ライフサイエンスコーパス: methanethiosulfonate

1 thyl methanethiosulfonate and ethylsulfonate methanethiosulfonate).

2 aut's reagent) and MTS1 [1,1-methanediyl bis(methanethiosulfonate)].

3 e was fully restored by adding ethylammonium methanethiosulfonate.

4 SEA-biotin) and [2-(trimethylammonium)ethyl] methanethiosulfonate.

5 either a biotin- or Texas red-derivative of methanethiosulfonate.

6 methanethiosulfonate and (2-sulfonatoethyl) methanethiosulfonate.

7 y quinacrine from reaction with 2-aminoethyl methanethiosulfonate.

8 thiol-specific agent ethyltrimethylammonium methanethiosulfonate.

9 t had been treated with N-biotinylaminoethyl methanethiosulfonate.

10 hanethiosulfonate and ethyltrimethylammonium methanethiosulfonate.

11 e Cys-directed reagent, N-biotinylaminoethyl methanethiosulfonate.

12 rd the impermeant 2-(trimethylammonium)ethyl methanethiosulfonate.

13 sensitive to the inhibition by (2-aminoethyl)methanethiosulfonate.

14 ne residues with impermeant 2-sulfonatoethyl methanethiosulfonate.

15 -impermeant probe 2-(trimethylammonium)ethyl methanethiosulfonate.

16 wo cysteines to modification by 2-aminoethyl methanethiosulfonate.

17 (TM) 6 as the residue responsible for methyl methanethiosulfonate (a membrane-permeable sulfhydryl mo

18 tants were labeled with N-biotinylaminoethyl methanethiosulfonate, a membrane-impermeable cysteine-di

19 (1-oxy-2,2,5,5-tetramethylpyrroline-3-methyl)methanethiosulfonate, a spin label reagent, were studied

20 tion of Cys201 was further demonstrated with methanethiosulfonate, a spin-labeled probe.

21 Treatment with 2-([biotinoyl] amino) ethyl methanethiosulfonate, a thiol-specific reagent that reac

22 ively large molecule [2-(trimethylammonium)] methanethiosulfonate accessed positions near the putativ

23 onist 2-nonanone protected the receptor from methanethiosulfonate action at position 148, placing thi

24 Exposure to methanethiosulfonate agents that modify cysteine residue

25 inactivation by [2-(trimethylammonium)ethyl] methanethiosulfonate and (2-sulfonatoethyl) methanethios

26 active methanethiosulfonates [sulforhodamine-methanethiosulfonate and 2-((biotinoyl)amino)ethyl metha

27 bited by thiol-specific agents (carboxyethyl methanethiosulfonate and ethylsulfonate methanethiosulfo

28 Added study with carboxyethyl methanethiosulfonate and ethylsulfonate methylthiosulfon

29 meant, thiol-specific reagents, carboxyethyl methanethiosulfonate and ethyltrimethylammonium methanet

30 n 172, which reacted with both (2-aminoethyl)methanethiosulfonate and N-biotinylaminoethyl methanethi

31 ifunctional cross-linker 1,3-propanediyl bis-methanethiosulfonate and Western blotting, hRFC species

32 f this residue to 2-(trimethylammonium)ethyl methanethiosulfonate, and the bumetanide insensitivity o

33 Y102C was accessible to modification by methanethiosulfonate, and this modification was prevente

34 ing were also modified by 1 mm (2-aminoethyl)methanethiosulfonate applied in the absence of ATP when

35 ssays with membrane-impermeable 2-aminoethyl methanethiosulfonate-biotin and streptavidin beads to de

36 TMD2-3 loop domain reacted with 2-aminoethyl methanethiosulfonate-biotin, establishing aqueous access

37 nit c and tested for cross-linking using bis-methanethiosulfonate (bis-MTS) reagents.

38 reactive reagent 2-(trimethylammonium)ethyl methanethiosulfonate bromide (MTSET) alters in a phospho

39 block by inside [2-(trimethylammonium)ethyl]methanethiosulfonate bromide (MTSET) at slow stimulation

40 or movement, via [2-(trimethylammonium)ethyl]methanethiosulfonate bromide (MTSET) modification and fl

41 ere sensitive to [2-(trimethylammonium)ethyl]methanethiosulfonate bromide (MTSET) or MTSEA.

