ライフサイエンスコーパス: methionine residue

1 ink from the Cbeta of the 2-vinyl group to a methionine residue.

2 bond, where the S is the sulfur atom of the methionine residue.

3 ding between a heme iron and the sulfur in a methionine residue.

4 y attaches to the terminal methyl group of a methionine residue.

5 s, which was attributed to the presence of a methionine residue.

6 10(-6) s, concomitant with heme binding of a methionine residue.

7 4 in the beta-subunit has been replaced by a methionine residue.

8 most of the protein retained the initiating methionine residue.

9 hile the remainder is missing the C-terminal methionine residue.

10 e native toxin, has an additional N-terminal methionine residue.

11 radical stabilized by an interaction with a methionine residue.

12 irst protein to exhibit automethylation at a methionine residue.

13 t tyrosine residue, which in turn links to a methionine residue.

14 ydrolyzes proteins on the C-terminal side of methionine residues.

15 aration, Pbp1 contains 24 similarly disposed methionine residues.

16 quence analysis, which showed four conserved methionine residues.

17 n of many proteins by reversing oxidation of methionine residues.

18 repeated with a penalty for the presence of methionine residues.

19 tions as well as their N-terminal initiating methionine residues.

20 tibility of each of alpha 1-antitrypsin's 10 methionine residues.

21 ding the reactivity of each of the protein's methionine residues.

22 nylalanine, tyrosine and tryptophan and 8.6% methionine residues.

23 and 3107.7 Da peptides, which identified the methionine residues.

24 le chain and lacks cysteine, tryptophan, and methionine residues.

25 on to the central iron atom by histidine and methionine residues.

26 sed free radicals which oxidized cysteine or methionine residues.

27 n approach in the identification of oxidized methionine residues.

28 Hypothiocyanite does not react with methionine residues.

29 loss of the antioxidant defense provided by methionine residues.

30 peptide were identified at the histidine and methionine residues.

31 ptide cleavages, and cleavages of N-terminal methionine residues.

32 ion upstream of the anchoring (histidine or methionine) residue.

33 Methionine residue 13 in TPN interacts with residue F148

34 e previously reported CaMKII mutant in which methionine residues 281 and 282 were mutated to valine (

35 eductase A (MSRA), which can reduce oxidized methionine residues, acts as a suppressor of pancreatic

36 icantly enhanced by a second mutation of the methionine residue adjacent to the active site tyrosine.

37 so characterized were oxidation of all three methionine residues, alpha-Met-32, alpha-Met-76, and bet

38 MS analysis identified oxidation of the same methionine residue and deamidation of the same asparagin

39 o group of proteins containing an N-terminal methionine residue and is essential for proper sister ch

40 e previously described loss of the initiator methionine residue and N-terminal acetylation.

41 quivocally the functional importance of this methionine residue and that it is unique among the aliph

42 formation of a covalent linkage between the methionine residue and the heme vinyl group in S160M(G).

43 he N terminus, which includes the N-terminal methionine residue and the proteinase P21 cleavage site,

44 me iron and the intrinsic sulfur ligand of a methionine residue and to enhance the peroxidatic proper

45 efficiently despite the presence of protein methionine residues and can distinguish between differen

46 yme that catalyzes the reduction of oxidized methionine residues and has protein repair function, in

47 rated into the Shaker Kv channel in place of methionine residues and modified with azide-reactive alk

48 (2)O(2) exhibits significantly more oxidized methionine residues and shows a lower degree of reversib

49 als maintain a system for repair of oxidized methionine residues and that this function is tuned in e

50 ed between the oxidation of the conserved Fc methionine residues and the loss of neonatal Fc receptor

51 of patients with ALI contained both oxidized methionine residues and the stalk region.

