ライフサイエンスコーパス: methionine sulfoxide

1 ynureninyl products as well as betaMet-55 to methionine sulfoxide.

2 elding both the (R) and (S) diastereomers of methionine sulfoxide.

3 non-polar methionine to the more hydrophilic methionine sulfoxide.

4 ected SO band at 1025 cm-1 characteristic of methionine sulfoxide.

5 of one of the peptides had been oxidized to methionine sulfoxide.

6 residues are posttranslationally oxidized to methionine sulfoxide.

7 could not grow, in the presence of H2O2 and methionine sulfoxide.

8 yeast strain could grow on either form of L-methionine sulfoxide.

9 eferentially targeted, forming predominantly methionine sulfoxide.

10 on of surface-exposed methionine residues to methionine sulfoxide.

11 HypT is activated by methionine oxidation to methionine sulfoxide.

12 e reaction, oxidizing methionine residues to methionine sulfoxide.

13 ic oxidation and reduction of methionine and methionine sulfoxide.

14 thionine and is specific for the S epimer of methionine sulfoxide.

15 rrelated and also correlated positively with methionine sulfoxide.

16 ic oxidation and reduction of methionine and methionine sulfoxide.

17 ndogenous methionines to their corresponding methionine sulfoxides.

18 ated CaMox, which varies from three to eight methionine sulfoxides.

19 multiple methionines to their corresponding methionine sulfoxides.

20 r/MsrA mutant could not grow on a mixture of methionine sulfoxides.

21 olysis of methionine gives rise primarily to methionine sulfoxide (+16 Da mass shift); this can be fu

22 ich both methionine residues are oxidized to methionine sulfoxide and a control peptide consisting of

23 e msrA gene increases free and protein-bound methionine sulfoxide and decreases cell viability.

24 correlated with an increase in the levels of methionine sulfoxide and dityrosine.

25 rew better, had lower free and protein-bound methionine sulfoxide and had a better survival rate unde

26 al oxidative protein modifications involving methionine sulfoxide and nitrotyrosine.

27 shed through mass spectrometric detection of methionine sulfoxide and the reactivation of a significa

28 HOCl can oxidize methionine to methionine sulfoxide and tyrosine to chlorotyrosine.

29 amino acid methionine is readily oxidized to methionine sulfoxide, and its reduction is catalyzed by

30 malondialdehyde, protein carbonyls, protein methionine sulfoxide, and oxidized glutathione as well a

31 on of microcystins containing methionine and methionine sulfoxide, and reveals the oxidation state of

32 idants react readily with methionine to form methionine sulfoxide, and surface exposed methionine res

33 n spectroscopy reveals the presence of H2O2, methionine sulfoxide, and tryptophan metabolites; i.e.,

34 We show that ortho-tyrosine and methionine sulfoxide are formed in concert with Nepsilon

35 eir corresponding oxidized forms cystine and methionine sulfoxide are presented.

36 This suggests that microcystins containing methionine sulfoxide are primarily postextraction oxidat

37 ereospecific methionine oxidase, producing S-methionine sulfoxide as its product.

38 to its facile oxidation via the formation of methionine sulfoxide, as shown by mass spectrometry.

39 is demonstrated that oxidation of Met-148 to methionine sulfoxide associated quantitatively with loss

40 the effects of oxidative damage by reducing methionine sulfoxide back to methionine and recovering p

41 oxidized methionine in proteins by reducing methionine sulfoxide back to methionine.

42 atalyze a thioredoxin-dependent reduction of methionine sulfoxide back to methionine.

43 he presence of Sec improves the reduction of methionine sulfoxide by MsrAs.

44 n be repaired via reduction of the resulting methionine sulfoxides by methionine-S-sulfoxide reductas

45 susceptible to oxidation, and the resulting methionine sulfoxides can be reduced back to methionines

46 oxidized proteins and MsrA, which reduces S-methionine sulfoxide, can protect lens cells against oxi

47 s are particularly sensitive to oxidation to methionine sulfoxide derivatives, these oxidations are r

48 sidues in proteins and peptides to (R and S)-methionine sulfoxide diasteriomers.