42 ide (MTSEA) and [(2-(trimethylammonium)ethyl]methanethiosulfonate bromide (MTSET)) and to Cd(2+) was

43 eactive reagent [2-(trimethylammonium)ethyl] methanethiosulfonate bromide (MTSET), alpha-beta-gamma H

44 fonate (MTSEA), [2-(trimethylammonium) ethyl]methanethiosulfonate bromide (MTSET), and sodium (2-sulf

45 modification by [2-(trimethylammonium)ethyl]methanethiosulfonate bromide (MTSET), channels exhibited

46 MTSEA) or 1 mM [2-(trimethylammonium) ethyl] methanethiosulfonate bromide (MTSET).

47 g site, because [2-(trimethylammonium)ethyl] methanethiosulfonate bromide did not prevent zinc potent

48 accessibility to 2-[(trimethylammonium)ethyl]methanethiosulfonate bromide modification were observed

49 modification by (2-(trimethylammonium)ethyl) methanethiosulfonate bromide of Cys at position 79 impac

50 n response to [(2-(trimethylammonium) ethyl] methanethiosulfonate bromide, or with brefeldin A, sugge

51 -active reagent [2-(trimethylammonium)ethyl] methanethiosulfonate bromide.

52 ubstrate analog [2-(trimethylammonium)-ethyl]methanethiosulfonate but was inaccessible to tetramethyl

53 hydryl modification of Y124C by 2-aminoethyl methanethiosulfonate, but not by N-ethylmaleimide, was f

54 s to the negatively charged 2-sulfonatoethyl methanethiosulfonate, but not neutral 2-hydroxyethyl met

55 tion, whereas [2-(trimethyl ammonium) ethyl] methanethiosulfonate chloride modification of I521C in t

56 in Xenopus oocytes and the current block by methanethiosulfonate compounds was measured.

57 ate the general utility of the 4-thiouridine/methanethiosulfonate coupling method to introduce nitrox

58 hetic propanethiol, or alternatively, propyl methanethiosulfonate, covalently binds to cysteine resid

59 However, an appropriate length MTS (MethaneThioSulfonate) cross-linking reagent (MTS14) rest

60 anethiosulfonate, or 2-trimethylammonioethyl methanethiosulfonate, decreased the glycine EC(50) to re

61 ced cysteine residues to sulfhydryl-reactive methanethiosulfonate derivatives ((2-aminoethyl)methanet

62 eaction of Cys-90 or Cys-306 with impermeant methanethiosulfonate derivatives enhanced dopamine uptak

63 ed sulfhydryl group with membrane-impermeant methanethiosulfonate derivatives inhibited substrate tra

64 reated with hydrophilic, sulfhydryl-specific methanethiosulfonate derivatives with control cell membr

65 brane domain three followed by labeling with methanethiosulfonate derivatives.

66 single and combination cysteine mutants with methanethiosulfonate ethylamine revealed that [(3)H]dihy

67 hen proteoliposomes were treated with MTSEA (methanethiosulfonate ethylamine), a thiol-specific reage

68 of Cys(439) by a 10,000-fold molar excess of methanethiosulfonate ethylamine, demonstrating that Cys(

69 logous mutation in NR2A, -2B, -2C, or -2D by methanethiosulfonate ethylammonium (MT-SEA) occurs only

70 the hydrophilic sulfhydryl-modifying agents methanethiosulfonate ethylammonium (MTSEA(+)) and methan

71 ssible in the binding-site crevice by use of methanethiosulfonate ethylammonium (MTSEA) and inferred

72 8, a piperidinyl antagonist, is inhibited by methanethiosulfonate ethylammonium (MTSEA) in a time- an

73 ositions tested, the presence of ACh changed methanethiosulfonate ethylammonium (MTSEA) modification

74 respectively, were found to be accessible to methanethiosulfonate ethylammonium (MTSEA) or methanethi