52 roteins bearing the Nt-acetylated N-terminal methionine residue are substrates of the Ac/N-end rule p

53 wide evidence that oxidation rates of buried methionine residues are also strongly influenced by the

54 These two methionine residues are located in a highly conserved re

55 The two methionine residues are located on the same face of the

56 In contrast, the specific functions of methionine residues are not known.

57 on of tyrosine residues and the oxidation of methionine residues are oppositely directed by the prese

58 the peptide, an oxidized form in which both methionine residues are oxidized to methionine sulfoxide

59 We show that in vitro, N-terminal methionine residues are particularly prone to chemical o

60 Although free and protein-bound methionine residues are particularly sensitive to oxidat

61 Methionine residues are particularly susceptible to oxid

62 go reversible methionine oxidation, in which methionine residues are posttranslationally oxidized to

63 Here, we show that the Pbp1 methionine residues are sensitive to hydrogen peroxide (

64 at alpha-Tyr-42, and oxidation at the three methionine residues are significantly higher in diabetic

65 at alpha-Tyr-42, and oxidation at the three methionine residues are significantly higher in the nons

66 As more and more methionine residues are substituted into the protein, th

67 reductase (MsrA) repairs oxidative damage to methionine residues arising from reactive oxygen species

68 the hydrogen peroxide-mediated oxidation of methionine residues as a function of the chemical denatu

69 le to distinguish between exposed and buried methionine residues, as significant portions of all five

70 We demonstrate that a methionine residue at position 16 of GolS, absolutely co

71 Mutation of the methionine residue at position 475 in the beta subunit t

72 Substitution of a methionine residue at position 79 in poliovirus protein

73 o steric clashes of vardenafil with a single methionine residue at position 806 in mouse PDE5A.

74 Through this analysis, a methionine residue at the junction of the amino-terminal

75 s a covalent link with the methyl group of a methionine residue at the peptide binding site.

76 Mutational analysis demonstrates that the methionine residue at this position has a unique combina

77 Human G6Pase contains five methionine residues at positions 1, 5, 121, 130, and 279

78 es demonstrate that an ensemble of conserved methionine residues at the cytoplasmic side of the T3SS

79 have been individually mutated to alanine or methionine residues at the nine sequence positions that

80 is particularly exposed to oxidation of its methionine residues, both in vivo and in vitro Oxidative

81 ially still allow initiation at a downstream methionine residue but we showed that this would not res

82 the alkylation also induces a conversion of methionine residues, but to the iso-threonine form.

83 idues, we measured the rates of oxidation of methionine residues by H(2)O(2) in granulocyte colony-st

84 ny proteins due to the oxidation of critical methionine residues by reducing methionine sulfoxide, Me

85 the formyl group must be removed before the methionine residue can be cleaved by methionine aminopep

86 These results demonstrate that methionine residues can act as reversible redox switches

87 case of CNBr digests, for example, modified methionine residues can be limited to occur only at the

88 mechanism of formation, we have engineered a methionine residue close to the 2-vinyl group in recombi

89 RGS2 contains four methionine residues close to the N terminus that can act

90 general belief, the unusually high number of methionine residues clustered outside the predicted heli

91 pts, based on the presence of the initiating methionine residue codon.

92 Methionine residues competitively take oxygen from H(2)O

93 Idelta gene to eliminate oxidation-sensitive methionine residues confers protection from ischemia/rep

94 We propose that methionine residues constitute an important antioxidant

95 Eight of the 16 methionine residues could be oxidized with little effect

96 rm methionine sulfoxide, and surface exposed methionine residues create an extremely high concentrati

97 The six methionine residues distributed throughout the enzyme pr

98 The results indicate that these methionine residues do not play a pivotal role in cataly

99 ity of a protein site, of the sulfur atom of methionine residues does not correlate well with the rat

100 the bioisosteric replacement of the original methionine residue due to its susceptibility to oxidatio

101 I-Bpa1-PTH-(1-34) conjugate suggested that a methionine residue (either Met414 or Met425) within the

102 and separate domains of the protein with its methionine residues enriched with (13)C to probe its qua

103 ne; NatE requires a substrate amino-terminal methionine residue for activity.

