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

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

5 10(-6) s, concomitant with heme binding of a methionine residue.

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

7 radical stabilized by an interaction with a methionine residue.

8 4 in the beta-subunit has been replaced by a methionine residue.

9 most of the protein retained the initiating methionine residue.

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

11 irst protein to exhibit automethylation at a methionine residue.

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

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

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

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

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

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

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

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

20 n approach in the identification of oxidized methionine residues.

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

22 Hypothiocyanite does not react with methionine residues.

23 loss of the antioxidant defense provided by methionine residues.

24 peptide were identified at the histidine and methionine residues.

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

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

27 quence analysis, which showed four conserved methionine residues.

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

29 Methionine residue 13 in TPN interacts with residue F148

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

51 Methionine residues are particularly susceptible to oxid

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

74 We propose that methionine residues constitute an important antioxidant

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

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

77 The six methionine residues distributed throughout the enzyme pr

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

103 Two methionine residues in actin are specifically converted

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

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

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

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

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

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

110 Oxidation of methionine residues in CaM resulted in significant pertu

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

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

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

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

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

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

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

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

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

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

121 Methionine residues in proteins are susceptible to oxida

122 Methionine residues in proteins are susceptible to oxida

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

139 Methionine residues in the structure of proteins and pep

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

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

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

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

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

145 Importantly, methionine residues inhibit chlorination, indicating tha

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

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

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

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

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

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

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

153 When this methionine residue is oxidized to methionine sulfoxide,

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

155 Reduction of oxidized methionine residues is catalyzed by methionine sulfoxide

156 2, pH 7.4, nitration occurs but oxidation of methionine residues is inhibited.

157 Oxidation of methionine residues is involved in several biochemical p

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

191 Three methionine residues of the chemokine were identified by

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

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

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

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

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

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

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

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

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

201 Oxidizing two native methionine residues predominantly populates the denature

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

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

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

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

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

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

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

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

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

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

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

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

214 The conserved methionine residues that are essential for Ctr1 function

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

231 The oxidizable methionine residues were found to be relatively surface

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

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

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

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

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

237 Substitution of this methionine residue with arginine in recombinant Yersinia

238 The substitution of these methionine residues with selenomethionine slightly stabi

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

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

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

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

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