49 ification of methionine to the corresponding methionine sulfoxide does not predispose CaM to further

50 n was through the oxidation of methionine to methionine sulfoxide, established through mass spectrome

51 ctivate the PM Ca-ATPase results solely from methionine sulfoxide formation and (ii) MsrA can repair

52 e roles of MsrB1, -B2 and -B3 which reduce R-methionine sulfoxide have not been established for any m

53 Substitution of methionine with methionine sulfoxide in a medium lacking hydrogen peroxi

54 ctional domains of ADAMTS13 were oxidized to methionine sulfoxide in an HOCl concentration-dependent

55 ine residues of ingested Escherichia coli to methionine sulfoxide in high yield.

56 , except that the myristoylated form reduced methionine sulfoxide in protein much faster than the non

57 e discuss how the oxidation of methionine to methionine sulfoxide in signalling proteins such as ion

58 -Raman Spectroscopy revealed the presence of methionine sulfoxide in the depigmented skin of patients

59 of Bacillus species were readily oxidized to methionine sulfoxide in vitro by t-butyl hydroperoxide (

60 hat MsrA is responsible for the reduction of methionine sulfoxide in vivo as well as in vitro in euka

61 Repair of selected methionine sulfoxides in CaMox by MsrA results in a part

62 Oxidation of methionine to methionine sulfoxide is a common form of damage observed

63 Oxidation of methionine to methionine sulfoxide is a major oxidative stress product

64 However, no single methionine sulfoxide is completely repaired in all CaM o

65 The oxidation of methionine in proteins to methionine sulfoxide is implicated in aging as well as i

66 lysis by reducing agents such as TCEP, while methionine sulfoxide is refractory to reduction by this

67 gments of CaMox vary by a factor of 2, where methionine sulfoxides located within hydrophobic sequenc

68 that oxidation of the Met-35 side chain to a methionine sulfoxide (Met-35(ox)) significantly hinders

69 ctase (MsrA; EC ) catalyzes the reduction of methionine sulfoxide (Met-O) in proteins to methionine (

70 lot in association with a functional loss of methionine sulfoxide (Met-S=O) repair in the entire gray

71 An enzyme that reduces methionine sulfoxide [Met(O)] residues in proteins [pept

72 epair enzyme that catalyzes the reduction of methionine sulfoxide [Met(O)] residues in proteins to me

73 ling, and their reversible oxidation to form methionine sulfoxides [Met(O)] in calmodulin (CaM) and o

74 of critical methionine residues by reducing methionine sulfoxide, Met(O), to methionine.

75 The reduction of methionine sulfoxide (MetO) is mediated by methionine su

76 Mammals contain two methionine sulfoxide (MetO) reductases, MsrA and MsrB, t

77 Reduction of methionine sulfoxide (MetO) residues in proteins is cata

78 These latter small peptides are enriched in methionine sulfoxides (MetO), suggesting a preferential

79 e oxygen species (ROS) oxidize methionine to methionine sulfoxide (MetSO) and thereby inactivate prot

80 e oxygen species (ROS) oxidize methionine to methionine sulfoxide (MetSO) and thereby inactivate prot

81 ve developed a new technique for quantifying methionine sulfoxide (MetSO) in protein to assess levels

82 ROS oxidize methionine to methionine sulfoxide (MetSO), rendering several proteins

83 ies that reduce the S and R stereoisomers of methionine sulfoxide (MetSO), respectively, and together

84 es, which is illustrated in the synthesis of methionine sulfoxide (MSO).

85 nd conversion of some methionine residues to methionine sulfoxide (MSOX) residues.

86 tified the major metabolite, 3-nitrotyrosine-methionine-sulfoxide (NSO)-MENK, using liquid chromatogr

87 mmunosuppressive activity than their reduced methionine sulfoxide peptide forms 4 and 6, respectively

88 loped a sensitive method of quantitating the methionine sulfoxide present at position 213 (MetSO213)

89 r Met(146) in wheat germ calmodulin (CaM) to methionine sulfoxide prevents the CaM-dependent activati

90 commentary shows that both diastereomers of methionine sulfoxide (R and S) can be repaired in the hu

91 rves as an excellent model for protein-bound methionine sulfoxide recognition and repair.

