ライフサイエンスコーパス: sulfenic acid

1 natively S-oxidized thiols (e.g. disulfides, sulfenic acids).

2 of proteins and is initially oxidized to the sulfenic acid.

3 es by converting their catalytic cysteine to sulfenic acid.

4 f intra- or intermolecular disulfide(s) or a sulfenic acid.

5 ntaining an active site cysteine or cysteine sulfenic acid.

6 esting that sulfhydryls were oxidized beyond sulfenic acid.

7 its catalytic site cysteine, most likely to sulfenic acid.

8 ative to dioxane) which represents the Cys42-sulfenic acid.

9 tructure for any naturally occurring protein-sulfenic acid.

10 th at least one cysteine thiol oxidized to a sulfenic acid.

11 hree structurally exposed cysteine thiols to sulfenic acid.

12 -nitrosylation, disulfide formation, and Cys-sulfenic acid.

13 ate AR by modifying its cysteine residues to sulfenic acids.

14 of cysteine thiol groups to form cysteine S-sulfenic acids.

15 Z oxidizes TRPA1 cysteines to disulfides and sulfenic acids.

16 nyne (BCN) derivatives as concerted traps of sulfenic acids.

17 valent adducts with cysteine-derived protein sulfenic acids.

18 lly be used to trap biologically significant sulfenic acids.

19 to the oxidation of its cysteine residues to sulfenic acids.

20 pm, respectively, corresponding to the Cys42-sulfenic acid and -thiolate species.

21 harge-transfer interaction between the Cys42-sulfenic acid and FAD.

22 Both the sulfenic acid and mixed disulfide forms are structurally

23 the sulfur or polarity matching between the sulfenic acid and olefin derivative.

24 city of Ln-DOTA-Dimedone and Ln-MeCAT toward sulfenic acid and thiol residues, respectively, allow th

25 plex I activity implicating the formation of sulfenic acid and/or disulfide derivatives of cysteine i

26 nt with the conversion of cysteine thiols to sulfenic acids and disulfides to disulfide-S-monoxides.

27 ity was observed for cysteines known to form sulfenic acids and redox-active disulfides.

28 steine residue to the corresponding cysteine-sulfenic acid, and perhaps to higher oxidation states.

29 ents, e.g., formation of disulfide bonds and sulfenic acids, and others not so reversed, e.g., format

30 Protein sulfenic acids are formed by the reaction of biologicall

31 Since cysteine sulfenic acids are known to play an important function i

32 able of rapidly and efficiently trapping the sulfenic acid as a disulfide.

33 hydrogen peroxide to water using a cysteine-sulfenic acid as a secondary redox center.

34 usively establish the existence of the Cys42-sulfenic acid as the functional non-flavin redox center

35 eplacement (2.2 A); it revealed a stabilized sulfenic acid at Cys60.

36 g the peroxide substrate, forming a cysteine sulfenic acid at the active site.

37 ctrometry analysis revealed the formation of sulfenic acids at Cys-298 and Cys-303.

38 The Cys42-sulfenic acid atoms C alpha-C beta-S gamma-O roughly def

39 obe to demonstrate that C182 was oxidized to sulfenic acid by air, hydrogen peroxide and hypochlorite

40 The rate of thiolate conversion to the sulfenic acid by hydrogen peroxide for Cdc25B is 15-fold

41 ve site cysteine susceptible to oxidation to sulfenic acid by micromolar concentrations of hydrogen p

42 d that Cys-298 of AR was readily oxidized to sulfenic acid by peroxynitrite.

43 ultaneous precipitation of the o-nitrophenyl sulfenic acid byproduct.

44 the sole cysteine residue in OhrR leads to a sulfenic acid-containing intermediate that retains DNA-b

45 general utility for this reagent with other sulfenic acid-containing proteins.

46 improved procollagen maturation and lowered sulfenic acid content in vivo.

