1 (pTyr-PAK1) in regulation of

97 a detailed understanding of how RTKs become tyrosyl phosphorylated, much less is known about RTK tyr

98 kinases (RTKs) exist in equilibrium between tyrosyl-phosphorylated and dephosphorylated states.

99 d modular units, which recognize and bind to tyrosyl-phosphorylated peptide sequences on their target

100 to promote cell migration, as a major hyper-tyrosyl-phosphorylated protein in mouse and zebrafish mo

101 Binding of the tyrosyl-phosphorylated proteins at the fructose 1,6-bisp

102 at each RPTP induced a unique fingerprint of tyrosyl phosphorylation among 42 RTKs.

103 ted SHP-2 mutants enhanced SIRPalpha and PZR tyrosyl phosphorylation either by impairing SIRPalpha de

104 sphatase PTPN9 significantly increases ErbB2 tyrosyl phosphorylation in the SKBR3 breast cancer cell

105 PZR hyper-tyrosyl phosphorylation is facilitated in a phosphatase-

106 We conclude that GRK5 tyrosyl phosphorylation is required for the activation o

107 expression of PTPN9 DA dramatically enhances tyrosyl phosphorylation of ErbB2 and EGFR, respectively.

108 expression of PTPN9 wild type (WT) inhibits tyrosyl phosphorylation of ErbB2 and EGFR.

109 ion of PTPN9 WT or DA mutant does not affect tyrosyl phosphorylation of ErbB3 and Shc.

110 a(2)-adrenergic receptor activation promoted tyrosyl phosphorylation of GRK5 in smooth muscle cells.

111 However, tyrosyl phosphorylation of GRK5 was not necessary for GR

112 We show that the tyrosyl phosphorylation of PAK1 promotes PAK1 binding to

113 NA/C6 interaction leads to increased tyrosyl phosphorylation of Src, FAK, Akt, GSK3beta, and

114 in- and interferon gamma (IFN-gamma)-induced tyrosyl phosphorylation of STAT1 and STAT5.

115 It is unclear, apart from a chronic tyrosyl phosphorylation of STAT3, what mechanisms contri

116 odies (intrabodies) enhanced insulin-induced tyrosyl phosphorylation of the beta subunit of the insul

117 knockdown of PTPN9 expression also enhances tyrosyl phosphorylation of the ErbB1/epidermal growth fa

118 findings are characterized by enhancement of tyrosyl phosphorylation of the insulin receptor, insulin

119 e was no effect of acute ethanol exposure on tyrosyl phosphorylation of the insulin receptor, IRS-1,

120 Tyrosyl phosphorylation of wild type PAK1 decreases apop

121 ne MCF-7 because it is kept downregulated by tyrosyl phosphorylation of Y(296) by EGFR kinase.

122 ha treatment triggered a robust induction of tyrosyl phosphorylation on Shp2.

123 Tyrosyl phosphorylation plays a critical role in multipl

124 Palpha dephosphorylation or by promoting PZR tyrosyl phosphorylation.

125 s 153, 201, and 285 in PAK1 as sites of JAK2 tyrosyl phosphorylation.

126 gastrulation in a manner dependent upon PZR tyrosyl phosphorylation.

127 a native (40-95) disulfide bond by a nearby tyrosyl-prolyl stacking interaction, when disulfide bond

128 Tyrosyl protein sulfotransferase (TPST) is an enzyme req

129 -tyrosine sulfation is mediated by two Golgi tyrosyl-protein sulfotransferases (TPST-1 and TPST-2) th

130 or VHZ mediates dephosphorylation of phospho-tyrosyl (pTyr) and phospho-seryl/threonyl (pSer/pThr) re

131 h Fe(II) and O2 can self-assemble a diferric-tyrosyl radical (Fe(III)2-Y(*)) cofactor (1.2 Y(*)/beta2

132 bonucleotide reductase (RNR) uses a diferric-tyrosyl radical (Fe(III)2-Y(*)) cofactor to initiate nuc

133 Ib RNR self-assembles an essential diferric-tyrosyl radical (Fe(III)2-Y(*)) in vitro, whereas assemb

134 leotide reductases (RNRs) require a diferric-tyrosyl radical (Fe(III)2-Y*) cofactor to produce deoxyn

135 onstrate that this enzyme uses a dimanganese-tyrosyl radical (Mn(III)2-Y(*)) cofactor in vivo.