92 these genes are fused to form a bifunctional methionine sulfoxide reductase (i.e., MsrBA) enzyme.

93 enerally accepted, primarily from studies on methionine sulfoxide reductase (Msr) A, that the biologi

94 The methionine sulfoxide reductase (MSR) enzyme converts Met

95 Methionine sulfoxide reductase (MSR) enzyme converts Met

96 The role of methionine sulfoxide reductase (Msr), a methionine repai

97 Met5 of alphaS are excellent substrates for methionine sulfoxide reductase (Msr), thereby providing

98 Met sulfoxide can be repaired back to Met by methionine sulfoxide reductase (Msr).

99 Peptide methionine sulfoxide reductase (MsrA) repairs oxidative

100 Peptide methionine sulfoxide reductase (MsrA) reverses oxidative

101 We have investigated the ability of methionine sulfoxide reductase (MsrA) to maintain optima

102 A gene homologous to methionine sulfoxide reductase (msrA) was identified as

103 The yeast peptide-methionine sulfoxide reductase (MsrA) was overexpressed

104 ty with the carboxyl terminus of the peptide-methionine sulfoxide reductase (MsrA), a repair enzyme,

105 We report that peptide methionine sulfoxide reductase (MsrA), a repair enzyme,

106 ted by an unrelated protein known as peptide methionine sulfoxide reductase (MsrA), an antioxidant re

107 an mutants in cytochrome c peroxidase (ccp), methionine sulfoxide reductase (msrA), or the metal-bind

108 oxidized alpha/beta-type SASP with peptidyl methionine sulfoxide reductase (MsrA), which can reduce

109 ly matches that of only one protein, peptide methionine sulfoxide reductase (MsrA).

110 ations are readily repaired by the action of methionine sulfoxide reductase (MsrA).

111 Peptide methionine sulfoxide reductase (MsrA; EC ) catalyzes the

112 Peptide methionine sulfoxide reductase (MsrA; EC ) reverses the

113 Peptide methionine sulfoxide reductase (MsrA; EC 1.8.4.6) is a u

114 Peptide methionine sulfoxide reductase (PMSR) is a ubiquitous en

115 ild-type plants and a mutant lacking peptide methionine sulfoxide reductase (pmsr2-1) showed increase

116 hesin (one UGA) of Mycoplasma pneumoniae and methionine sulfoxide reductase (two UGAs) of Mycoplasma

117 thione peroxidase, ascorbate peroxidase, and methionine sulfoxide reductase 2) are slightly up-regula

118 cardial CaMKII inhibition, overexpression of methionine sulfoxide reductase A (an enzyme that reduces

119 The enzyme peptide methionine sulfoxide reductase A (MSRA) catalyzes the re

120 Methionine sulfoxide reductase A (MsrA) catalyzes the re

121 Methionine sulfoxide reductase A (MsrA) is an antioxidan

122 Methionine sulfoxide reductase A (MsrA) is an enzyme inv

123 Methionine sulfoxide reductase A (MsrA) maintains the fu

124 Methionine sulfoxide reductase A (MsrA) repairs oxidized

125 that a mutant form of M. genitalium lacking methionine sulfoxide reductase A (MsrA), an antioxidant

126 CaMKII oxidation is reversed by methionine sulfoxide reductase A (MsrA), and MsrA-/- mic

127 n that can be reversed through the action of methionine sulfoxide reductase A (MsrA), which is implic

128 n-like domain (NT domain) is fused to tandem methionine sulfoxide reductase A and B domains (MsrA/B).

129 r, we demonstrate almost absent catalase and methionine sulfoxide reductase A and B protein expressio

130 horesis (CE) method for the determination of methionine sulfoxide reductase A and methionine sulfoxid

131 Methionine sulfoxide reductase A is an essential enzyme

132 Methionine sulfoxide reductase A is an essential enzyme

133 Lipidation of methionine sulfoxide reductase A occurs in the mouse, in

134 have unraveled the redox relay mechanisms of methionine sulfoxide reductase A of the pathogen Coryneb

135 quinone reductase, glutathione reductase and methionine sulfoxide reductase A proteins were significa

136 xpressions of only glutathione reductase and methionine sulfoxide reductase A proteins were significa

137 ecies signaling by targeting the antioxidant methionine sulfoxide reductase A to modulate liposarcoma

138 dium-restricted transgenic overexpression of methionine sulfoxide reductase A, an enzyme that reduces

139 dants superoxide dismutase (SOD2), catalase, methionine sulfoxide reductase A, and the 20S proteasome

140 ysine residues of diverse targets, including methionine sulfoxide reductase A, myosin light chain kin

141 whereas over-expression of a repair enzyme, methionine sulfoxide reductase A, rendered them resistan

142 of myristoylated and nonmyristoylated mouse methionine sulfoxide reductase A.