104 peptidase (MetAP) removes the amino-terminal methionine residue from newly synthesized proteins, and

105 is DNA binding, which protects the protein's methionine residues from oxidation both in vitro and in

106 oordination with the axial ligands being two methionine residues from the same Shp molecule.

107 ylalanine residues (G/F) and another rich in methionine residues (G/M), is critical for prion mainten

108 e two complementary determining region (CDR) methionine residues had little or no impact on antigen b

109 in the inhibitor-binding site with a bulkier methionine residue (Hck-T338M).

110 an mutant GABAA receptors expressing the RDL methionine residue (i.e. alpha6beta3N289Mgamma2L) were p

111 We show here that oxidation of a methionine residue in a voltage-dependent potassium chan

112 Because a single methionine residue in apoA-I, Met-148, resides near the

113 e found that, in human cells, the initiating methionine residue in DDB2 was removed and that the N-te

114 ditional amino acids on the N terminus and a methionine residue in place of the native leucine residu

115 Mutation of the methionine residue in the conserved YMDD motif of the HT

116 nt further highlight the central role of the methionine residue in the enzyme mechanism.

117 We have previously identified a conserved methionine residue in the fourth membrane-associated dom

118 ive in the two peptides; however, the single methionine residue in the peptides appears to play a cru

119 Mutations of a methionine residue in the sugar phosphate binding site p

120 The methionine residue in TPN can be oxidized by air, which

121 VP1-Ser274, which is located N terminal to a methionine residue in VP1-2A.

122 The extent to which methionine residues in a protein are oxidized after spec

123 BHP should be useful for identifying surface methionine residues in a protein of unknown structure an

124 Two methionine residues in actin are specifically converted

125 ously established that oxidation of all four methionine residues in alpha-synuclein (to the sulfoxide

126 Methionine residues in alpha/beta-type small, acid-solub

127 We detect increased oxidation of Sup35 methionine residues in antioxidant mutants and show that

128 und to correspond linearly with oxidation of methionine residues in bacterial cytosolic and inner mem

129 The oxidation of methionine residues in both proteins and in the tripepti

130 Oxidation of methionine residues in calmodulin (CaM) lowers the affin

131 Oxidation of methionine residues in CaM resulted in significant pertu

132 Oxidation of methionine residues in CaM-DA produced a substantial inc

133 d in the specific oxidation and reduction of methionine residues in cellular signalling proteins, whi

134 es, including a high content of aromatic and methionine residues in disordered N-terminal extensions.

135 hypothesis directly, we replaced 40% of the methionine residues in Escherichia coli with norleucine,

136 e computed free energies of the oxidation of methionine residues in G-CSF indicate that the protein e

137 implicate oxidation of specific tyrosine and methionine residues in impairing the ABCA1 transport act

138 dox state via reversible oxidation of tandem methionine residues in its regulatory domain.

139 e Copper(I)-Nitrene Platform allows labeling methionine residues in live cancer cells, observing mini

140 esidues, as significant portions of all five methionine residues in native rIFN-gamma were oxidized b

141 sed to hydrolyze peptide bonds C-terminal to methionine residues in peptides and proteins.

142 as well as oxidation of free methionine and methionine residues in peptides and proteins.

143 o suggesting an essential role for aliphatic methionine residues in promoting single-chain compaction

144 ch high concentrations of H(2)O(2) oxidize L-methionine residues in proteins and peptides to (R and S

145 Methionine residues in proteins are susceptible to oxida

146 Methionine residues in proteins are susceptible to oxida

147 Oxidized forms of methionine residues in proteins can be repaired by methi

148 ing hydrogen peroxide to selectively oxidize methionine residues in proteins in order to probe the so

149 tochondrial dysfunction through oxidation of methionine residues in proteins located in different cel

150 f reactive oxygen species react readily with methionine residues in proteins to form methionine sulfo

151 The results showed that two of the five methionine residues in rIFN-gamma were susceptible to ox

152 Thus, the cyclic oxidation and reduction of methionine residues in STARD3 provides a catalytically e

153 ain in response to oxidative modification of methionine residues in the carboxyl-terminal domain.

