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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 y" trans-cyclooctenes react only slowly with sulfenic acids.
14 ate AR by modifying its cysteine residues to sulfenic acids.
15 of cysteine thiol groups to form cysteine S-sulfenic acids.
16 Z oxidizes TRPA1 cysteines to disulfides and sulfenic acids.
17 nyne (BCN) derivatives as concerted traps of sulfenic acids.
18 valent adducts with cysteine-derived protein sulfenic acids.
19 lly be used to trap biologically significant sulfenic acids.
20 to the oxidation of its cysteine residues to sulfenic acids.
21 agents and the unique chemical properties of sulfenic acid, a pivotal post-translational cysteine mod
22 rsal' of sulfur when cysteine is oxidized to sulfenic acid, a widespread post-translational modificat
25 the C-Ala domain) were modified to cysteine sulfenic acid and methionine sulfoxide, respectively.
29 city of Ln-DOTA-Dimedone and Ln-MeCAT toward sulfenic acid and thiol residues, respectively, allow th
30 plex I activity implicating the formation of sulfenic acid and/or disulfide derivatives of cysteine i
31 nt with the conversion of cysteine thiols to sulfenic acids and disulfides to disulfide-S-monoxides.
32 reliminary hypothesis about participation of sulfenic acids and methylsulfinyl radicals as radical tr
34 enzothiazine probes to sequentially alkylate sulfenic acids and then free thiols and, finally, after
35 dized thiol derivatives (i.e. disulfides and sulfenic acids) and thereby forms persulfides, which are
36 steine residue to the corresponding cysteine-sulfenic acid, and perhaps to higher oxidation states.
37 ents, e.g., formation of disulfide bonds and sulfenic acids, and others not so reversed, e.g., format
44 usively establish the existence of the Cys42-sulfenic acid as the functional non-flavin redox center
50 obe to demonstrate that C182 was oxidized to sulfenic acid by air, hydrogen peroxide and hypochlorite
52 ve site cysteine susceptible to oxidation to sulfenic acid by micromolar concentrations of hydrogen p
55 the sole cysteine residue in OhrR leads to a sulfenic acid-containing intermediate that retains DNA-b
60 ations in proteins, including oxidation into sulfenic acid (Cys-SOH) by reactive oxygen species gener
61 than 20 years that unusually stable cysteine-sulfenic acid (Cys-SOH) derivatives can be introduced in
63 bclass of Prxs (human Prx1-4) utilizes a Cys sulfenic acid (Cys-SOH) intermediate and disulfide bond
64 translational protein modification, cysteine sulfenic acid (Cys-SOH) is well established as an oxidat
65 nzo-2-oxa-1,3-diazole to identify a cysteine sulfenic acid (Cys-SOH) modification that forms on Cys(3
68 aracterized flavoprotein with an active-site sulfenic acid (Cys-SOH), also yielded the spectrally-dis
71 t-translational redox generation of cysteine-sulfenic acids (Cys-SOH) functions as an important rever
73 transfers its electrons to the single Cys42-sulfenic acid (Cys42-SOH) redox center, which remains ox
77 with the latter reductant are the respective sulfenic acids CysS(O)H and GS(O)H, although these react
79 nucleophilic cysteine is regulated through a sulfenic acid-dependent switch, leading to S-glutathiony
80 -CoA results in the transient formation of a sulfenic acid derivative of CoA which subsequently react
81 oxide leads to significant accumulation of a sulfenic acid derivative of Cys420 which is located in t
82 th the N-terminal cysteine of MtMrx1 and the sulfenic acid derivative of the peroxidatic cysteine of
83 nder these conditions, H(2)O(2) oxidizes the sulfenic acid derivative of the Prx peroxidatic Cys (C(P
84 e oxidation states of cysteine, formation of sulfenic acid derivatives or disulfides can be relevant
88 ctly capture the reactivity of an individual sulfenic acid embedded within the core of a single Ig do
89 hione reductase provides an insight into the sulfenic acid FAD charge-transfer interaction observed w
90 cysteine residues of target proteins to the sulfenic acid form and, similar to other organisms, this
91 the crystal structures of the reduced form, sulfenic acid form, and mixed disulfide form of SarZ.
