ライフサイエンスコーパス: selenocysteine

1 proteins in the form of the 21st amino acid, selenocysteine.

2 nslational recoding of the UGA stop codon as selenocysteine.

3 nslational recoding of the UGA stop codon to selenocysteine.

4 doxin reductase contains the rare amino acid selenocysteine.

5 , whereas related sensitive moths accumulate selenocysteine.

6 to proteins that lack canonical encoding for selenocysteine.

7 ctors in the late amino acids tryptophan and selenocysteine.

8 athway amino acids selenohomocysteine and/or selenocysteine.

9 more stable than the corresponding alkylated selenocysteine.

10 orelevant functional groups and is unique to selenocysteine.

11 selenoproteins are known to contain multiple selenocysteines.

12 metry to contain selenomethionine and methyl-selenocysteine (1:1-3 ratio), both excellent dietary Se

13 allireducens harboring 4 tungsten, 4 zinc, 2 selenocysteines, 6 FAD, and >50 FeS cofactors.

14 are recoded to cotranslationally incorporate selenocysteine, a rare selenium-containing amino acid.

15 The selenocysteine allows SelS to rapidly re-form its selene

16 hat of atypical 2-Cys peroxiredoxin and that selenocysteine allows SelS to sustain activity under oxi

17 o cis-acting elements for UGA translation as selenocysteine, although different mechanisms may underl

18 ed by expressed protein ligation of a single selenocysteine amino acid to a 243-CA truncation.

19 , the selenium donor for the biosynthesis of selenocysteine and 2-selenouridine residues in seleno-tR

20 s, in that it catalyzes the decomposition of selenocysteine and allows selenium to be recycled for ad

21 nd that the codon UGA specifies insertion of selenocysteine and cysteine in the ciliate Euplotes cras

22 duced homolysis of the C-Se and C-S bonds of selenocysteine and cysteine, respectively, we demonstrat

23 ected at low concentrations while Se-(Methyl)selenocysteine and inorganic selenium species (selenite

24 cs, glucosinolates, sulphoraphane, Se-methyl selenocysteine and myrosinase in broccoli.

25 bly selenocystathionine) in addition to some selenocysteine and selenate.

26 onstrate (77)Se NMR spectroscopy of multiple selenocysteine and selenomethionine residues in the sulf

27 ight play an important role in regulation of selenocysteine and selenoprotein synthesis.

28 r/Se assimilation followed by methylation of selenocysteine and the targeted sequestration of methyls

29 5% C-Se-C forms, 33-42% selenocystine, 5-12% selenocysteine, and 11-14% trimethylselenonium ion.

30 imilation and volatilization, methylation of selenocysteine, and conversion of selenocysteine to elem

31 (SepSecS) catalyzes the terminal reaction of selenocysteine, and is vital for human selenoproteome in

32 aryotic organisms lack the ability to insert selenocysteine, and prokaryotes have a recoding apparatu

33 or broad and direct detection of proteogenic selenocysteines are limited.

34 suggest that Sepp1 isoforms with six or more selenocysteines are taken up by apoER2.

35 (i.e., after decoding the first UGA codon as selenocysteine) are fully competent to terminate transla

36 ur analysis also provides robust support for selenocysteine as the ancestral ligand for the Mo/W atom

37 ranging from 1.03-2.03+/-0.2 mug kg(-1) and selenocysteine at a concentration of 1.47+/-0.1 mug kg(-

38 ) facilitates translational incorporation of selenocysteine at a UGA codon.

39 er in the polypeptide chain as compared with selenocysteine at the UGA codon, expression of the catal

40 uced to only two proteins, one of which is a selenocysteine-based glutathione peroxidase, the first f

41 We report the development of two facile selenocysteine-based strategies to generate the DUB prob

42 essential micronutrient, with the amino acid selenocysteine being genetically encoded in 25 natural h

43 nase activities as well as molybdopterin and selenocysteine biosynthetic pathways.