136 in vitro, whereas assembly of a dimanganese-tyrosyl radical (Mn(III)2-Y(*)) cofactor requires NrdI,

137 lpha), CDP and effector ATP to trap an amino tyrosyl radical (NH2Y*) in the active alpha2beta2 comple

138 b) ribonucleotide reductase (RNR) employs a tyrosyl radical (Y (*)) in its R2 subunit for reversible

139 and Ib RNRs, this reaction requires a stable tyrosyl radical (Y(*)) generated by oxidation of a reduc

140 In a class Ia or Ib RNR, a stable tyrosyl radical (Y(*)) is the C oxidant, whereas a Mn(IV

141 ribonucleotide reductase (RNR) uses either a tyrosyl radical (Y(*)) or a Mn(IV)/Fe(III) cluster in it

142 beta2 contains a stable di-iron tyrosyl radical (Y(122)(*)) cofactor required to generat

143 esides in alpha2, and the essential diferric-tyrosyl radical (Y(122)(*)) cofactor that initiates tran

144 beta2 contains the essential diferric tyrosyl radical (Y(122)(*)) cofactor which, in the prese

145 eine (C(439)) in alpha2 by a stable diferric tyrosyl radical (Y(122)*) cofactor in beta2.

146 long-range radical transfer over 35 A from a tyrosyl radical (Y(122)*) within the beta2 subunit to a

147 During turnover, a stable tyrosyl radical (Y*) at Y(122)-beta2 reversibly oxidizes

148 tal clusters for activity: an Fe(III)Fe(III)-tyrosyl radical (Y*) cofactor (class Ia), a Mn(III)Mn(II

149 beta contains the diferric-tyrosyl radical (Y*) cofactor essential for the reductio

150 beta subunit contains the essential diferric-tyrosyl radical (Y*) cofactor.

151 subunit is transiently oxidized by a stable tyrosyl radical (Y*) in the RNR small (beta2) subunit ov

152 s to deoxynucleotides with either a Mn(III)2-tyrosyl radical (Y*) or a Fe(III)2-Y* cofactor in the Nr

153 RNR was rapidly produced with 0.25 +/- 0.03 tyrosyl radical (Y*) per beta2 and a specific activity o

154 I/IV) intermediate, which generates a stable tyrosyl radical (Y*).

155 beta2 contains the essential tyrosyl radical (Y122(*)) that generates a thiyl radical

156 tide reduction, and beta2 harbors a diferric tyrosyl radical (Y122*) cofactor.

157 A diferric-tyrosyl radical (Y122*) in one subunit (beta2) generates

158 coupled mu-oxo bridged diiron cluster and a tyrosyl radical (Y122*).

159 quires a reversible oxidation over 35 A by a tyrosyl radical (Y122*, Escherichia coli) in subunit bet

160 beta2 subunit contains an essential diferric-tyrosyl radical (Y122O(*)) cofactor that is needed to in

161 nce electron transfer involving an essential tyrosyl radical (Y122O.) in the beta2 subunit.

162 ecombinant NrdF (rNrdF) contained a diferric-tyrosyl radical [Fe(III)(2)-Y(*)] cofactor.

163 We investigated electron transfer between a tyrosyl radical and cysteine residue in two systems, oxy

164 RNR is inactivated by loss of the essential tyrosyl radical and formation of a new radical.

165 rule out the possibility that MCR(BES) is a tyrosyl radical and indicate that if a tyrosyl radical i

166 iron(III/IV) cluster, X, which generates the tyrosyl radical and product (mu-oxo)diiron(III/III) clus

167 he nearly diffusion-limited reaction between tyrosyl radical and superoxide.

168 logue of the redox reaction between the PSII tyrosyl radical and the oxygen-evolving complex.

169 tions on the related interaction between the tyrosyl radical and the water in biological systems.

170 ry stable products of superoxide addition to tyrosyl radical are para-hydroperoxide derivatives (para

171 by redox-linked electrostatic changes in the tyrosyl radical aromatic ring.