143 ained by uniform selenium deficiency because methionine sulfoxide reductase activities were similar i

144 tion of methionine sulfoxide reductase A and methionine sulfoxide reductase B activities in mouse liv

145 fraction of inactivated GroEL by the enzyme methionine sulfoxide reductase B/A (MsrB/A).

146 We further expressed mouse methionine sulfoxide reductase B1 (MsrB1), a selenoenzym

147 Methionine sulfoxide reductase enzymes MsrA and MsrB hav

148 ossesses significant homology to the peptide methionine sulfoxide reductase family of enzymes, specif

149 s of apoA-I and oxidized apoA-I treated with methionine sulfoxide reductase implicate oxidation of sp

150 This characteristic supports a role for methionine sulfoxide reductase in redox signaling.

151 ding or the repair of oxidized calmodulin by methionine sulfoxide reductase induces comparable change

152 e pK(a) of the active site cysteine of mouse methionine sulfoxide reductase is 7.2 even in the absenc

153 of oxidized methionine residues performed by methionine sulfoxide reductase is important for the gast

154 Reversing oxidation with methionine sulfoxide reductase restored HDL's ability to

155 MsrPQ is a newly identified methionine sulfoxide reductase system found in bacteria,

156 ine in proteins involving the enzyme peptide methionine sulfoxide reductase type A (MSRA) is postulat

157 Methionine sulfoxide reductase, which reduces methionine

158 In contrast, CshA- and methionine sulfoxide reductase-negative (MsrA-) strains

159 and the oxidized protein was incubated with methionine sulfoxide reductase.

160 ribonucleotide reductase, peroxiredoxin, and methionine sulfoxide reductase.

161 it is reversed by coexpression with peptide methionine sulfoxide reductase.

162 ion mediated by a ubiquitous enzyme, peptide methionine sulfoxide reductase.

163 ould be reversed by treating the enzyme with methionine sulfoxide reductase.

164 nt study on the reducing requirement for the methionine sulfoxide reductases (Msr), we have shown tha

165 ein functional changes through the action of methionine sulfoxide reductases (Msr).

166 f methionine sulfoxide (MetO) is mediated by methionine sulfoxide reductases (Msr).

167 Peptide methionine sulfoxide reductases (MsrA) from many differe

168 Methionine sulfoxide reductases (Msrs) are oxidoreductas

169 s damage is reversible through the action of methionine sulfoxide reductases (MSRs), which play key r

170 n is catalyzed by a family of enzymes called methionine sulfoxide reductases (MSRs).

171 oxidized methionine residues is catalyzed by methionine sulfoxide reductases (Msrs).

172 revisiae as a model, we show that of the two methionine sulfoxide reductases (MXR1, MXR2), deletion o

173 rx2) and the intracellular and extracellular methionine sulfoxide reductases (SpMsrAB1 and SpMsrAB2,

174 (MetO) residues in proteins is catalyzed by methionine sulfoxide reductases A (MSRA) and B (MSRB), w

175 In normal healthy human skin, methionine sulfoxide reductases A and B specifically red

176 S) can be repaired in the human epidermis by methionine sulfoxide reductases A and B, respectively.

177 MSRAs (methionine sulfoxide reductases A) are enzymes that reve

178 Inactivation of HypT depends on the methionine sulfoxide reductases A/B.

179 Methionine sulfoxide reductases are conserved enzymes th

180 Peptide methionine sulfoxide reductases are conserved enzymes th

181 Methionine sulfoxide reductases are key enzymes that rep

182 activity of plastidial thiol peroxidases and methionine sulfoxide reductases employing a single cyste

183 However, the identity of all methionine sulfoxide reductases involved, their cellular

184 Here we used yeast methionine sulfoxide reductases MsrA and MsrB to address

185 teins or repair oxidized residues, including methionine sulfoxide reductases MsrA and MsrB, which red

186 sporadically evolved Sec-containing forms of methionine sulfoxide reductases reflect catalytic advant

187 Reduction back to methionine by methionine sulfoxide reductases would allow the antioxid

188 Most cells contain methionine sulfoxide reductases, which catalyze a thiore

189 so observed that are catalyzed by endogenous methionine sulfoxide reductases.