75 was diminished by chemical modification with methanethiosulfonate ethylammonium (MTSEA) to the outer

76 plication of the cysteine modification agent methanethiosulfonate ethylammonium (MTSEA) to V787C demo

77 hanethiosulfonate ethylsulfonate (MTSES) and methanethiosulfonate ethylammonium (MTSEA)) did not affe

78 charged, hydrophilic, thiol-specific reagent methanethiosulfonate ethylammonium (MTSEA), [(3)H]CP5594

79 delta receptor was relatively insensitive to methanethiosulfonate ethylammonium (MTSEA), a positively

80 hin the protein that binds membrane-permeant methanethiosulfonate ethylammonium (MTSEA), but not memb

81 s of introduced cysteines to modification by methanethiosulfonate ethylammonium (MTSEA)-Biotin were m

82 o not externally accessible when probed with methanethiosulfonate ethylammonium (MTSEA).

83 Previously we showed that methanethiosulfonate ethylammonium (MTSEA+) covalently m

84 sitively charged sulfhydryl-specific reagent methanethiosulfonate ethylammonium reacted with a cystei

85 by the sulfhydryl-specific modifying reagent methanethiosulfonate ethylammonium.

86 hanges when the sulphydryl modifying reagent methanethiosulfonate-ethylammonium (MTSEA) was applied.

87 nethiosulfonate ethylammonium (MTSEA(+)) and methanethiosulfonate ethylsulfonate (MTSES(-)) on wild-t

88 channels with methanethiosulfonate reagents (methanethiosulfonate ethylsulfonate (MTSES) and methanet

89 Labeling studies with methanethiosulfonate ethylsulfonate (MTSES) show that po

90 g loops, with N-[14C]ethylmaleimide (NEM) or methanethiosulfonate ethylsulfonate (MTSES) was studied

91 c reagents N-[(14)C]ethylmaleimide (NEM) and methanethiosulfonate ethylsulfonate (MTSES) which are pe

92 Studies with methanethiosulfonate ethylsulfonate (MTSES), a hydrophil

93 h membrane-impermeant thiol reagents such as methanethiosulfonate ethylsulfonate (MTSES).

94 sulfonate ethyltrimethylammonium (MTSET) and methanethiosulfonate ethylsulfonate (MTSES).

95 nium)ethyl]methanethiosulfonate (MTSET), and methanethiosulfonate ethylsulfonate (MTSES)] of mutants

96 Studies with methanethiosulfonate ethylsulfonate indicate that Cys re

97 storing the negative charge at position 518 (methanethiosulfonate ethylsulfonate modification of 518C

98 Methanethiosulfonate ethylsulfonate, an impermeant thiol

99 ionally, the smaller thiol-reactive reagent, methanethiosulfonate ethylsulfonate, reduced transport b

100 mmonium (MTSEA), but not membrane-impermeant methanethiosulfonate ethyltrimethylammonium (MTSET) and

101 ethanethiosulfonate ethylammonium (MTSEA) or methanethiosulfonate ethyltrimethylammonium (MTSET) and

102 Extracellular treatment with methanethiosulfonate ethyltrimethylammonium (MTSET) of a

103 .1 outer pore from permanent modification by methanethiosulfonate ethyltrimethylammonium (MTSET).

104 f the membrane-impermeant sulfhydryl reagent methanethiosulfonate ethyltrimethylammonium with the ext

105 ammonium pharmacophore of the agonist analog methanethiosulfonate-ethyltrimethylammonium would be in

106 beling by MTSET {[2-(trimethylammonium)ethyl]methanethiosulfonate} from both the cytoplasmic and extr

107 MTST could trap thiols through its methanethiosulfonate group to form the corresponding dis

108 hanethiosulfonate derivatives ((2-aminoethyl)methanethiosulfonate hydrobromide (MTSEA) and [(2-(trime

109 2-(Aminoethyl)methanethiosulfonate hydrobromide (MTSEA) failed to inhi

110 le to both outside and inside 2-(aminoethyl)-methanethiosulfonate hydrobromide (MTSEA) Further study