44 eavage complex induction, the thiol-reactive selenocysteine, but not the non-thiol-reactive selenomet

45 y of the human terminal synthetic complex of selenocysteine by using small angle x-ray scattering, mu

46 Following ligation, the selenocysteine can be deselenized into an alanine or ser

47 o-peptides and thus constrained by where the selenocysteine can be positioned.

48 Furthermore, the selenocysteine can be used to selectively introduce site

49 ing that efficient incorporation of multiple selenocysteines can be reconstituted in rabbit reticuloc

50 and is incorporated into more than 25 human selenocysteine-containing (Sec-containing) proteins via

51 its enzymatic function, we have isolated the selenocysteine-containing enzyme by relying on the aggre

52 Only the selenocysteine-containing enzyme is active.

53 hospholipid glutathione peroxidase (GPX4), a selenocysteine-containing enzyme that dissipates lipid p

54 Glutathione peroxidase-1 (GPx-1) is a selenocysteine-containing enzyme that plays a major role

55 ondrial thioredoxin reductases are essential selenocysteine-containing enzymes that control thioredox

56 f thioredoxin glutathione reductase (TGR), a selenocysteine-containing flavoenzyme required by the pa

57 ver, 100- to 1,000-fold more active than non-selenocysteine-containing MsrB enzymes for free Met-(R)-

58 Recently, a novel selenocysteine-containing oxidoreductase, Sep15, has bee

59 Glutathione peroxidase-3 (GPx-3) is a selenocysteine-containing plasma protein that scavenges

60 Employing selenocysteine-containing protein fragments to form the

61 Thioredoxin reductase 1 (TrxR1) is a selenocysteine-containing protein involved in cellular r

62 The synthesis of selenocysteine-containing proteins (selenoproteins) invo

63 emonstrate that the selective translation of selenocysteine-containing proteins can be regulated by t

64 Selenoproteins are a group of selenocysteine-containing proteins with major roles in c

65 hich are predicted to have a large number of selenocysteine-containing proteins.

66 The glutathione peroxidases, a family of selenocysteine-containing redox enzymes, play pivotal ro

67 s a radical SAM domain peptide maturase with selenocysteine-containing targets, suggesting a new biol

68 ), was recombinantly fused with a C-terminal selenocysteine-containing tetrapeptide Sel-tag, allowing

69 an early stop codon, and SelP, which had low selenocysteine content.

70 ontaining compounds, but increased Se-methyl-selenocysteine content.

71 ysteine separated by two other residues from selenocysteine) corresponds to the CXXC motif in thiored

72 vities on specialized fast reacting cysteine/selenocysteine (Cys/Sec) residues.

73 ve Cys in proteins by searching for sporadic selenocysteine-Cys pairs in sequence databases.

74 Deiodinases are selenocysteine-dependent membrane proteins catalyzing th

75 the CXC motif, and by construction of a CXU selenocysteine derivative, which has permitted XAS studi

76 In mammals, UGA can be reassigned to selenocysteine during translation of selenoproteins by a

77 The nucleophilic selenol group of selenocysteine endows this rare amino acid with unique c

78 e utilization of the 21st natural amino acid selenocysteine for the generation of IgG and Fab molecul

79 nthase (SepSecS) catalyzes the final step of selenocysteine formation by a poorly understood tRNA-dep

80 X-HPLC/ICPMS also detected selenocystine and selenocysteine, further confirming the results obtained

81 f Orp1 is similar to that found in mammalian selenocysteine glutathione peroxidases.

82 ion of saturation concentration of Se-methyl-selenocysteine in broccoli cv.

83 hat the covalent inhibition of the catalytic selenocysteine in Gpx4 prevents elimination of PUFA hydr

84 ered voltage-gated Na(+) channel harboring a selenocysteine in its inactivation motif, as a non-photo

85 oprotein P (SelenoP) has a redox-functioning selenocysteine in its N-terminal domain and nine seleniu

86 epresentatives that lack this metal, whereas selenocysteine in proteins is dynamically exchanged with

87 relies on the co-translational insertion of selenocysteine in response to UGA codons.