172 The mechanism is thought to involve a tyrosyl radical as the oxidant on the basis of compariso

173 cleotide reductase (RNR) contains a diferric tyrosyl radical cofactor (Fe(2)(III)-Tyr(*)) that is ess

174 eductase (RNR) employs a mu-oxo-Fe2(III/III)/tyrosyl radical cofactor in its beta subunit to oxidize

175 radical transfer (RT) from a stable diferric-tyrosyl radical cofactor located >35 A away across the a

176 on the magnetic properties of the manganese-tyrosyl radical cofactor of Bacillus anthracis NrdF and

177 e direct precursor of the essential diferric-tyrosyl radical cofactor of the beta2 subunit of Escheri

178 cleotide reductases (RNRs) use a dimanganese-tyrosyl radical cofactor, Mn(III)(2)-Y(*), in their homo

179 nit is denoted NrdF, and harbors a manganese-tyrosyl radical cofactor.

180 ne, we report herein direct observation of a tyrosyl radical during both reactions of H2O2 with oxidi

181 c site and RR2 (beta) that houses a diferric-tyrosyl radical essential for ribonucleoside diphosphate

182 n state of the metal site, as opposed to the tyrosyl radical generated by other R2 subclasses.

183 The mechanism for tyrosyl radical generation in the [Re(P-Y)(phen)(CO)3]PF

184 for the formation of the C228-Y272 bond and tyrosyl radical generation is proposed.

185 The tyrosyl radical in NrdF is stabilized through its intera

186 ectroscopy, providing a firm support for the tyrosyl radical in the HCO enzymatic mechanism.

187 xyferryl heme decay, but not with changes in tyrosyl radical intensity or EPR line shape, indicating

188 is a tyrosyl radical and indicate that if a tyrosyl radical is formed during the reaction, it does n

189 conserved location of the cysteine-oxidizing tyrosyl radical of class Ia and Ib RNRs, we suggested th

190 Results are consistent with formation of a tyrosyl radical reasonably assigned to residue Tyr(229)

191 Reduction of the tyrosyl radical reveals Y122* Raman bands at 1499 and 15

192 ethyl peroxide led to some narrowing of the tyrosyl radical signal detected by EPR spectroscopy, con

193 This is the position proximal to the tyrosyl radical site in other R2 proteins and consistent

194 This dramatic modulation of tyrosyl radical stability by cyclooxygenase site ligands

195 the novel cofactor functionally replaces the tyrosyl radical used by conventional class I RNRs to ini

196 The half-life of total tyrosyl radical was 4.1 min in the control, >10 h with a

197 length aCRY revealed an unusually long-lived tyrosyl radical with a lifetime of 2.6 s, which is prese

198 roscopic observation of chemically competent tyrosyl radical(s).

199 ferric DHP contains both a ferryl heme and a tyrosyl radical, analogous to Compound ES of cytochrome

200 icating that the oxyferryl heme, and not the tyrosyl radical, is responsible for the self-destructive

201 he widely proposed mechanism that involves a tyrosyl radical, its direct observation under O2 reducti

202 is fully capable of generating the oxidized, tyrosyl radical-containing form of Mn-NrdF when exposed

203 diate that contains both a ferryl heme and a tyrosyl radical.

204 ies functions as a direct substitute for the tyrosyl radical.

205 giving rise to the temporary appearance of a tyrosyl radical.

206 the iron cluster and by the reduction of the tyrosyl radical.

207 and a shift in g values away from the native tyrosyl radical.

208 properties similar to those of the wild-type tyrosyl radical.

209 irmed that the majority radical species is a tyrosyl radical.

210 rom the kinetics of formation and decay of a tyrosyl radical.

211 g a conserved hydrogen bond to the catalytic tyrosyl radical/tyrosine, was examined for the first tim

212 a distance of ~35 A from the stable diferric/tyrosyl-radical (Y122(*)) cofactor in the beta subunit t

213 ucleotide reductase that requires a diferric-tyrosyl-radical [(Fe(III)(2)-Y.)(Fe(III)(2))] cofactor f

214 nd that, at high DMPO concentrations, mainly tyrosyl radicals (Hb-Tyr42/Tyr24 and Mb-Tyr103) are trap

215 Both tyrosyl radicals are transient and rapidly dissipated by

216 X-band EPR demonstrates that the two tyrosyl radicals differ in the orientation of their beta

217 heir unprotonated neutral form, but to date, tyrosyl radicals have only been observed in their unprot

218 generated on L-Tyr by UV-irradiation and to tyrosyl radicals identified in many other enzyme systems

219 he framework of the important role played by tyrosyl radicals in biological systems.

