ライフサイエンスコーパス: disulphide

1 performance of vertically aligned molybdenum disulphide.

2 on of the opto-electronic gain in molybdenum disulphide.

3 methyldithio)furan and bis(2-methyl-3-furyl) disulphide.

4 nt grain boundary reconstruction in tungsten disulphide.

5 ed sites in tungsten diselenide and tungsten disulphide.

6 -methyldithiofuran, and bis(2-methyl-3-furyl)disulphide.

7 aphene and few-layer semiconducting tungsten disulphide.

8 isulphide bonds or protein-glutathione mixed disulphides.

9 that Ero1alpha is regulated by non-catalytic disulphides.

10 Zeeman effect in monolayer transition-metal disulphides.

11 olecules on graphene ( 0.15 eV) and tungsten disulphide ( 0.24 eV).

12 large-area synthesis of monolayer molybdenum disulphide, a new two-dimensional direct-bandgap semicon

13 e successive folding, metal ion binding, and disulphide acquisition steps in this pathway can be cata

14 RIalpha knock-in mice fully resistant to PKA disulphide-activation have deficient angiogenesis in mod

15 Disulphide-activation of PKA represents a new therapeuti

16 reacts with substrate proteins to form mixed disulphide adducts.

17 stinosin is responsible for transporting the disulphide amino acid cystine from the lysosomal compart

18 hione) and oxidized (cystine and glutathione disulphide) aminothiols were quantified by high performa

19 roducers of sulphur compounds where dimethyl disulphide and dimethyl trisulfide were the most promine

20 fur compounds, namely methanethiol, dimethyl disulphide and dimethyl trisulphide.

21 amily are able to directly reduce this PrxIV disulphide and in the process become oxidized.

22 both I241C and I287C can spontaneously form disulphide and metal bridges with R362C, the position of

23 to maintain optimal redox ratios for CoA/CoA-disulphide and NAD(+) /NADH during periods of rapid repl

24 h of ultra-high-quality monolayer molybdenum disulphide appears a primary task for the community purs

25 he molybdenum-terminated edges of molybdenum disulphide are mainly responsible for its catalytic perf

26 Here we identify molybdenum disulphide as a promising cost-effective substitute for

27 In particular, using titanium disulphide as an encapsulation material, we demonstrate

28 E(m) = -290 mV) indicate that reduction of a disulphide at the CXXCH site of apocytochrome c (E(m) =

29 Two mutant CA proteins with engineered disulphides at different positions (P17C/T19C and N21C/A

30 trolled vapour phase synthesis of molybdenum disulphide atomic layers and elucidate a fundamental mec

31 boundaries in the polycrystalline molybdenum disulphide atomic layers are examined, and the primary m

32 ity and scalable synthesis of the molybdenum disulphide atomic layers.

33 support of this hypothesis, we demonstrated disulphide band formation between cysteines substituted

34 s that catalyse an activating intermolecular-disulphide between regulatory-RIalpha subunits of protei

35 hicker crystals such as monolayer molybdenum disulphide, bilayer graphene or multilayer hBN.

36 es that provide it with stability: a vicinal disulphide bond and a Ca(2+)-binding site (CBS).

37 ovided by its 2 structural elements (vicinal disulphide bond and CBS) is a key protective determinant

38 sis of residues involved in both the vicinal disulphide bond and the CBS to demonstrate that both of

39 , a combined mutant, T53C-T142C/T46P, with a disulphide bond at 53-142 and a proline substitution at

40 icating receptor function was inhibited by a disulphide bond between an A+ and an A- interface in bot

41 aracterized by the formation of an incorrect disulphide bond between C185 and C187, as opposed to the

42 crystallography structure of hBCATc showed a disulphide bond between C335 and C338.

43 onfirmed by the formation of a site-specific disulphide bond between TatC M205C and TatB L9C variants

44 m.), and the second elongating the substrate disulphide bond by 0.17 +/- 0.02 A (+/- s.e.m.).

45 be improved by reducing the intra and inter-disulphide bond by using appropriate reducing agents.

46 thiol-disulphide exchange, thus facilitating disulphide bond formation and rearrangement reactions.

47 eering cysteine residues into OtpA and using disulphide bond formation as a reporter of periplasmic l

48 o acids of the protein and is dependent upon disulphide bond formation between two conserved cysteine

49 Deleting either dsbA or dsbB or both reduces disulphide bond formation but does not entirely eliminat

50 xidoreductases, which are involved in native disulphide bond formation in the endoplasmic reticulum o

51 cts of overexpressing endogenous proteins on disulphide bond formation in the periplasm.