111 inding by the cysteine reagent 2-(aminoethyl)methanethiosulfonate hydrobromide (MTSEA) in membrane pr

112 sured in the presence of 2.5 mM 2-aminoethyl methanethiosulfonate hydrobromide (MTSEA) or 1 mM [2-(tr

113 2-(Aminoethyl)-methanethiosulfonate hydrobromide (MTSEA)-biotin labeled

114 ently covalently modified with (2-aminoethyl)methanethiosulfonate hydrobromide, a reagent that restor

115 substituted for D43 and T47) by 2-aminoethyl methanethiosulfonate in the GABAA alpha1 subunit loop G

116 sulfhydryl-specific chemical cross-linkers, methanethiosulfonates, inactivated the AcrB transporter

117 -reactive reagent 2-(trimethylammonium)ethyl methanethiosulfonate, indicating the location of candida

118 Exposure to ethylammonium methanethiosulfonate inhibited acetylcholine-induced cur

119 with the cysteine protease inhibitor, methyl methanethiosulfonate, inhibited both cleavage and enzyma

120 Propyl methanethiosulfonate is an anesthetic analog that covale

121 ved when the smaller labeling reagent methyl methanethiosulfonate is employed, suggesting that it ref

122 ET) method employing a novel, nonfluorescent methanethiosulfonate-linked acceptor that can be reversi

123 full inhibition of S359C by the impermeable methanethiosulfonate-linked probes must reflect an appro

124 this study, the reactivity between S-methyl methanethiosulfonate (MMTS) with persulfide was unambigu

125 The accessibility of Y67C to methanethiosulfonate modification indicated that its sid

126 vation of the receptor increased the rate of methanethiosulfonate modification of alpha(1)D62C and al

127 gamma-Aminobutyric acid (GABA) slowed methanethiosulfonate modification of alpha(1)F64C, alpha

128 [2-(Trimethylammonium)-ethyl]methanethiosulfonate modification of Cys-478 blocked sub

129 nd pentobarbital slowed N-biotinylaminoethyl methanethiosulfonate modification of T160C and D163C, in

130 the strongest influence on conductance from methanethiosulfonate modification, while leaving the sit

131 N-Biotinylaminoethyl methanethiosulfonate modified P174C-, R176C-, S177C-, V1

132 performed cysteine-scanning mutagenesis and methanethiosulfonate (MTS) accessibility studies on thes

133 P2X2(I328C) receptor was activated by propyl-methanethiosulfonate (MTS) as effectively as by ATP, but

134 The ability of sulfhydryl-specific alkyl methanethiosulfonate (MTS) compounds of different length

135 mutant receptors can be regulated by charged methanethiosulfonate (MTS) compounds.

136 delta, and kappa opioid receptors to charged methanethiosulfonate (MTS) derivatives and identified th

137 gle cysteine-substitution mutants with three methanethiosulfonate (MTS) derivatives.

138 With regard to methanethiosulfonate (MTS) inactivation of uptake, TM6a

139 The present study characterizes the methanethiosulfonate (MTS) inhibition profiles of 26 con

140 er (hSERT) proteins, we utilized the largely methanethiosulfonate (MTS) insensitive hSERT C109A mutan

141 ore rapidly modified by a negatively charged methanethiosulfonate (MTS) reagent, 2-sulfonatoethyl MTS

142 residues in subunit a with cysteine reactive methanethiosulfonate (MTS) reagents and Cd(2+).

143 Cytoplasmic-side methanethiosulfonate (MTS) reagents blocked K(+) permeat

144 positions (E54C/D58C) and tested a series of methanethiosulfonate (MTS) reagents for their effects on

145 We demonstrate that methanethiosulfonate (MTS) reagents form disulfide bonds

146 Here, we investigated CFTR's TM1 by applying methanethiosulfonate (MTS) reagents from both cytoplasmi

147 ere recorded before and after application of methanethiosulfonate (MTS) reagents in the resting, GABA

148 Intracellular application of certain charged methanethiosulfonate (MTS) reagents modified and irrever

149 Here we probed the reactivity toward methanethiosulfonate (MTS) reagents of channels with cys

150 rg(436) with Cys and examining the effect of methanethiosulfonate (MTS) reagents on gamma.