95 amined the importance of reversible cysteine sulfenic acid formation in naive CD8(+) T cell activatio
96 results demonstrate that reversible cysteine sulfenic acid formation is an important regulatory mecha
98 the site, timing, and conditions of protein sulfenic acid formation remains crucial to understanding
100 mine the contribution of reversible cysteine sulfenic acid formation to T cell activation, increasing
101 :alliinase of 5:1, LFS sequesters all of the sulfenic acid formed by alliinase action on petiveriin,
105 H10A mutants, in their oxidized E(FAD, Cys42-sulfenic acid) forms, exhibit enhanced long-wavelength a
108 ion and the subsequent reactions of cysteine sulfenic acid have been studied by stopped-flow spectrop
114 s the reduction of cysteine sulfinic acid to sulfenic acid in proteins subject to oxidative stress.
116 cyclic benzoxaboroles can form adducts with sulfenic acids in aqueous medium and that these boron-ba
117 ditions for selective labeling of cysteine S-sulfenic acids in intact cells with the commercially ava
118 O biotin conjugate was used to label protein sulfenic acids in live cells, and subsequent quenching b
119 strained cycloalkynes react efficiently with sulfenic acids in proteins and small molecules yielding
120 findings reveal a vast expanse of ligandable sulfenic acids in the human proteome and highlight the u
121 H-terminal cysteine (C581), and the level of sulfenic acid increases in response to oxidant exposure.
122 azole (NBD-Cl), it was shown that a cysteine sulfenic acid intermediate (Cys-SOH) is formed after att
123 vitro oxidation pathway begins with a stable sulfenic acid intermediate and is followed by the format
125 is activity likely involves reduction of the sulfenic acid intermediate form of PTP1B by TrxR1 and is
126 the LFS sequesters, to varying degrees, the sulfenic acid intermediate formed by alliinase-mediated
127 tive EgtE substrate and the involvement of a sulfenic acid intermediate in the ergothioneine C-S lyas
128 osition 315 to sulfonic acid occurring via a sulfenic acid intermediate in the H(2)O(2)-treated C318A
130 Copper-mediated sulfenylation leads to a sulfenic acid intermediate that eventually resolves to f
131 This initial oxidation generates an unstable sulfenic acid intermediate that is quickly converted int
136 Current methods for trapping and analyzing sulfenic acids involve the use of dimedone and other nuc
139 so observed in two conformations; in one the sulfenic acid is hydrogen bonded to His10 and in the oth
141 iation between protein-associated thiols and sulfenic acids is therefore now possible by means of bot
142 ion intermediates and implicate the cysteine-sulfenic acid ligand as the catalytic nucleophile, a her
144 s sensitive to oxidation; thus, the cysteine sulfenic acid may play a role in the regulation of a "D-
145 This cysteine, which can be oxidized to a sulfenic acid, mediates the formation of a disulfide-lin
148 ased oxidant damage, which led to a cysteine sulfenic acid modification in endothelin B receptor and
149 dione (DAz-2) shows that Cys420 also forms a sulfenic acid modification in vivo when cells are expose
150 Moreover, Western blotting demonstrated that sulfenic acid modification is a trigger for channel degr
157 edox status and reveals a diverse pattern of sulfenic acid modifications across different subtypes of
158 n blotting demonstrated a global increase in sulfenic acid-modified proteins in human patients with a
160 to form methanesulfinic acid (MSIA), methane sulfenic acid (MSEA), the methylthio radical (CH(3)S), a
161 s fast with hydroperoxides, forming a stable sulfenic acid (MtAhpE-SOH), which we chose here as a mod
162 rate that unlike the case for some PTPs, the sulfenic acid of the active site cysteine in MKP3 is not
163 wild-type AhpC by reacting with the nascent sulfenic acid of the oxidized protein (Cys46-SOH) to gen
165 r studies showed that Kv1.5 is modified with sulfenic acid on a single COOH-terminal cysteine (C581),
166 0S BCP mutant reacts with peroxide to form a sulfenic acid on Cys-45, in the same manner as wild-type
168 nversion to the reactive cationic thiophilic sulfenic acid or sulfenamide depends mainly not on pyrid
170 hese results provide the first example where sulfenic acid oxidation of a cysteine in a HTH-motif lea