154 revious work has shown that converting three methionine residues in the cytochrome c peroxidase (CcP)

155 ent interactions involving phenylalanine and methionine residues in the disordered flanking regions c

156 site of this oxidation to a cluster of three methionine residues in the Fes1 core domain.

157 We show that a series of clustered methionine residues in the hydrophilic extracellular dom

158 n together, these data demonstrate that both methionine residues in the LINGO2 tail mediate the effec

159 Using mass spectrometry, methionine residues in the Met-rich central region of Ss

160 The replacement of three methionine residues in the native enzyme with selenometh

161 site is located between the third and fourth methionine residues in the ORF, predicting a primary ami

162 en mammalian 15- and 12-lipoxygenases, three methionine residues in the porcine leukocyte 12-lipoxyge

163 ies and globally measured oxidation rates of methionine residues in the presence and absence of terti

164 e, we have identified two strictly conserved methionine residues in the PRMT1 active site that are no

165 kably similar to the arrangements around the methionine residues in the protein.

166 s mimicking specific regions of the reactive methionine residues in the protein.

167 sly reported mechanism involves oxidation of methionine residues in the regulatory domain.

168 -endorphin in vitiligo owing to oxidation of methionine residues in the sequences of these peptides.

169 Methionine residues in the structure of proteins and pep

170 Seven other methionine residues in the VWF A1A2A3 region (containing

171 s that result from oxidative modification of methionine residues in wheat germ calmodulin (CaM), and

172 jugates, and identification of hyperreactive methionine residues in whole proteomes.

173 eral other proteins with oxidation-sensitive methionine residues, including apolipoprotein A-I, throm

174 a series of phage T4 lysozymes with up to 14 methionine residues incorporated within the protein has

175 lecular dynamics simulations reveal that the methionine residue increases flexibility within the ZU5

176 Importantly, methionine residues inhibit chlorination, indicating tha

177 ion also indicate that the side chain of the methionine residue interacts less strongly with the meta

178 utated to convert the invariant sixth ligand methionine residue into histidine, creating the site-spe

179 We show here that the N-terminal methionine residue is cleaved from the mature protein.

180 mbers of the annexin family of proteins, the methionine residue is conserved only in three plant prot

181 cterial topoisomerase I enzymes, a conserved methionine residue is found at the active site next to t

182 tance of about 5.5 A, the sulfur atom of the methionine residue is in their close vicinity and appare

183 and off of the factor's interaction with the methionine residue is likely to play an important role i

184 When this methionine residue is oxidized to methionine sulfoxide,

185 ive of honey bee toxin tertiapin (TPN) whose methionine residue is replaced with a glutamine residue.

186 Reduction of oxidized methionine residues is catalyzed by methionine sulfoxide

187 2, pH 7.4, nitration occurs but oxidation of methionine residues is inhibited.

188 Oxidation of methionine residues is involved in several biochemical p

189 strategy to assign the methyl resonances of methionine residues is presented.

190 Because oxidation of methionine residues is reversible, this covalent modific

191 revealing an N-terminal helical segment with methionine residues juxtaposed for Cu(I) ligation and a

192 icated that replacing valine with the larger methionine residue led to greater solvent exposure of re

193 Substitution of a methionine residue located in the P-segment of the chann

194 the active site of the SET domain, with the methionine residue located in the pocket that normally a

195 does not depend on any of the three in-frame methionine residues located at the beginning of CM2 ORF.

196 e in having a sequence rich in histidine and methionine residues located on the lumenal side of the m

197 ocated at CD4 residue 405 or of arginine and methionine residues located, respectively, at residue 40

198 f AQP4 result from translation initiation at methionine residues M1 and M23, but no functional differ

199 ypes of transcripts initiates at a conserved methionine residue, M1727, which lies within the Notch1

200 sidue in the editing site, Cys666, and three methionine residues (M217 in the active site, M658 in th

201 loss results in the selective oxidation of a methionine residue (M239) in pyruvate kinase M2 (PKM2).