220 the redox-active tyrosine radical; the Y272 tyrosyl radicals in both the W290G and W290H variants ha

221 ) EPR reveals the presence of two species of tyrosyl radicals in Cpd ES with their g-tensor component

222 d assignments and to deduce the role(s) that tyrosyl radicals play in DHP, stopped-flow UV-visible an

223 Stabilization of the tyrosyl radicals was evident even at substoichiometric l

224 inhibitors on the stability of the preformed tyrosyl radicals were dramatic.

225 hanism for regulating the reactivity of PGHS tyrosyl radicals with cellular antioxidants.

226 ical derivatives of the amino acid tyrosine (tyrosyl radicals) which are also involved in physiologic

227 nhibitors that bind rapidly to COX-2, quench tyrosyl radicals, and reduce higher oxidation states of

228 xanthine oxidase, to several peptide-derived tyrosyl radicals, formed from horseradish peroxidase.

229 sines, Y(Z) and Y(D), which form the neutral tyrosyl radicals, Y(z)(*) and Y(D)(*).

230 -dependent, effects on the stability of both tyrosyl radicals.

231 .00186) similar to but not typical of native tyrosyl radicals.

232 yrosinase-catalyzed oxidation of tyrosine or tyrosyl residue in peptides.

233 onsible for dephosphorylating the C-terminal tyrosyl residue of histone H2A.X.

234 riant H2A.X is characterized by a C-terminal tyrosyl residue, Tyr-142, which is phosphorylated by an

235 ents and two helical re-entry loops and that tyrosyl residues are the structural specialization of th

236 cond phase, Src family kinases phosphorylate tyrosyl residues within the transmembrane and cytoplasmi

237 8 flies were defective in hydrolyzing 3'-DNA-tyrosyl residues, demonstrating that gkt is the Drosophi

238 elective hydroxylation of 3-substituted beta-tyrosyl-S-SgcC2 analogues, including the chloro-, bromo-

239 nalogues, but does not accept 3-hydroxy-beta-tyrosyl-S-SgcC2 as a substrate.

240 yzes the hydroxylation of ( S)-3-chloro-beta-tyrosyl-S-SgcC2 as the final step in the biosynthesis of

241 iciency, between (S)-3-chloro-5-hydroxy-beta-tyrosyl-(S)-SgcC2 and (R)-2-amino-1-phenyl-1-ethanol, an

242 SgcC5 uses (S)-3-chloro-5-hydroxy-beta-tyrosyl-SgcC2 as the donor substrate and exhibits regios

243 ex structures indicate that aromatic, mostly tyrosyl, side chains constitute the major part of the pr

244 nt family member interaction that depends on tyrosyl sulfation.

245 e enhanced markedly by overexpression of the tyrosyl sulfotransferase TPST2.

246 The propensity of the cYY tyrosyl to point toward Arg(386) was dependent on the pr

247 Because human tyrosyl transfer-RNA (tRNA) synthetase (TyrRS) transloca

248 The Methanococcus jannaschii tyrosyl-transfer-RNA synthetase-tRNA(CUA) (MjTyrRS-tRNA(

249 PO, the secondary reaction predominates over tyrosyl trapping, and a thiyl radical is formed and then

250 In this manner, a natural fragment of human tyrosyl tRNA synthetase (TyrRS), mini-TyrRS, has been sh

251 etic code, only the Methanococcus jannaschii tyrosyl tRNA synthetase and tRNA have been used extensiv

252 has a mutation in the gene (dtd) encoding D-tyrosyl-tRNA deacylase, an enzyme that prevents the misi

253 alleles of the nuclear-encoded mitochondrial tyrosyl-tRNA synthetase (Aatm) and the mitochondrial-enc

254 bifunctional Neurospora crassa mitochondrial tyrosyl-tRNA synthetase (CYT-18 protein) both aminoacyla

255 y explores the twin attributes of Leishmania tyrosyl-tRNA synthetase (LdTyrRS) namely, aminoacylation

256 The Neurospora crassa mitochondrial tyrosyl-tRNA synthetase (mtTyrRS; CYT-18 protein) evolve

257 ral effect of three CMT-causing mutations in tyrosyl-tRNA synthetase (TyrRS or YARS).

258 nation of methods, here we showed that human tyrosyl-tRNA synthetase (TyrRS) distributes to the nucle

259 The single tyrosyl-tRNA synthetase (TyrRS) gene in trypanosomatid g

260 Tyrosyl-tRNA synthetase (TyrRS) is able to catalyze the

261 Tyrosyl-tRNA synthetase (TyrRS) is known for its essenti

262 in catalysis by Bacillus stearothermophilus tyrosyl-tRNA synthetase (TyrRS), the temperature depende

263 internally deleted, SVs of homodimeric human tyrosyl-tRNA synthetase (TyrRS).