52 -43 cross-linking via cysteine oxidation and disulphide bond formation leading to decreased TDP-43 so

53 ore, we tested the hypothesis that incorrect disulphide bond formation might be a factor that affects

54 ic rhodanese, partially restores substantial disulphide bond formation to a dsbA strain.

55 higher turbidity, surface hydrophobicity and disulphide bond formation were obtained in NAM added wit

56 The transfer of reducing equivalents, from disulphide bond formation, to oxygen involves the partic

57 tself gets oxidized and proceeds to catalyse disulphide bond formation.

58 is reversibly inactivated by oxygen through disulphide bond formation.

59 fold and fail to fluoresce due to non-native disulphide bond formation.

60 , suggesting a requirement for regulation of disulphide bond formation/reduction during rod opsin bio

61 rod opsin biogenesis and supports a role for disulphide bond formation/reduction in rod opsin biogene

62 Whether such background disulphide bond forming activity is enzyme-catalysed is

63 system is not responsible for the background disulphide bond forming activity, we suggest that it mig

64 e show that ComEC contains an intramolecular disulphide bond in its N-terminal extracellular loop (be

65 Reduction of the seemingly inaccessible disulphide bond in the membrane-proximal alpha3 domain o

66 in-folding pathway is thought to introduce a disulphide bond into the haem-binding motif of apocytoch

67 This disulphide bond is believed to be reduced through a thio

68 An extracellular NCX1 disulphide bond is rapidly reduced by tris(2-carboxyethy

69 This activity depends on DsbC, the bacterial disulphide bond isomerase, but not on DsbB.

70 As formation of a disulphide bond most likely inactivates SpoVD activity,

71 e conformational switch upon cleavage of the disulphide bond of MtrC, but without concomitant increas

72 specifically reduces the Cys(155) -Cys(185) disulphide bond of S(C10) -Rnase, resulting in a signifi

73 The disulphide bond pattern has been further altered by the

74 Thioredoxins are enzymes that catalyse disulphide bond reduction in all living organisms.

75 hanical force in the range of 25-600 pN to a disulphide bond substrate and monitored the reduction of

76 ver, its release also requires cleavage of a disulphide bond suggesting that its activity is mediated

77 ation, this cysteine forms an intramolecular disulphide bond with a vicinal "backdoor" cysteine, a pr

78 hydroperoxides (OHPs) forms an intersubunit disulphide bond with residue C127'.

79 ovel helical fold, dependent on a structural disulphide bond, a structural feature consistent with th

80 slation of C127', formation of the C22-C127' disulphide bond, and alpha6-alpha6' helix-swapped reconf

81 t requiring a reorientation of the substrate disulphide bond, causing a shortening of the substrate p

82 uN2B ATD, by engineering of an inter-subunit disulphide bond, markedly decreases sensitivity to ifenp

83 translationally modified other than a single disulphide bond, raising the possibility that it might r

84 determined the structures of three different disulphide bond-trapped prepore intermediates.

85 o the correct and highly conserved C110-C187 disulphide bond.

86 onomer at a position that can be locked by a disulphide bond.

87 to a specific site on the receptor through a disulphide bond.

88 nger domain stalls due to the formation of a disulphide bond.

89 ription activation domain is stabilized by a disulphide bond.

90 h threonine that enables formation of stable disulphide-bond complexes with substrate proteins.

91 By introducing a new disulphide-bond in the protein product and also disrupti

92 state analyses led to the discovery that the disulphide-bond plays an important role in receptor bind

93 Finally, activation of TRPA1 by disulphide-bond-forming MTSEA is blocked by the reducing

94 Both reduced (active) and disulphide bonded (inactive) forms of IL-33 can be detec

95 this enzyme are mostly heavily glycosylated, disulphide bonded proteins.

96 at proteins that are flanked at both ends by disulphide-bonded caps that protect the hydrophobic core

97 hy allow us to distinguish between different disulphide-bonded species and to monitor the formation o

98 e partially restores secretion, showing that disulphide bonding contributes to the intracellular rete

99 ol oxidoreductases catalyse the formation of disulphide bonds (DSB) in extracytoplasmic proteins.

100 ysteine residues that were predicted to form disulphide bonds across the dimer interface.

101 gand-binding pocket and is stabilized by two disulphide bonds and a sodium ion.