88 sm of oxidation of the catalytic cysteine or selenocysteine in thiol peroxidases.

89 umpolung strategy for the bioconjugation of selenocysteine in unprotected peptides.

90 n IgG1-derived Fc fragment with a C-terminal selenocysteine in yields comparable to conventional mono

91 in and nine selenium transporter-functioning selenocysteines in its C-terminal domain.

92 Mice, rats, and humans have 10 selenocysteines in Sepp1, which are incorporated via rec

93 vitamin B(12)), and selenium (in the form of selenocysteine) in 747 sequenced organisms at the follow

94 that ribosomes in the "processive" phase of selenocysteine incorporation (i.e., after decoding the f

95 translational control pathways that regulate selenocysteine incorporation and affect ribosomal tRNA s

96 int for the presence of factors required for selenocysteine incorporation and as a "bottleneck," slow

97 Additionally, SECp43 increases selenocysteine incorporation and selenoprotein mRNA leve

98 The mechanisms of selenocysteine incorporation and selenoprotein synthesis

99 affecting the SECISBP2 protein necessary for selenocysteine incorporation are linked to human disease

100 ons, that ribosomes become less efficient at selenocysteine incorporation as the distance between UGA

101 Selenocysteine incorporation at the first UGA codon is i

102 ssages would seem to demand highly efficient selenocysteine incorporation due to the compounding effe

103 translational GTPases such as EF-Tu and the selenocysteine incorporation factor SelB.

104 that increase or decrease the efficiency of selenocysteine incorporation in Escherichia coli without

105 eukaryotes and SelB in prokaryotes, promotes selenocysteine incorporation into selenoproteins by a st

106 UGA codons is increased, and that efficient selenocysteine incorporation is not dependent on cis-act

107 The mechanism by which the limiting selenocysteine incorporation machinery is preferentially

108 Studies of the eukaryotic selenocysteine incorporation mechanism suggest that sele

109 Selenocysteine incorporation occurs during translation o

110 Bacterial selenocysteine incorporation occurs in response to opal

111 Engineered ribosomes with improved selenocysteine incorporation provide valuable tools for

112 r mutations that can alter the efficiency of selenocysteine incorporation.

113 ative splicing, dicistronic translation, and selenocysteine incorporation.

114 e R543Q missense substitution located in the selenocysteine insertion domain resulted in residual act

115 ysteine incorporation mechanism suggest that selenocysteine insertion is inefficient compared with te

116 the first report of a land plant possessing selenocysteine insertion machinery at the sequence level

117 nism involving a 3 untranslated region (UTR) selenocysteine insertion sequence (SECIS) and the SECIS-

118 This recoding event is specified by the selenocysteine insertion sequence (SECIS) element and re

119 It is thought that the SelenoCysteine Insertion Sequence (SECIS) element and UG

120 A selenocysteine insertion sequence (SECIS) element in the

121 the presence of two copies of tRNA-Sec and a selenocysteine insertion sequence (SECIS) element which

122 s, the recoding of UGA as Sec depends on the selenocysteine insertion sequence (SECIS) element, a ste

123 codons and is dependent on the presence of a selenocysteine insertion sequence (SECIS) element, which

124 (Sec) codons in selenoproteins depends on a selenocysteine insertion sequence (SECIS) in the 3'-UTR

125 ture in the 3'-untranslated region, termed a selenocysteine insertion sequence (SECIS), and SECIS-bin

126 SelB), and a specific mRNA sequence known as selenocysteine insertion sequence (SECIS).

127 Selenocysteine insertion sequence binding protein 2 (SBP

128 GPX4 rs713041 is located near the selenocysteine insertion sequence element in the GPX4 3'

129 This process depends on the nature of the selenocysteine insertion sequence element located in the

130 could only be expressed when the Drosophila selenocysteine insertion sequence element was used, wher

131 Selenocysteine insertion sequence-associating factors, a

132 CIS binding protein 2, which is required for selenocysteine insertion, thereby inhibiting the synthes

133 stop codon reassignment that is required for selenocysteine insertion.