47 The function of the cysteine sulfenic acid coordinated to the iron active site of NHa

48 radical (Cys(231)-S(*)) on one cysteine and sulfenic acid (Cys(231)-SOH) on the other.

49 than 20 years that unusually stable cysteine-sulfenic acid (Cys-SOH) derivatives can be introduced in

50 general trap for proteins that form cysteine sulfenic acid (Cys-SOH) in vivo.

51 bclass of Prxs (human Prx1-4) utilizes a Cys sulfenic acid (Cys-SOH) intermediate and disulfide bond

52 translational protein modification, cysteine sulfenic acid (Cys-SOH) is well established as an oxidat

53 nzo-2-oxa-1,3-diazole to identify a cysteine sulfenic acid (Cys-SOH) modification that forms on Cys(3

54 face FAD is consistent with oxidation to the sulfenic acid (Cys-SOH) state.

55 We have proposed a cysteine-sulfenic acid (Cys-SOH) structure for the oxidized form

56 aracterized flavoprotein with an active-site sulfenic acid (Cys-SOH), also yielded the spectrally-dis

57 t-translational redox generation of cysteine-sulfenic acids (Cys-SOH) functions as an important rever

58 ntain post-translationally modified cysteine sulfenic acids (Cys-SOH).

59 transfers its electrons to the single Cys42-sulfenic acid (Cys42-SOH) redox center, which remains ox

60 supporting its identification as a cysteine sulfenic acid (Cys46-SOH).

61 he condensation of two molecules of cysteine sulfenic acid (CySOH) to give CyS(=O)SCy.

62 Cysteine sulfenic acid CysS(O)H is shown to be formed for the rea

63 with the latter reductant are the respective sulfenic acids CysS(O)H and GS(O)H, although these react

64 The sulfenic acids, CysS(O)H and GS(O)H, are transient speci

65 nucleophilic cysteine is regulated through a sulfenic acid-dependent switch, leading to S-glutathiony

66 -CoA results in the transient formation of a sulfenic acid derivative of CoA which subsequently react

67 oxide leads to significant accumulation of a sulfenic acid derivative of Cys420 which is located in t

68 th the N-terminal cysteine of MtMrx1 and the sulfenic acid derivative of the peroxidatic cysteine of

69 e oxidation states of cysteine, formation of sulfenic acid derivatives or disulfides can be relevant

70 Interestingly, the oxidation is only to sulfenic acid despite the crystal growth time period of

71 thionine S-sulfoxide and to employ a similar sulfenic acid/disulfide mechanism.

72 In vitro, the presence of a sulfenic acid donor accelerated the oxidative inactivati

73 ctly capture the reactivity of an individual sulfenic acid embedded within the core of a single Ig do

74 hione reductase provides an insight into the sulfenic acid FAD charge-transfer interaction observed w

75 the crystal structures of the reduced form, sulfenic acid form, and mixed disulfide form of SarZ.

76 ngly, the cysteine sulfur is oxidized to the sulfenic acid form.

77 Cys651-sulfenic acid formation could be one DTT-reversible inac

78 text-independent, and capable of visualizing sulfenic acid formation in cells.

79 amined the importance of reversible cysteine sulfenic acid formation in naive CD8(+) T cell activatio

80 results demonstrate that reversible cysteine sulfenic acid formation is an important regulatory mecha

81 Sulfenic acid formation modulates the function of enzyme

82 the site, timing, and conditions of protein sulfenic acid formation remains crucial to understanding

83 ive to the inhibition of reversible cysteine sulfenic acid formation than IFN-gamma.

84 mine the contribution of reversible cysteine sulfenic acid formation to T cell activation, increasing

85 :alliinase of 5:1, LFS sequesters all of the sulfenic acid formed by alliinase action on petiveriin,

86 ate constant of the reaction of H2S with the sulfenic acid formed in HSA was determined.