190 he action of stereospecific enzymes known as methionine sulfoxide reductases.

191 Methionine-sulfoxide reductases are unique, in that thei

192 Comparable extents of methionine sulfoxide reduction are also observed that ar

193 Alternatively, MsrA catalyzes methionine sulfoxide reduction linked to the mycothiol/m

194 rved SelR enzyme family, define a pathway of methionine sulfoxide reduction, reveal a case of converg

195 Disruption of bacterial methionine sulfoxide repair systems rendered E. coli mor

196 metry to investigate the extent and rates of methionine sulfoxide repair within CaMox.

197 sulfoxide reductase (MsrA), which can reduce methionine sulfoxide residues back to methionine, restor

198 4.6) is a ubiquitous protein that can reduce methionine sulfoxide residues in proteins as well as in

199 fense against oxidative stresses by reducing methionine sulfoxide residues in proteins back to methio

200 MsrA and MsrB in E. coli are able to reduce methionine sulfoxide residues in proteins to methionines

201 Oxidative damage, mainly methionine sulfoxide residues, was also increased: 2.5 v

202 and to conversion of methionine residues to methionine sulfoxide residues.

203 24) thiolate, which directly interacted with methionine sulfoxide, resulting in methionine and a Cys(

204 oxide reductases A and B specifically reduce methionine sulfoxides (S) and (R), respectively, back to

205 activity and the reduction activity of free methionine sulfoxide(s) were stereoselective toward the

206 Raman bands characteristic of methionine sulfoxide show that extensive methionine oxid

207 ous substitution by glutamine, mimicking the methionine sulfoxide state, increased the viability of E

208 ge into methionine, N-glycyl-methionine, and methionine sulfoxide suggests that a prominent solvent e

209 )H incorporation into the gamma-methylene of methionine sulfoxide that is absent for N-glycyl-methion

210 For methionine sulfoxide the inflection point energy is 2.8

211 nonoxidized), and with increasing numbers of methionine sulfoxides the kinetics of fibrillation becam

212 When this methionine residue is oxidized to methionine sulfoxide, the inactivation is disrupted, and

213 tein repair each targeting a diastereomer of methionine sulfoxide, their deletion resulted in differe

214 with methionine residues in proteins to form methionine sulfoxide, thus scavenging the reactive speci

215 eductase A (MsrA) catalyzes the reduction of methionine sulfoxide to methionine and is specific for t

216 ethionine sulfoxide reductase, which reduces methionine sulfoxide to methionine in a thioredoxin-depe

217 Taken together, MSRB3-catalyzed reduction of methionine sulfoxides to methionine is essential for hea

218 so capable of reducing nicotinamide N-oxide, methionine sulfoxide, trimethylamine-N-oxide, and dimeth

219 However, much more methionine sulfoxide was generated by peroxide treatment

220 rmore, high levels of free and protein-bound methionine sulfoxide were detected in extracts of msrA m

221 metformin therapy, arginine-derived AGE and methionine sulfoxide were lower than in patients not rec

222 markers of oxidative stress such as urinary methionine sulfoxide were observed in Hhip (+/-) but not

223 of a variety of other substrates, including methionine sulfoxide, with decreased efficiencies, sugge

224 sulfoxide formation and (ii) MsrA can repair methionine sulfoxides within cytosolic proteins.

225 air by MsrA, there remains a distribution of methionine sulfoxides within functionally reactivated Ca

226 The rates of repair of methionine sulfoxides within individual tryptic fragment

227 dary structure, suggesting that MsrA repairs methionine sulfoxides within unfolded sequences until na