151 five predicted internal loops, reacted with methanethiosulfonate (MTS) reagents only when the plasma

152 Tethering thiol-reactive methanethiosulfonate (MTS) reagents onto alpha1K219C, be

153 Small, cysteine-specific methanethiosulfonate (MTS) reagents reacted with four TM

154 ccessibility mutagenesis and thiol-modifying methanethiosulfonate (MTS) reagents to further probe the

155 Methanethiosulfonate (MTS) reagents were used to modify

156 respectively, to inhibition by all the three methanethiosulfonate (MTS) reagents, I441C had >50% sens

157 2.59S which is relatively insensitive to the methanethiosulfonate (MTS) reagents, we mutated to cyste

158 re assayed for inhibition by thiol-reactive, methanethiosulfonate (MTS) reagents.

159 nd extracellularly placed positively charged methanethiosulfonate (MTS) reagents.

160 e extracellular side of M2, were modified by methanethiosulfonate (MTS) reagents.

161 end of the first transmembrane segment, with methanethiosulfonate (MTS) reagents.

162 agenesis and hydrophilic sulfhydryl-reactive methanethiosulfonate (MTS) reagents.

163 cessible to hydrophilic, membrane-impermeant methanethiosulfonate (MTS) reagents.

164 e permeation pathway that were reactive with methanethiosulfonate (MTS) reagents.

165 extracellularly and intracellularly applied methanethiosulfonate (MTS) reagents.

166 elix seven, C386 (C7.42), is reactive toward methanethiosulfonate (MTS) sulfhydryl labeling agents, a

167 before and after treatment with a variety of methanethiosulfonate (MTS)-based compounds, using voltag

168 secutive amino acids was performed against a methanethiosulfonate (MTS)-resistant background (C270A).

169 the sulfhydryl reagent, N-biotinylaminoethyl methanethiosulfonate (MTS).

170 ted cysteine to modification by 2-aminoethyl methanethiosulfonate (MTS-EA) in excised macropatches.

171 6)-tetramethylrhodamine)carboxylamino) ethyl methanethiosulfonate (MTS-TAMRA) cysteine-reactive reage

172 6)-tetramethylrhodamine)carboxylamino) ethyl methanethiosulfonate (MTS-TAMRA) revealed Thr-442 marks

173 (6)-tetramethylrhodamine)carboxylamino)ethyl methanethiosulfonate (MTS-TAMRA)) sulfhydryl reagents, 4

174 Methanethiosulfonates (MTS) are known to inactivate the

175 Membrane-impermeant methanethiosulfonates (MTS) inhibited bile acid transpor

176 Disulfide, bis(methanethiosulfonate) (MTS), and dibromobimane (DBB) cro

177 2-Aminoethyl methanethiosulfonate (MTSEA(+)) failed to modify Cd(2+)-

178 tion by the sulfhydryl reagents 2-aminoethyl methanethiosulfonate (MTSEA) and 2-(trimethylammonium)et

179 Pretreatment with (2-aminoethyl)methanethiosulfonate (MTSEA) inhibited [(3)H]diprenorphi

180 reased the rate of reaction of (2-aminoethyl)methanethiosulfonate (MTSEA) with X-A342C, the construct

181 ity to polar MTS derivatives [(2-aminoethyl)-methanethiosulfonate (MTSEA), [2-(trimethylammonium)ethy

182 ntrast, the smaller compound, 2-(aminoethyl) methanethiosulfonate (MTSEA), modified a position predic

183 rachloromercuribenzoic acid and 2-aminoethyl methanethiosulfonate (MTSEA), which share with ONOO(-) t

184 anethiosulfonate (MTSET), and (2-aminoethyl) methanethiosulfonate (MTSEA).