102 has a globular structure stabilized by eight disulphide bonds and contains a deep open folate-binding

103 involves the formation and isomerisation of disulphide bonds and is catalysed by foldases in the lum

104 in structure on ATP binding, and introducing disulphide bonds between adjacent subunits to restrict i

105 Reduction of disulphide bonds enhanced both the EAI and ESI compared

106 VKOR and its homologues generate disulphide bonds in organisms ranging from bacteria to h

107 for ERp57 in the isomerisation of non-native disulphide bonds in specific glycoprotein substrates.

108 ption factor TcpP by inducing intermolecular disulphide bonds in the TcpP periplasmic domain.

109 li uses the DsbA/DsbB system for introducing disulphide bonds into proteins in the cell envelope.

110 ions that prevent the formation of incorrect disulphide bonds involving C185.

111 nt forms aberrant inter- and intra-molecular disulphide bonds involving the acquired Cys39 and the on

112 (Grxs) are small oxidoreductases that reduce disulphide bonds or protein-glutathione mixed disulphide

113 ealed a 63 amino acid residue peptide with 4 disulphide bonds that belongs to the three-finger toxin

114 ctases catalyse the formation or breakage of disulphide bonds to control the red-ox status of a varie

115 data demonstrate the importance of zinc and disulphide bonds to MCR-1 activity, suggest that assays

116 teine residues readily formed intermolecular disulphide bonds upon binding to the receptor complex, r

117 The SH groups were oxidized to disulphide bonds when higher chopping temperature was ap

118 Formation of disulphide bonds within the mammalian endoplasmic reticu

119 at Mpg1 hydrophobin variants, lacking intact disulphide bonds, retain the capacity to self-assemble,

120 f unstructured intermediates with one or two disulphide bonds, the majority of which then fold to for

121 a small, globular protein stabilized by two disulphide bonds, which is structurally related to aller

122 hannel TRPA1 via formation of amino-terminal disulphide bonds, which results in sustained calcium inf

123 ogether by an extensive hydrophobic core and disulphide bonds.

124 long extracellular loops stabilized by four disulphide bonds.

125 ight chain polypeptides covalently linked by disulphide bonds.

126 ised by an intricate, bespoke arrangement of disulphide bonds.

127 products that help cells reduce cytoplasmic disulphide bonds.

128 the oxidation-reduction state of cytoplasmic disulphide bonds.

129 phosphatase/sulphatase fold containing three disulphide bonds.

130 a CXXC motif that catalyses the reduction of disulphide bonds.

131 cleases evolved from a progenitor with three disulphide bonds.

132 l responses to protein antigens that contain disulphide bonds.

133 some, but not all, substrates with multiple disulphide bonds.

134 sent in hydrophobins and form intramolecular disulphide bonds.

135 more, the polymerization occurs only through disulphide bonds.

136 the formation of inter- and intra-molecular disulphide bonds.

137 reveals that Sdp1 employs an intramolecular disulphide bridge and an invariant histidine side chain

138 ns and a dimeric form with an intermolecular disulphide bridge between Cys67 and Cys187.

139 cium-binding site and to the vicinity of the disulphide bridge connecting with the light chain.

140 When oxidized, leptin contains a disulphide bridge creating a covalent-loop through which

141 Analyses of disulphide bridge energy and flexibility reflect the str

142 vitro reconstitution of vitamin K-dependent disulphide bridge formation.

143 With AZD1283 bound, the highly conserved disulphide bridge in GPCRs between helix III and extrace

144 its use of a [4Fe-4S] cluster and a proximal disulphide bridge in the conversion of a light signal in

145 al complexity within this motif created by a disulphide bridge in the long-chain helical bundle cytok

146 educed thioredoxin, which acts by breaking a disulphide bridge in the predicted extracellular loop ad

147 m of the FTR active site is free to attack a disulphide bridge in Trx and the other sulphur atom form

148 Cytochrome cL is unusual in having a disulphide bridge that tethers the long C-terminal exten

149 f the cysteine residues that probably form a disulphide bridge within Rpf impaired but did not comple

150 Optimal activity critically requires the disulphide bridge, and thus, to the best of our knowledg

151 resence of a solvent-exposed redox-sensitive disulphide bridge, unique among the subtilisin family, t

152 nd primes the protein for the formation of a disulphide bridge, which could be at the origin of the l

153 critically linked by a conserved but labile disulphide bridge.