134 oding the stop codon UGA from termination to selenocysteine insertion.

135 om mice carrying genomic deletions of 3' UTR selenocysteine-insertion-sequences (SECIS1 and SECIS2).

136 site-specific antibody conjugation methods, selenocysteine interface technology (i) only involves a

137 tial trace element, which is incorporated as selenocysteine into at least 25 selenoproteins using a u

138 cis-acting elements for the incorporation of selenocysteine into selenoproteins.

139 Selenocysteine is cotranslationally inserted into protei

140 Known as the "21st" amino acid, selenocysteine is inserted into proteins by recoding UGA

141 Selenocysteine is inserted into selenoproteins via the t

142 Although the site specific incorporation of selenocysteine is of great interest for protein engineer

143 The decoding of specific UGA codons as selenocysteine is specified by the Sec insertion sequenc

144 Selenocysteine is the only genetically encoded amino aci

145 Selenocysteine is the only proteinogenic amino acid enco

146 Here it is demonstrated that selenocysteine is the residue oxidized by the peroxide s

147 Because it contains the rare amino acid selenocysteine, it belongs to the family of selenoprotei

148 Selenocysteine, known as the 21st amino acid, is then in

149 GPX4 by covalently targeting the active site selenocysteine, leading to accumulation of PUFA hydroper

150 s bind to the Mo following dissociation of a selenocysteine ligand to create a vacant coordination si

151 Selenocysteine lyase (Scly) is an enzyme that plays an i

152 Selenocysteine lyase (Scly) is the enzyme that supplies

153 , selenium levels are controlled through the selenocysteine machinery and expression of abundant sele

154 ssion data linked certain selenoproteins and selenocysteine machinery genes and suggested functional

155 rcome the placement and size restrictions in selenocysteine-mediated chemical ligation.

156 Therefore, selenocysteine-mediated expressed protein ligation simpl

157 Selenocysteine-mediated ligation is noteworthy for its h

158 dimer), selenomethionine (SeMet), and methyl-selenocysteine (MeSeCys) were separated, identified and

159 We describe this concept as illustrated in selenocysteine metabolism and other pathways and discuss

160 rization of the gene that encodes a putative selenocysteine methyltransferase (SMT) enzyme from the n

161 the accumulator enzyme (AbSMT) but lacks the selenocysteine methyltransferase activity in vitro, expl

162 Se accumulator species results in increased selenocysteine methyltransferase activity, but these mut

163 S. pinnata had higher selenocysteine methyltransferase protein levels and, jud

164 (Cys(59)/Cys(64)), and a C-terminal cysteine/selenocysteine motif (Cys(497)/Sec(498)).

165 er in their ability to transaminate methyl-L-selenocysteine (MSC) and L-selenomethionine (SM) to beta

166 with a targeted mutation of the active site selenocysteine of Gpx4 (Gpx4_U46S).

167 The C-terminal selenocysteine of TR1 was characterized as the primary a

168 omplete oxidation of the selenol function of selenocysteine or selenohomocysteine by dioxygen is achi

169 led facultative incorporation of selenium as selenocysteine or selenomethionine into proteins that la

170 ame UGA codons that can be decoded as either selenocysteine or termination codons.

171 depleted KIIIA[C1A,C2U,C9A,C15U] (where U is selenocysteine) or ddKIIIA were used.

172 n O-phosphoseryl-tRNA kinase involved in the selenocysteine pathway.