185 thiosulfonate reagents N-biotinoylaminoethyl methanethiosulfonate (MTSEA-biotin) and [2-(trimethylamm

186 the thiol oxidant 2-((biotinoyl)amino)ethyl methanethiosulfonate (MTSEA-biotin) and that electrophil

187 data received from the N-biotinylaminoethyl methanethiosulfonate (MTSEA-biotin) labeling of SERT on

188 N-biotinylaminoethyl methanethiosulfonate (MTSEA-biotin) reacts with cysteine

189 hydryl-specific reagent N-biotinylaminoethyl methanethiosulfonate (MTSEA-Biotin) was used to covalent

190 Treatment with sodium (2-sulfonatoethyl) methanethiosulfonate (MTSES) had no effect on hRFC activ

191 ibition mediated by sodium (2-sulfonatoethyl)methanethiosulfonate (MTSES) indicated that citrate conf

192 Two probes, the large [2-sulfonatoethyl]methanethiosulfonate (MTSES) molecule and permeant Au(CN

193 ification of the site with (2-sulfonatoethyl)methanethiosulfonate (MTSES) results in an enhanced resp

194 omide (MTSET), and sodium (2-sulfonatoethyl)-methanethiosulfonate (MTSES) similarly and profoundly in

195 on of the Y126C mutant by (2-sulfonatoethyl) methanethiosulfonate (MTSES)) hRFC monomers were express

196 anethiosulfonate reagents (2-sulfonatoethyl) methanethiosulfonate (MTSES), [2-(trimethylammonium)ethy

197 hiol-reactive anion sodium (2-sulfonatoethyl)methanethiosulfonate (MTSES), and the requirement for a

198 cysteine-specific reagent (2-sulfonatoethyl) methanethiosulfonate (MTSES), but only K84C was sensitiv

199 In addition, sodium (2-sulfonatoethyl) methanethiosulfonate (MTSES), used to irreversibly bind

200 methods (SCAM) with sodium (2-sulfonatoethyl)methanethiosulfonate (MTSES).

201 id) were both inhibited by (2-sulfonatoethyl)methanethiosulfonate (MTSES; 10-500 microm)-induced alka

202 ermeant reagent [2-(trimethylammonium)ethyl]-methanethiosulfonate (MTSET) and protected by substrate.

203 in HeLa cells by [2-(trimethylammonium)ethyl]methanethiosulfonate (MTSET) occurred much more readily

204 sition 380/449 by 2-(trimethylammonium)ethyl methanethiosulfonate (MTSET) proceeded at identical rate

205 permeant reagent [2-(trimethylammonium)ethyl]methanethiosulfonate (MTSET) to the replacement cysteine

206 with the reagent [2-(triethylammonium)ethyl]methanethiosulfonate (MTSET) which introduces five posit

207 lfonate (MTSES), [2-(trimethylammonium)ethyl]methanethiosulfonate (MTSET), and (2-aminoethyl) methane

208 bed with Hg(2+), [2-(trimethylammonium)ethyl]methanethiosulfonate (MTSET), and biotin-maleimide, appl

209 lfonate (MTSEA), [2-(trimethylammonium)ethyl]methanethiosulfonate (MTSET), and methanethiosulfonate e

210 ocytin (MPB) and [2-(trimethylammonium)ethyl]methanethiosulfonate (MTSET), have no effect.

211 [2-(Trimethylammonium)-ethyl]-methanethiosulfonate (MTSET), which attaches thiocholine

212 onate (MTSEA) and 2-(trimethylammonium)ethyl methanethiosulfonate (MTSET).

213 oreactive agent 2-((trimethylammonium)ethyl) methanethiosulfonate (MTSET).

214 modification by [2-(trimethylammonium)ethyl] methanethiosulfonate (MTSET+), which increases conductan

215 mechanism, we used the membrane-impermeable methanethiosulfonates, MTSET and MTS-TEAH, to modify Kir

216 at of MTSEA(+) or 3-(triethylammonium)propyl methanethiosulfonate (MTSPTrEA(+)), implying that qBBr(+

217 were subsequently modified with one of three methanethiosulfonate nitroxide reagents to introduce a s

218 protection of Cys148 in lactose permease, a methanethiosulfonate nitroxide spin-label was directed s

219 ethanethiosulfonate and N-biotinylaminoethyl methanethiosulfonate on the surface of intact cells.