154 Thus, the disulphide-bridge appears to function as a point of tens

155 Here we have used disulphide-bridge crosslinking to show that the loop at

156 le of the knotted topology introduced by the disulphide-bridge on leptin folding and function.

157 the C-terminal alpha-helix is shortened, the disulphide-bridge pattern altered and N and C termini se

158 amily, but with a unique modification of its disulphide-bridge scaffold.

159 receptor-binding sites, far removed from the disulphide-bridge.

160 cross-links were found to consist of 36% of disulphide bridges (compared to >75% in the absence of g

161 the predicted protein structure, a series of disulphide bridges and proline substitutions were create

162 nt, the former being characterized mainly by disulphide bridges and the latter by additional covalent

163 his provides the first genetic evidence that disulphide bridges in a hydrophobin are dispensable for

164 leaved into four subunits linked together by disulphide bridges in tube foot adhesive cells.

165 chain is pinned to the "Kunitz head" by two disulphide bridges not found in classical Kunitz/BPTI pr

166 Recombinant VEGF-A165-HBD that contains four disulphide bridges was expressed in specialised E. coli

167 concerning beta-structures, conformation of disulphide bridges, and aromatic amino acid environment,

168 of the protein fold, presence or absence of disulphide bridges, and secondary structure composition,

169 cellular environment by the formation of two disulphide bridges, resulting in an extensive conformati

170 oured, although these do not form intrasheet disulphide bridges.

171 We apply varying stretching force to the disulphide by incorporating it into a series of increasi

172 ationally that the reduction rate of organic disulphides by phosphines in water, which in the absence

173 membrane-anchored MICA form transitory mixed disulphide complexes from which soluble MICA is released

174 to thiocholine, which was oxidised to give a disulphide compound by dimerisation at 0.60V versus satu

175 o their oxidation to other compounds such as disulphide compounds which showed significant increase i

176 and 2748 IgG4 structures that satisfied the disulphide connectivity in their hinges.

177 furcation involving NADH, Fdox and the thiol/disulphide-containing DsrC.

178 four-disulphide structural domain [whey four disulphide core domain (WFDC)], WAP proteins are increas

179 ic activity, such as pyrite structure cobalt disulphide (CoS2), and substituting non-metal elements t

180 , whereas K8 G62C/R341C animals had aberrant disulphide cross-linked keratins.

181 isation and not hydrophobic interactions nor disulphide cross-links.

182 r conformation with a high-affinity toxin or disulphide crossbridge impedes the return of this voltag

183 lasmic cap but abolished a substrate-induced disulphide crosslink in transmembrane helix 5 of TatC.

184 me quaternary structure, indicating that the disulphide-crosslinked proteins recapitulate the structu

185 We previously used a disulphide crosslinking strategy to enable isolation and

186 The substitutions did not alter disulphide crosslinking to neighbouring TatC molecules f

187 The target analytes were diallyl disulphide (DADS), diallyl sulphide (DAS), diallyl trisu

188 n (2-VD), diallyl sulphide (DAS) and diallyl disulphide (DADS).

189 Dimethyl sulphide, dimethyl disulphide, dimethyl trisulphide 2-propylthiazole and 2-

190 nds present in onion essential oil; dipropyl disulphide, dipropyl sulphide and their mixture.

191 ve forms of OhrR can be reactivated by thiol-disulphide exchange reactions allowing restoration of re

192 may be higher levels of initiators for thiol-disulphide exchange reactions, resulting in an increase

193 ss, S-glutathionylation occurs through thiol-disulphide exchange with oxidized glutathione or reactio

194 PDI catalyses thiol-disulphide exchange, thus facilitating disulphide bond f

195 olymerisation of hydrated gluten proteins by disulphide exchange.

196 ive site for copper transfer, while delaying disulphide formation and complex dissociation.

197 In vivo rates of disulphide formation between diagnostic cysteine pairs s

198 ng helix in chemoreceptor Trg using rates of disulphide formation between introduced cysteines.

199 y PrxIV may therefore increase efficiency of disulphide formation by Ero1 and also allows disulphide

200 Disulphide formation in the endoplasmic reticulum (ER) i

201 disulphide formation by Ero1 and also allows disulphide formation via alternative sources of H(2)O(2)

202 ein ER oxidoreductin 1 (Ero1), which couples disulphide formation with reduction of oxygen to form hy

203 how oxidation by H(2)O(2) can be coupled to disulphide formation.