173 centage of ribosomes decoding a UGA codon as selenocysteine rather than termination can be increased

174 hat is characterized by up-regulation of UGA-selenocysteine recoding efficiency and relocalization of

175 ites on key metabolic proteins, including as selenocysteine-replacing cysteine at position 253 in unc

176 the electrophilic reactivity of an oxidized selenocysteine residue in polypeptides and proteins, and

177 electrophile resulting in alkylation of the selenocysteine residue in the active site of thioredoxin

178 blocked by auranofin and required an intact selenocysteine residue in TrxR1.

179 due to a Michael addition of the penultimate selenocysteine residue of TrxRs to the QMs.

180 to modify covalently the protein's catalytic selenocysteine residue, the discovery and mechanistic el

181 ve due to the fact that it contains multiple selenocysteine residues and has been postulated to act i

182 protein that in humans and mice contains 10 selenocysteine residues in its primary structure.

183 RNA (Sec tRNA) required for the insertion of selenocysteine residues into SPs during their translatio

184 t of site-specific incorporation of pairs of selenocysteine residues on oxidative folding and the fun

185 Selenocysteine residues were replaced mainly by cysteine

186 at Sepp1, with a potential for containing 10 selenocysteine residues, contained an average of 5 selen

187 and 168 amino acids, including a TGA-encoded selenocysteine, respectively.

188 ysteine, selenomethionine, and seleno-methyl-selenocysteine, respectively.

189 nt of the cysteine thiolate iron ligand by a selenocysteine results in UV-vis, EPR, and resonance Ram

190 Neither the C terminus selenocysteine-rich domain of Sepp1 nor ApoER2 was requi

191 elenomethylselenocysteine (Se-MetSeCys), and selenocysteine (Se-Cys) preconcentration.

192 f the electrophilic character of an oxidized selenocysteine (Se-S bond) to react with a nucleophilic

193 rough biomimetic chemical access to Se-allyl-selenocysteine (Seac), a metathesis-reactive amino acid

194 Selenocysteine (Sec or U) is encoded by UGA, a stop codo

195 Notably, mammalian H-TrxR contains a selenocysteine (Sec) and has wider substrate reactivity

196 ement that occurs in proteins in the form of selenocysteine (Sec) and in tRNAs in the form of selenou

197 p codons to the 21st non-standard amino acid selenocysteine (Sec) and plays a vital role in human hea

198 Selenocysteine (Sec) and pyrrolysine (Pyl) are rare amin

199 In addition, selenocysteine (Sec) and pyrrolysine (Pyl), known as the

200 ins are proteins that contain the amino acid selenocysteine (Sec) and the first release of the databa

201 Proteins containing the 21st amino acid selenocysteine (Sec) are present in the three domains of

202 The use of selenocysteine (Sec) as the 21st amino acid in the genet

203 Selenocysteine (Sec) biosynthesis in archaea and eukaryo

204 Recoding of UGA codons as selenocysteine (Sec) codons in selenoproteins depends on

205 We report the semisynthesis of a selenocysteine (Sec) derivative of the human copper chap

206 was originally developed as a masked form of selenocysteine (Sec) for the chemical synthesis of chall

207 expressed cytosolic region of VIMP where the selenocysteine (Sec) in position 188 is replaced with a

208 Selenocysteine (Sec) incorporation into selenoproteins r

209 Selenocysteine (Sec) incorporation is an essential proce

210 IS) element and UGA codon are sufficient for selenocysteine (Sec) insertion.

211 eins requires the decoding of a UGA codon as selenocysteine (Sec) instead of translation termination.

212 Selenocysteine (Sec) is found in the catalytic centers o

213 Selenocysteine (Sec) is incorporated at UGA codons in mR

214 Selenocysteine (Sec) is known as the 21st amino acid, a

215 Selenocysteine (Sec) is naturally co-translationally inc

216 In Archaea selenocysteine (Sec) is synthesized in three steps.

217 Selenocysteine (Sec) is the 21st genetically encoded ami

218 oreductase that contains the rare amino acid selenocysteine (Sec) on a C-terminal extension.