220 ning effects of sulfhydryl-modifying agents (methanethiosulfonates) on 20 cysteine-substituted mutant

221 of alphaM1, which reacted with 2-aminoethyl methanethiosulfonate only in the presence of ACh, reacte

222 iosulfonate, positively charged 2-aminoethyl methanethiosulfonate, or 2-trimethylammonioethyl methane

223 2,2,5,5-tetramethyl-3-pyrrolidin-3-yl)methyl methanethiosulfonate] placed at three locations in the t

224 hiosulfonate, but not neutral 2-hydroxyethyl methanethiosulfonate, positively charged 2-aminoethyl me

225 be selectively and irreversibly inhibited by methanethiosulfonates presumably through conjugation to

226 In addition, methanethiosulfonate reaction rates were fastest for alp

227 er supported by [2-(trimethylammonium)ethyl]-methanethiosulfonate reactivity on the DAT E2C I159C.

228 lf-inhibition responses and the effects of a methanethiosulfonate reagent on channel currents in sing

229 ile cross-linking reaction of a bifunctional methanethiosulfonate reagent with pairs of cysteine resi

230 ng of M2 positions with an alcohol analog, a methanethiosulfonate reagent, further implicated residue

231 ion of intact cells with a novel fluorescent methanethiosulfonate reagent.

232 idues toward N-ethyl maleimide and a charged methanethiosulfonate reagent.

233 448 were tested for their sensitivity to the methanethiosulfonate reagents (2-sulfonatoethyl) methane

234 on of the cysteine-substituted channels with methanethiosulfonate reagents (methanethiosulfonate ethy

235 utated to cysteines and their sensitivity to methanethiosulfonate reagents (MTS) was tested.

236 nctional channel differentially sensitive to methanethiosulfonate reagents and cadmium, suggested tha

237 tituted cysteines to extracellularly applied methanethiosulfonate reagents and the rates of their mod

238 Positively charged methanethiosulfonate reagents derivatized alpha(1)F64C a

239 ltered the rates of cysteine modification by methanethiosulfonate reagents differently than GABA.

240 ation rate of these substituted cysteines by methanethiosulfonate reagents either in the presence or

241 Methanethiosulfonate reagents inhibited the activity of

242 open state, but Ag+ and sulfhydryl-specific methanethiosulfonate reagents modified the channels with

243 of zinc potentiation upon treatment with the methanethiosulfonate reagents N-biotinoylaminoethyl meth

244 Methanethiosulfonate reagents of different size and char

245 ACh increased the inhibition by methanethiosulfonate reagents of N170C and did not chang

246 Tethering chemically diverse thiol-reactive methanethiosulfonate reagents onto alpha(1)K219C and alp

247 Reaction with several methanethiosulfonate reagents potentiated currents to wi

248 Methanethiosulfonate reagents reacted with alpha(1)T60C,

249 ies of accessibility with positively charged methanethiosulfonate reagents suggest that the permeatio

250 bility of three hydrophilic, thiol reactive, methanethiosulfonate reagents to a library of 21 single-

251 ccessibility of hydrophilic, thiol-reactive, methanethiosulfonate reagents to a library of 68 indepen

252 eated with Cu(2+) ions or with bi-functional methanethiosulfonate reagents to catalyze cross-link for

253 ave been modified with a series of nitroxide methanethiosulfonate reagents to investigate the structu

254 cessibility of each single Cys mutant to two methanethiosulfonate reagents was evaluated by determini

255 ssibility of each single Cys mutant to three methanethiosulfonate reagents was evaluated by determini

256 Sensitivity to N-ethylmaleimide (NEM) and methanethiosulfonate reagents was localized to a membran

257 bited by incubation with sulfhydryl-specific methanethiosulfonate reagents, denoting their solvent ac

258 rt protein to hydrophilic, cysteine-specific methanethiosulfonate reagents, enabled identification of

259 ying the cysteine side chain with reversible methanethiosulfonate reagents.

260 in accessibility of substituted cysteines to methanethiosulfonate reagents.

261 t those two positions with variously charged methanethiosulfonate reagents.