171 te constant for H2O2 inactivation (via Cys42-sulfenic acid oxidation) of the H10Q mutant, these obser
172 reagents, the BCN compounds distinguish the sulfenic acid oxoform from the thiol, disulfide, sulfini
173 c acid oxygen, this structure shows that the sulfenic acid oxygen does not occupy this position, nor
174 such as dimedone is in the retention of the sulfenic acid oxygen in the modified product; differenti
176 ture was taken to represent the native Cys42-sulfenic acid oxygen, this structure shows that the sulf
177 cal mechanisms include reaction with protein sulfenic acids (P-SOH) or the involvement of metal cente
178 generated at its sources and (b) mapping of sulfenic acid posttranslational modification targets tha
179 2, the LFS is unable to sequester all of the sulfenic acid produced by the alliinase, with the result
183 165S was also modified by dimedone, a common sulfenic acid reagent, to give the expected inactivated
184 ant advantage of NBD-Cl over previously-used sulfenic acid reagents such as dimedone is in the retent
185 In order to characterize the native Cys42-sulfenic acid redox center of the flavoprotein NADH pero
186 tions in part to stabilize the unusual Cys42-sulfenic acid redox center within the active-site enviro
187 rotein NADH peroxidase with its native Cys42-sulfenic acid redox center, a strategy combining reduced
188 AM-TCO probes to identify and quantify known sulfenic acid redox proteins as well as targets not capt
189 hetic molecules for rapid isotopic coding of sulfenic acids, reduced cysteines, and disulfides in cel
192 particularly oxidation of cysteine thiols to sulfenic acids, represents a prominent posttranslational
194 ses protein thiols to competing oxidation to sulfenic acid, resulting in depletion of ascorbic acid,
195 ution at position 420 that mimics a cysteine sulfenic acid results in a ~4-fold increase in DNA bindi
201 In this study, we demonstrate that a stable sulfenic acid (-SOH) derivative also forms at Cys-265 in
203 n mass spectrometric analysis using DAz-2, a sulfenic acid (-SOH)-specific probe, demonstrates that e
205 f homocysteine to engender the corresponding sulfenic acid species that further participates into the
206 ic analysis of protein S-sulfenylation using sulfenic acid-specific chemical probes and mass spectrom
210 hemical labeling of cysteine residues in the sulfenic acid state, we visualize oxidized Src homology
213 duced by the alliinase, with the result that sulfenic acid that escapes the action of the LFS condens
214 ast, the E18D mutation stabilizes a cysteine-sulfenic acid that is readily reduced to the thiol in so
215 nt of an immunochemical method for detecting sulfenic acid, the initial oxidation product that result
219 evidence in support of the peroxidase Cys42-sulfenic acid/thiol redox cycle and add significantly to
220 enamine, which then undergoes loss of phenyl sulfenic acid to furnish the aromatized amine in good yi
221 n suggests that the condensation of cysteine sulfenic acid to give cysteine thiosulfinate ester can b
222 ly been attributed to oxidation of the Cys42-sulfenic acid to the Cys42-sulfinic and/or sulfonic acid
223 the peroxidase results from oxidation of the sulfenic acid to the sulfinic or sulfonic acid forms.
225 ed: (1) below pH 12, the condensation of two sulfenic acids to give cysteine thiosulfinate ester foll
226 roxynitrite-mediated oxidation of Cys-298 to sulfenic acid via the PI3K/Akt/endothelial NOS pathway.
227 These probes enable a new mode of capturing sulfenic acids via transannular thioetherification, wher
228 ed that the reversible formation of cysteine sulfenic acid was critical for ERK1/2 phosphorylation, c
231 e.g., phenols, diarylamines, hydroxylamines, sulfenic acids), which tend to have high H-bond aciditie
233 ins (Prxs) react rapidly with H2O2 to form a sulfenic acid, which then condenses with the resolving c
234 ive Cys residues of PDI to the corresponding sulfenic acids, which reacted with the resolving thiols
239 of H(2)O(2) facilitates condensation of C(P) sulfenic acid with GSH to give diglutathionylated produc
242 the active-site cysteine in the Cdc25's, the sulfenic acid would rapidly oxidize further to the irrev
243 Both reactions of H2S with disulfides and sulfenic acids yield persulfides (RSSH), recently identi
244 e titration of an R303M mutant [E(FAD, Cys42-sulfenic acid)] yields a two-electron reduced intermedia