87 Although the sulfenic acid forms of Prx2 and Prx3 are ~1000-fold less

88 H10A mutants, in their oxidized E(FAD, Cys42-sulfenic acid) forms, exhibit enhanced long-wavelength a

89 Cysteine sulfenic acid has been generated in alkaline aqueous sol

90 ion and the subsequent reactions of cysteine sulfenic acid have been studied by stopped-flow spectrop

91 Cysteine sulfenic acids have been shown to play diverse roles in

92 W197I variant is the first reported cysteine sulfenic acid in a serine esterase.

93 se, which use a single redox-active cysteine-sulfenic acid in catalysis.

94 Unlike the case for other PTPs, the sulfenic acid in MKP3 does not form a sulfenyl-amide spe

95 Yet the dynamics of sulfenic acid in proteins remains largely elusive due to

96 s the reduction of cysteine sulfinic acid to sulfenic acid in proteins subject to oxidative stress.

97 ROI resulted in elevated levels of cysteine sulfenic acid in the total proteome.

98 cyclic benzoxaboroles can form adducts with sulfenic acids in aqueous medium and that these boron-ba

99 ditions for selective labeling of cysteine S-sulfenic acids in intact cells with the commercially ava

100 strained cycloalkynes react efficiently with sulfenic acids in proteins and small molecules yielding

101 H-terminal cysteine (C581), and the level of sulfenic acid increases in response to oxidant exposure.

102 azole (NBD-Cl), it was shown that a cysteine sulfenic acid intermediate (Cys-SOH) is formed after att

103 vitro oxidation pathway begins with a stable sulfenic acid intermediate and is followed by the format

104 Furthermore, a sulfenic acid intermediate at Cys(61) generated by cumen

105 is activity likely involves reduction of the sulfenic acid intermediate form of PTP1B by TrxR1 and is

106 the LFS sequesters, to varying degrees, the sulfenic acid intermediate formed by alliinase-mediated

107 tive EgtE substrate and the involvement of a sulfenic acid intermediate in the ergothioneine C-S lyas

108 osition 315 to sulfonic acid occurring via a sulfenic acid intermediate in the H(2)O(2)-treated C318A

109 reversible inactivation involving a cysteine sulfenic acid intermediate is proposed.

110 Copper-mediated sulfenylation leads to a sulfenic acid intermediate that eventually resolves to f

111 This initial oxidation generates an unstable sulfenic acid intermediate that is quickly converted int

112 hydrogen peroxide potentially through a C335 sulfenic acid intermediate.

113 xide, resulting in methionine and a Cys(124) sulfenic acid intermediate.

114 form either an intermolecular disulfide or a sulfenic acid intermediate.

115 n utilize thioredoxin as a reductant for the sulfenic acid intermediate.

116 Current methods for trapping and analyzing sulfenic acids involve the use of dimedone and other nuc

117 Our results demonstrate that sulfenic acid is a crucial short-lived intermediate that

118 For this approach, the sulfenic acid is derivatized with a chemical tag to gene

119 so observed in two conformations; in one the sulfenic acid is hydrogen bonded to His10 and in the oth

120 A transient sulfenic acid is initially formed on Cys-45, before reso

121 iation between protein-associated thiols and sulfenic acids is therefore now possible by means of bot

122 ion intermediates and implicate the cysteine-sulfenic acid ligand as the catalytic nucleophile, a her

123 tofore unknown role for the alphaCys(113)-OH sulfenic acid ligand.

124 s sensitive to oxidation; thus, the cysteine sulfenic acid may play a role in the regulation of a "D-

125 This cysteine, which can be oxidized to a sulfenic acid, mediates the formation of a disulfide-lin

126 Our results suggest that a sulfenic acid modification at Cys-265 performs a regulat

127 SHP-2, as well as actin, underwent increased sulfenic acid modification following stimulation.

128 ased oxidant damage, which led to a cysteine sulfenic acid modification in endothelin B receptor and

129 dione (DAz-2) shows that Cys420 also forms a sulfenic acid modification in vivo when cells are expose

130 Moreover, Western blotting demonstrated that sulfenic acid modification is a trigger for channel degr

131 This sulfenic acid modification is reversible and stable in t

132 The Cys(13) sulfenic acid modification is stabilized through two hyd

133 ydroxyproline content and enhanced cysteinyl sulfenic acid modification of ER proteins.