262 utants in transmembrane domains 3 and 4 with methanethiosulfonate reagents.

263 the membrane-impermeant, sulfhydryl-specific methanethiosulfonate reagents.

264 of wild type (WT) and E53C GlyRs exposed to methanethiosulfonate reagents.

265 agents tested, including membrane impermeant methanethiosulfonate reagents.

266 hanol as well as reagents: mixed disulfides (methanethiosulfonate reagents: MTSET+, MTSES-) and an al

267 ethiosulfonate and 2-((biotinoyl)amino)ethyl methanethiosulfonate] reduced both ATP-evoked currents a

268 f alphaY198C by [3-(trimethylammonium)propyl]methanethiosulfonate resulted in irreversible activation

269 CFTR channels by [2-(trimethylammonium)ethyl]methanethiosulfonate resulted in the simultaneous modifi

270 itions tested) by [(trimethylammonium)methyl]methanethiosulfonate resulted only in irreversible inhib

271 However, propyl methanethiosulfonate reversibly inhibited cysteine-subst

272 hermore, labeling with N-biotinoylaminoethyl methanethiosulfonate showed that I66C was weakly reactiv

273 a negatively charged group [2-sulfonatoethyl methanethiosulfonate sodium salt (MTSES)] rescued the cG

274 find that the thiol modifying reagent methyl methanethiosulfonate specifically inhibits NO activation

275 the behavior of CM15 analogs labeled with a methanethiosulfonate spin label (MTSL) and a brominated

276 situ labeling of engineered cysteines with a methanethiosulfonate spin label (MTSL) with minimal back

277 We find that the methanethiosulfonate spin label can occasionally induce

278 in fusion peptide that has been labeled with methanethiosulfonate spin label.

279 -oxyl-2,2,5,5-tetramethylpyrroline-3-methyl)-methanethiosulfonate spin labels (MTSSL) bound to CaM mu

280 lysozyme (T4L) mutants, doubly labeled with methanethiosulfonate spin-label (MTSSL), have been studi

281 -resolution structures were obtained for the methanethiosulfonate spin-label derivatized to cysteines

282 ed the cysteine with the sulfhydryl-specific methanethiosulfonate spin-label, and used electron param

283 hree Ca(2+)-binding loops and labeled with a methanethiosulfonate spin-label.

284 tants of motifs II and III are accessible to methanethiosulfonates, suggesting that these segments ex

285 cient PK15 cells and probed with a series of methanethiosulfonate sulfhydryl-modifying reagents.

286 Furthermore, larger cysteine-reactive methanethiosulfonates [sulforhodamine-methanethiosulfona

287 te and the covalent attachment of benzocaine-methanethiosulfonate to a cysteine introduced in the ext

288 We also applied [2-(triethylammonium)ethyl] methanethiosulfonate to covalently modify the introduced

289 ility and reaction rate of propyl- and hexyl-methanethiosulfonate to cysteine residues introduced int

290 d MTSEA-biotinylation (N-Biotinoylaminoethyl methanethiosulfonate) to show ATP-sensitive accessibilit

291 Mutagenesis and methanethiosulfonate treatment are less effective at pos

292 Mutagenesis and methanethiosulfonate treatment are most effective at pos

293 brane-impermeant [2-(trimethylammonium)ethyl]methanethiosulfonate was able to access the inner pore f

294 ein showed that inhibition by ethylsulfonate methanethiosulfonate was blocked by substrate and that t

295 lly, 2-[(5-fluoresceinyl)aminocarbonyl]ethyl methanethiosulfonate was conjugated to a free cysteine o

296 the amount of inactivation by (2-aminoethyl)methanethiosulfonate was less than expected if the two f

297 ccess alkylator, 2-[(trimethylammonium)ethyl]methanethiosulfonate, was not effective in unmasking the

298 larly and intracellularly added 2-aminoethyl methanethiosulfonate, we previously located the closed g

299 of reduced PDI by N-ethylmaleimide or methyl-methanethiosulfonate, which abolished PDI oxidoreductase

300 dryl-specific, charged reagent, 2-aminoethyl methanethiosulfonate with cysteines substituted for resi