202 xtracellular loop of SaeS, we discovered one methionine residue (M31) was essential for the ability o

203 Replacement of the noncanonical methionine residue M584 (Walker B sequence of nucleotide

204 repaired by DTT suggests that a cysteine or methionine residue may be involved.

205 Thus, methionine residues may act as catalytic antioxidants, p

206 We have identified a methionine residue (Met(823)) in the M4 domain of the NR

207 with copper or mutational replacement of two methionine residues (Met-44 and Met-64) that are present

208 The Fc region has two highly conserved methionine residues, Met 33 (C(H)3 domain) and Met 209 (

209 ne residue Cys4 with the alpha-carbon of the methionine residue Met12.

210 cholesterol hydroperoxides and that its two methionine residues, Met307 and Met427, could be oxidize

211 A series of mutations was targeted at the methionine residue, Met471, coordinating the Cu(M) site

212 ormone [hPTH(1-34)] and the oxidation of its methionine residues, Met8 and Met18, by hydrogen peroxid

213 [(13)C(e)H(3)]Methionine residues near the microswitches exhibited dis

214 AT contains two adjacent methionine residues near the reactive site loop cleaved

215 nce alpha/beta-type SASP containing oxidized methionine residues no longer bind DNA well and alpha/be

216 itions -22, -24, -26, -36, and -38 using the methionine residue normally used to initiate the 18-kDa

217 The structure reveals a methionine residue of one MsrA molecule bound at the act

218 The methionine residue of one of the peptides had been oxidi

219 We discovered that keeping the N-terminal methionine residue of one subunit of the streptavidin ho

220 site and in the recognition site for the +3 methionine residue of the peptide, the side chain of whi

221 sence of DOPAC leads to the oxidation of the methionine residues of alpha-Syn, probably due to the H(

222 HP and H2O2 caused some oxidation of the two methionine residues of an alpha/beta-type SASP (SspC) in

223 Oxidative modification of methionine residues of CaM to their corresponding sulfox

224 rophils use myeloperoxidase (MPO) to convert methionine residues of ingested Escherichia coli to meth

225 ion of tyrosine residues or the oxidation of methionine residues of metabolically regulated proteins

226 ciably to carbonyl formation or oxidation of methionine residues of proteins at physiological pH and

227 Three methionine residues of the chemokine were identified by

228 The 9 methionine residues of vertebrate calmodulin (CaM) were

229 Post-translational redox modification of methionine residues often triggers a change in protein f

230 This positive interaction with the methionine residue on the tRNA may serve to ensure that

231 lorous acid preferentially oxidizes specific methionine residues on the alpha, beta, and gamma chains

232 The enzyme contains seven methionine residues, one of which is at the amino termin

233 selectivity, as the necessary combination of methionine residues only occurs in 9.3% of human kinases

234 can occur cotranslationally on the initiator methionine residue or on the penultimate residue if the

235 solvent-accessible surface areas (SASAs) of methionine residues (Pearson's r = 0.78, p < 0.0001) and

236 The reductive repair of oxidized methionine residues performed by methionine sulfoxide re

237 Wild-type lysozyme contains two fully buried methionine residues plus three more on the surface.

238 Oxidizing two native methionine residues predominantly populates the denature

239 , together with the accompanied oxidation of methionine residue, presents a significant challenge to

240 tochrome b562 containing the H102M mutation, methionine residues provide both axial ligands to the he

241 osed of the catalytic histidine and a nearby methionine residue, rather than the catalytic histidine

242 rotein and determined the position of [(35)S]methionine residues released by Edman degradation reacti

243 , HS12_Yeast (11.6 kDa), with the initiating methionine residue removed.