134 We therefore hypothesized that sulfenic acid modification of the channel itself may reg

135 atients with atrial fibrillation, as well as sulfenic acid modification to Kv1.5 in the heart.

136 Sulfenic acid modification to proteins, which is elevate

137 edox status and reveals a diverse pattern of sulfenic acid modifications across different subtypes of

138 n blotting demonstrated a global increase in sulfenic acid-modified proteins in human patients with a

139 rate that unlike the case for some PTPs, the sulfenic acid of the active site cysteine in MKP3 is not

140 wild-type AhpC by reacting with the nascent sulfenic acid of the oxidized protein (Cys46-SOH) to gen

141 r studies showed that Kv1.5 is modified with sulfenic acid on a single COOH-terminal cysteine (C581),

142 0S BCP mutant reacts with peroxide to form a sulfenic acid on Cys-45, in the same manner as wild-type

143 Formation of sulfenic acid on cysteine residues of proteins is an imp

144 nversion to the reactive cationic thiophilic sulfenic acid or sulfenamide depends mainly not on pyrid

145 Dithiothreitol could reduce either the sulfenic acid or the disulfide, but the disulfide was a

146 hese results provide the first example where sulfenic acid oxidation of a cysteine in a HTH-motif lea

147 te constant for H2O2 inactivation (via Cys42-sulfenic acid oxidation) of the H10Q mutant, these obser

148 reagents, the BCN compounds distinguish the sulfenic acid oxoform from the thiol, disulfide, sulfini

149 c acid oxygen, this structure shows that the sulfenic acid oxygen does not occupy this position, nor

150 such as dimedone is in the retention of the sulfenic acid oxygen in the modified product; differenti

151 epsilon 2 contributes a hydrogen bond to the sulfenic acid oxygen, at a distance of 3.2 A.

152 ture was taken to represent the native Cys42-sulfenic acid oxygen, this structure shows that the sulf

153 cal mechanisms include reaction with protein sulfenic acids (P-SOH) or the involvement of metal cente

154 generated at its sources and (b) mapping of sulfenic acid posttranslational modification targets tha

155 2, the LFS is unable to sequester all of the sulfenic acid produced by the alliinase, with the result

156 When exposed to the solution, sulfenic acid rapidly undergoes further chemical modific

157 165S was also modified by dimedone, a common sulfenic acid reagent, to give the expected inactivated

158 ant advantage of NBD-Cl over previously-used sulfenic acid reagents such as dimedone is in the retent

159 In order to characterize the native Cys42-sulfenic acid redox center of the flavoprotein NADH pero

160 tions in part to stabilize the unusual Cys42-sulfenic acid redox center within the active-site enviro

161 rotein NADH peroxidase with its native Cys42-sulfenic acid redox center, a strategy combining reduced

162 B proteins employ alternative mechanisms for sulfenic acid reduction.

163 ssist in analyzing the chemical mechanism of sulfenic acid reduction.

164 particularly oxidation of cysteine thiols to sulfenic acids, represents a prominent posttranslational

165 Dimedone alkylates protein sulfenic acid residues and presumably will alkylate sele

166 ses protein thiols to competing oxidation to sulfenic acid, resulting in depletion of ascorbic acid,

167 ution at position 420 that mimics a cysteine sulfenic acid results in a ~4-fold increase in DNA bindi

168 n sulfide (H2S) and disulfides (RSSR) and/or sulfenic acids (RSOH).

169 In addition, H2S is able to react with sulfenic acids (RSOH).

170 tain relative and absolute quantification of sulfenic acid (SA) in peptides and proteins.

171 cilitate the discovery of previously unknown sulfenic acid sites and their parent proteins.