264 utation of the gene encoding the cytoplasmic tyrosyl-tRNA synthetase (TyrRS).

265 protein, the Neurospora crassa mitochondrial tyrosyl-tRNA synthetase (TyrRS; CYT-18), is bifunctional

266 Expression of CMT-mutant tyrosyl-tRNA synthetase also impairs translation, sugges

267 for both d-tyrosine activation by wild-type tyrosyl-tRNA synthetase and activation of l-tyrosine by

268 Bacillus stearothermophilus tyrosyl-tRNA synthetase binds d-tyrosine with an 8.5-fol

269 Catalysis of tRNA(Tyr) aminoacylation by tyrosyl-tRNA synthetase can be divided into two steps.

270 ed sigmoidal behavior presents a paradox, as tyrosyl-tRNA synthetase displays an extreme form of nega

271 K233A variant of Bacillus stearothermophilus tyrosyl-tRNA synthetase displays sigmoidal kinetics simi

272 Furthermore, as is the case for l-tyrosine, tyrosyl-tRNA synthetase exhibits "half-of-the-sites" rea

273 The activation of D-tyrosine by tyrosyl-tRNA synthetase has been investigated using sing

274 sine suggests that their side chains bind to tyrosyl-tRNA synthetase in similar orientations and that

275 e van't Hoff plots for the binding of ATP to tyrosyl-tRNA synthetase in the absence and presence of s

276 dy-state kinetic analyses of CHO cytoplasmic tyrosyl-tRNA synthetase revealed a 25-fold lower specifi

277 ional comparisons of mammalian and bacterial tyrosyl-tRNA synthetase revealed key differences at resi

278 ora crassa CYT-18 protein is a mitochondrial tyrosyl-tRNA synthetase that also promotes self-splicing

279 DI-CMTC is due to a defect in the ability of tyrosyl-tRNA synthetase to catalyze the aminoacylation o

280 ytokine function of the 528-amino acid human tyrosyl-tRNA synthetase was associated with pinpointed u

281 charging of tRNA(Tyr) with noncognate Phe by tyrosyl-tRNA synthetase was responsible for mistranslati

282 rmore, we find that downregulation of yars-2/tyrosyl-tRNA synthetase, an NMD target transcript, by da

283 of tyrosyl adenylate by the dimeric class I tyrosyl-tRNA synthetase, operates as well in this homote

284 ly>Val) in YARS2 gene encoding mitochondrial tyrosyl-tRNA synthetase, which interacts with m.11778G>A

285 An example is the 528-amino acid human tyrosyl-tRNA synthetase, which is made up of an N-termin

286 Its genome encodes a single copy of tyrosyl-tRNA synthetase.

287 DI-CMTC is not due to a catalytic defect in tyrosyl-tRNA synthetase.

288 ts the non-canonical function of L. donovani tyrosyl-tRNA synthetase.

289 which ATP binds to the functional subunit in tyrosyl-tRNA synthetase.

290 zed 1 and evolved a Methanococcus jannaschii tyrosyl-tRNA synthetase/tRNA(CUA) pair to genetically en

291 The mitochondrial tyrosyl-tRNA synthetases (mt TyrRSs) of Pezizomycotina f

292 The mitochondrial tyrosyl-tRNA synthetases (mtTyrRSs) of Pezizomycotina fu

293 netic reconstruction, two types of bacterial tyrosyl-tRNA synthetases (TyrRS) form distinct clades wi

294 Our results suggest that mitochondrial tyrosyl-tRNA synthetases with group I intron splicing ac

295 f genomic sequences shows that mitochondrial tyrosyl-tRNA synthetases with structural adaptations sim

296 ptations compared with nonsplicing bacterial tyrosyl-tRNA synthetases.

297 ocaldococcus jannaschii and Escherichia coli tyrosyl-tRNA synthetases.

298 thetase (Aatm) and the mitochondrial-encoded tyrosyl-tRNA that it aminoacylates.

299 reaction between amino acid hydroperoxides (tyrosyl, tryptophan, and histidine hydroperoxides) and C

300 correct positioning of the hydroxyl of this tyrosyl was essential for conversion of cYY.