244 -type cytochromes in which a histidine and a methionine residue serve as the axial ligands to the hem

245 age in vivo may be of singular importance if methionine residues serve as antioxidants.

246 dition, unprocessed actin with an N-terminal methionine residue shows very different effects on formi

247 n vitro, the addition of a single N-terminal methionine residue significantly enhanced the fibrillati

248 es of backbone hydrogen bonds with the first methionine residue specified through multiple van der Wa

249 ation was unequivocally determined to be the methionine residue, suggesting that the oxidation of hem

250 w that oxidation of paired regulatory domain methionine residues sustains CaMKII activity in the abse

251 Key to proton permeation is a methionine residue that interrupts the series of regular

252 is a significant reduction in the number of methionine residues that are conserved in CaM and CaBP1

253 The conserved methionine residues that are essential for Ctr1 function

254 We found that replacements of several methionine residues that are essential for hCtr1-mediate

255 in extracellular fluids contain cysteine and methionine residues that are subject to oxidation.

256 itches, which consist of protein cysteine or methionine residues that become transiently oxidized whe

257 R-DBD contains several strategically located methionine residues, they are less susceptible to oxidat

258 , while 3 of 50 were mutations of the native methionine residue to isoleucine (M499I).

259 e demonstrate that addition of an N-terminal methionine residue to SDF-1beta (Met-SDF-1beta) results

260 The conversion of these methionine residues to cysteine, by site-directed mutage

261 Mutations of three of these methionine residues to isoleucine resulted in significan

262 ome tyrosine residues and conversion of some methionine residues to methionine sulfoxide (MSOX) resid

263 active carbonyl content and to conversion of methionine residues to methionine sulfoxide residues.

264 Reactive oxygen species oxidize methionine residues to methionine sulfoxide, and the met

265 elicited by the oxidation of surface-exposed methionine residues to methionine sulfoxide.

266 to catalyze the reverse reaction, oxidizing methionine residues to methionine sulfoxide.

267 e been shown to impact the susceptibility of methionine residues to oxidation.

268 We report evidence that one or more methionine residues undergo a structural change during t

269 and SNRNP27K orthologs, or a single SNRNP27K methionine residue, was associated with a preference for

270 valine of the alpha chains is preceded by a methionine residue, was prepared by the same procedure.

271 a protein molecule and the oxidation of its methionine residues, we measured the rates of oxidation

272 tween rhTRAIL(WT) and rhTRAIL(4C7) contained methionine residues, we oxidized these quantitatively to

273 The oxidized methionine residues were found to be in the sulfoxide [M

274 The oxidizable methionine residues were found to be relatively surface

275 a native protein with TBHP only the exposed methionine residues were oxidized.

276 gG monoclonal antibodies (mAbs) contains two methionine residues which are susceptible to oxidation.

277 amino acid structure, starting at the fourth methionine residue, which includes a possible signal pep

278 -terminal domain (NTD) rich in histidine and methionine residues, which are commonly associated with

279 the second shell generally contains multiple methionine residues, which are elements of a statistical

280 been utilized to profile oxidation-sensitive methionine residues, which might increase our understand

281 on, except for the terminal methyl groups of methionine residues, which required rotational optimizat

282 Substitution of this methionine residue with arginine in recombinant Yersinia

283 The substitution of these methionine residues with selenomethionine slightly stabi

284 we present a straightforward method to label methionine residues with specific (13)CHD(2) methyl isot

285 The axial binding reactions of histidine and methionine residues with the Fe(II) heme cofactor were m

286 introduced into proteins upon replacement of methionine residues with the non-canonical amino acid az

287 port a preliminary analysis of (methyl- d 3) methionine residues within dihydrofolate reductase.

288 ulfoxide reductase A (MsrA) repairs oxidized methionine residues within proteins and may also functio

289 of peptide side-chains to yield non-natural methionine residues within small peptides.

290 Methionine residues within the kinase domain of Src serv

291 , which is mediated by 2 oxidation-sensitive methionine residues within the regulatory domain.