219 catalytic activity without the presence of a selenocysteine (Sec) residue (which is essential for the

220 n thioredoxin reductase (TR) contains a rare selenocysteine (Sec) residue in a conserved redox-active

221 n many life forms due to its occurrence as a selenocysteine (Sec) residue in selenoproteins.

222 xin, especially the presence or absence of a selenocysteine (Sec) residue in this tetrapeptide.

223 , which deiodinates TH inner rings through a selenocysteine (Sec) residue, revealed a thioredoxin-fol

224 s chemically programmed through a C-terminal selenocysteine (Sec) residue.

225 Selenocysteine (Sec) residues occur in thiol oxidoreduct

226 This Cys was synthesized by selenocysteine (Sec) synthase on tRNA([Ser]Sec) and its

227 Selenoproteins use the rare amino acid selenocysteine (Sec) to act as the first line of defense

228 inase (PSTK) is the key enzyme in recruiting selenocysteine (Sec) to the genetic code of archaea and

229 n was targeted for removal by disrupting the selenocysteine (Sec) tRNA([Ser]Sec) gene (trsp), and sel

230 Selenoproteins are proteins that incorporate selenocysteine (Sec), a nonstandard amino acid encoded b

231 Selenoproteins contain the amino acid selenocysteine (Sec), co-translationally inserted at a p

232 up of proteins containing a rare amino acid, selenocysteine (Sec), encoded by the codon, UGA.

233 ealth, is incorporated into some proteins as selenocysteine (Sec), generating a family of selenoprote

234 The 21st amino acid, selenocysteine (Sec), is incorporated translationally in

235 ecies; selenate (Se(VI)), Selenite (se(IV)), selenocysteine (SeC), Se-methylselenocysteine (SeMC) and

236 Selenocysteine (Sec), the 21(st) amino acid, is synthesi

237 ace element selenium is found in proteins as selenocysteine (Sec), the 21st amino acid to participate

238 ment, is incorporated into selenoproteins as selenocysteine (Sec), the 21st amino acid.

239 Selenium is incorporated into the amino acid selenocysteine (Sec), which in turn is inserted into sel

240 tive site in the form of the 21st amino acid selenocysteine (Sec), which is encoded by an in-frame UG

241 eneticin (G418) interfered with insertion of selenocysteine (Sec), which is encoded by the stop codon

242 Mammalian thioredoxin reductase (TR) is a selenocysteine (Sec)-containing homodimeric pyridine nuc

243 Selenocysteine (Sec)-decoding archaea and eukaryotes emp

244 on sequence (SECIS) element and requires the selenocysteine (Sec)-specific elongation factor, eEFSec,

245 The selenocysteine (Sec)-specific eukaryotic elongation fact

246 s are a diverse group of proteins containing selenocysteine (Sec)-the twenty-first amino acid-incorpo

247 e proteins containing an uncommon amino acid selenocysteine (Sec).

248 otein N incorporates selenium in the form of selenocysteine (Sec).

249 o encode the selenium containing amino acid, selenocysteine (Sec).

250 ynthesis via decomposition of the amino acid selenocysteine (Sec).

251 as also explored using the cysteine analogue selenocysteine (Sec).

252 osition of the dyad with the rare amino acid selenocysteine (Sec).

253 ows for UGA codons to specify the amino acid selenocysteine (Sec).

254 Selenocysteine (Sec, U) insertion into proteins is direc

255 organic forms selenomethionine (SeMet), and selenocysteine (SeCys2) was also examined, and the effec

256 ined were 7.37, 8.63, and 9.64 ug kg(-1) for selenocysteine, selenomethionine, and seleno-methyl-sele

257 sequence (SECIS) element, which recruits the selenocysteine specific elongation factor and tRNA(Sec)

258 ent study, fruit flies with knock-out of the selenocysteine-specific elongation factor were metabolic

259 oding efficiency and relocalization of SBP2, selenocysteine-specific elongation factor, and L30 recod