172 In this study, we demonstrate that a stable sulfenic acid (-SOH) derivative also forms at Cys-265 in

173 uring ER-derived oxidative stress, forming a sulfenic acid (-SOH) moiety.

174 n mass spectrometric analysis using DAz-2, a sulfenic acid (-SOH)-specific probe, demonstrates that e

175 re cysteine residues that become oxidized to sulfenic acid (-SOH).

176 f homocysteine to engender the corresponding sulfenic acid species that further participates into the

177 ic analysis of protein S-sulfenylation using sulfenic acid-specific chemical probes and mass spectrom

178 Labeling studies with the sulfenic acid-specific probe DAz and horseradish peroxid

179 ve enzyme, formed a covalent adduct with the sulfenic acid-specific reagent dimedone.

180 our structure-based understanding of protein-sulfenic acid stabilization and function.

181 hemical labeling of cysteine residues in the sulfenic acid state, we visualize oxidized Src homology

182 Comparison of the native Cys42-sulfenic acid structure with that of two-electron reduce

183 in tandem, with the alliinase furnishing the sulfenic acid substrate on which the LFS acts.

184 duced by the alliinase, with the result that sulfenic acid that escapes the action of the LFS condens

185 ast, the E18D mutation stabilizes a cysteine-sulfenic acid that is readily reduced to the thiol in so

186 nt of an immunochemical method for detecting sulfenic acid, the initial oxidation product that result

187 Oxidation of the sulfenic acid, the secondary redox center, results in in

188 ough a hydrolytic mechanism that generates a sulfenic acid/thiol pair.

189 evidence in support of the peroxidase Cys42-sulfenic acid/thiol redox cycle and add significantly to

190 enamine, which then undergoes loss of phenyl sulfenic acid to furnish the aromatized amine in good yi

191 n suggests that the condensation of cysteine sulfenic acid to give cysteine thiosulfinate ester can b

192 ly been attributed to oxidation of the Cys42-sulfenic acid to the Cys42-sulfinic and/or sulfonic acid

193 the peroxidase results from oxidation of the sulfenic acid to the sulfinic or sulfonic acid forms.

194 nism that regulates the reduction of protein sulfenic acids to cysteines.

195 ed: (1) below pH 12, the condensation of two sulfenic acids to give cysteine thiosulfinate ester foll

196 roxynitrite-mediated oxidation of Cys-298 to sulfenic acid via the PI3K/Akt/endothelial NOS pathway.

197 ed that the reversible formation of cysteine sulfenic acid was critical for ERK1/2 phosphorylation, c

198 imedone), which covalently binds to cysteine sulfenic acid, were added to cultures.

199 e.g., phenols, diarylamines, hydroxylamines, sulfenic acids), which tend to have high H-bond aciditie

200 The latter reaction occurred via the sulfenic acid, which reacted sufficiently rapidly (k = 5

201 ins (Prxs) react rapidly with H2O2 to form a sulfenic acid, which then condenses with the resolving c

202 ive Cys residues of PDI to the corresponding sulfenic acids, which reacted with the resolving thiols

203 A further reaction of the Cys(13) sulfenic acid with an external thiol leads to formation

204 rate-limiting comproportionation of cysteine sulfenic acid with cysteinate to give cystine.

205 rate-limiting comproportionation of cysteine sulfenic acid with cysteinate to give cystine.

206 be competitive with the reaction of cysteine sulfenic acid with cysteine.

207 ncluding the transient formation of cysteine sulfenic acid within AhpC is proposed.

208 The trapping of a sulfenic acid within the fully active C165S mutant of th

209 the active-site cysteine in the Cdc25's, the sulfenic acid would rapidly oxidize further to the irrev

210 Both reactions of H2S with disulfides and sulfenic acids yield persulfides (RSSH), recently identi

211 e titration of an R303M mutant [E(FAD, Cys42-sulfenic acid)] yields a two-electron reduced intermedia