260 Ribosome profiling indicates that selenocysteine specification occurs with ~5% efficiency

261 product distribution in the reaction of the selenocysteine substituted enzyme reveals a gain in the

262 (selenoproteins) involves the interaction of selenocysteine synthase (SelA), tRNA (tRNA(Sec)), seleno

263 Selenocysteine synthase (SepSecS) catalyzes the terminal

264 t with kinetic behavior similar to bacterial selenocysteine synthase and the archaeal/eukaryotic SepS

265 In Bacteria, the selenocysteine synthase SelA converts Ser-tRNA(Sec), for

266 me P450 superfamily of enzymes, transfer RNA selenocysteine synthase, formiminotransferase cyclodeami

267 se that this complex is necessary for proper selenocysteine synthesis and may be involved in avoiding

268 that share the common feature of containing selenocysteine, the "twenty-first" amino acid.

269 Selenoproteins typically contain a single selenocysteine, the 21st amino acid, encoded by a contex

270 The synthesis of selenocysteine, the 21st amino acid, occurs on its trans

271 e resulting truncated SelK was shown to lack selenocysteine, the amino acid that defines selenoprotei

272 bited a sixfold higher capacity to methylate selenocysteine, thereby establishing the evolutionary re

273 ntrinsically disordered enzyme that utilizes selenocysteine to catalyze the reduction of disulfide bo

274 ylation of selenocysteine, and conversion of selenocysteine to elemental Se.

275 prokaryotes was also identified wherein the selenocysteine trait was largely a subset of the Mo trai

276 The D-stem of the selenocysteine tRNA (tRNA(Sec)) contains 2 additional ba

277 cursor in a series of reactions that require selenocysteine tRNA (tRNA(Sec)).

278 The selenocysteine tRNA (tRNASec) has a uniquely long D-stem

279 l cysteine tRNA with an 8/4 structure mimics selenocysteine tRNA and may function as opal suppressor.

280 Enhanced secondary structure in selenocysteine tRNA compensates for the absence of canon

281 element is recognized by SPH-binding factor/selenocysteine tRNA gene transcription activating factor

282 oters, including the U6 spliceosomal RNA and selenocysteine tRNA genes.

283 ll interfering RNA, selenium deficiency, and selenocysteine tRNA mutations; and was immunoprecipitate

284 nd histidine tRNAs, while minor cysteine and selenocysteine tRNA species may have a modified 8/4 stru

285 RNA(Ser)AGA, tRNA(Ser)CGA, tRNA(Ser)UGA, and selenocysteine tRNA with UCA (tRNA([Ser]Sec)UCA) contain

286 vels because of the expression of an altered selenocysteine-tRNA (i6A-) and mice that develop prostat

287 n factor (eEFSec) delivers the aminoacylated selenocysteine-tRNA (Sec-tRNA(Sec)) to the ribosome and

288 They were found during the search for selenocysteine tRNAs in terabytes of genome, metagenome

289 As to the ribosome, aside from initiator and selenocysteine tRNAs.

290 selenopeptides, which contain the amino acid selenocysteine (U, SeCys), were identified after tryptic

291 A link between Mo and selenocysteine utilization in prokaryotes was also ident

292 The truncated form of TR3 lacking selenocysteine was particularly efficient in binding Trx

293 Sec46Ala-Gpx4 mutant, in which the catalytic selenocysteine was replaced by a redox inactive alanine.

294 For the amino acids analysis, selenocysteine was the primary seleno-containing species

295 cing and uses of the non-standard amino acid selenocysteine were also identified.

296 Cellular selenocysteines, where sulfur is replaced with selenium,

297 of mammalian TR contains the rare amino acid selenocysteine, which is essential to its activity.

298 o-translational incorporation of selenium as selenocysteine, which play key roles in antioxidant defe

299 an suppress amber stop codons to incorporate selenocysteine with high efficiency.

300 lic arylboronic acid to provide the arylated selenocysteine within hours.