204 uced nanoindentation of monolayer molybdenum disulphide from a tailored nanopattern, and demonstrate

205 nd device properties of monolayer molybdenum disulphide grown by chemical vapour deposition.

206 ies of nanostructured flower-like molybdenum disulphide grown by hydrothermal route has been studied.

207 er molybdenum disulphide (MoS2) and tungsten disulphide, grown directly on insulating SiO2 substrates

208 redox pair glutathione (GSH) and glutathione disulphide (GSSG) forms the most important redox buffer

209 BD) on the glutathione (GSH) and glutathione disulphide (GSSG) molecules as the most important redox

210 oughout the enzootic cycle, to support thiol-disulphide homeostasis, and to indirectly protect the sp

211 ctive exfoliation of graphite and molybdenum disulphide in water mixtures with methanol, ethanol, iso

212 p the new prospect of using transition metal disulphides instead of conventional carbon-based materia

213 Our results reveal that disulphide interactions enhance intracellular accumulati

214 of lactoferrin during heating through thiol/disulphide interchange.

215 hich then fold to form the native-like three-disulphide intermediate, des-[77-95].

216 enous substrates for ERp57 by trapping mixed disulphide intermediates between enzyme and substrate.

217 the two-dimensional semiconductor molybdenum disulphide introduced a new optically active material po

218 Molybdenum disulphide is a layered transition metal dichalcogenide

219 Human protein disulphide isomerase (hPDI) is an endoplasmic reticulum

220 (ER) is catalysed by members of the protein disulphide isomerase (PDI) family.

221 on substance protein A (NusA), human protein disulphide isomerase (PDI), and the b'a' domain of PDI (

222 e response proteins GRP78 and GRP94, protein disulphide isomerase (PDI), homocysteine-inducible, endo

223 glucose-regulated protein (GRP) and protein-disulphide isomerase (PDI), which assist in the maturati

224 combined activities of Ero1alpha and protein disulphide isomerase (PDI).

225 for fertilization/transmission, and exhibits disulphide isomerase activity which is up-regulated post

226 In addition, we show that protein disulphide isomerase can catalyse the oxidative folding

227 amino acid 526 in close vicinity to a "CGLC" disulphide isomerase consensus sequence.

228 Conversely, over-expression of the disulphide isomerase DsbA increases the colistin MIC of

229 Here we describe a protein disulphide isomerase essential for malarial transmission

230 ERp57 is a member of the protein disulphide isomerase family of oxidoreductases, which ar

231 This study shows that protein disulphide isomerase provides a key component of these b

232 lled PDIA6 or P5), which, similar to protein disulphide isomerase, usually assists in the folding of

233 doplasmic reticulum luminal protein, protein disulphide isomerase.

234 the central part of the molecule (N-terminal disulphide knot, NDSK) resulted in strong interactions w

235 technique, using atomically thin molybdenum disulphide layers as a model material.

236 le formation in WPBs and template N-terminal disulphide linkage between VWF dimers, to form ultralong

237 Prevention of such disulphide linkage through the introduction of the Cys23

238 Less flexible spacers between the disulphide linkages and the helix will restrict each het

239 ies were undertaken to chemically modify the disulphide linkages present and to investigate the effec

240 Lactoferrin also formed disulphide-linked aggregates when it was heated with bet

241 ly cystatin to be synthesised as an inactive disulphide-linked dimeric precursor.

242 Upon oxidation of immature particles, a disulphide-linked Gag hexamer was formed, implying that

243 CD247 share high sequence homology and form disulphide-linked homodimers that contain a pair of acid

244 The levels of disulphide-linked whey proteins were higher in SM-ME tha

245 FimD disulphide loop and F4 mutants were able to bind chapero

246 PapC disulphide loop mutants were able to bind PapDG chaperon

247 ects in two-dimensional monolayer molybdenum disulphide may be responsible for large variation of ele

248 vestigated in this study and show that these disulphide-modified oligonucleotide probes offer signifi

249 asured as a function of force applied on the disulphide moiety yields a usefully accurate estimate of

250 ng to grain boundary migration in a tungsten disulphide monolayer.

251 emitters in tungsten diselenide and tungsten disulphide monolayers, emitting across a range of wavele

252 n a free-standing single layer of molybdenum disulphide (MoS(2)) and a measured piezoelectric coeffic

253 , other layered materials such as molybdenum disulphide (MoS(2)) have been investigated to address th

254 2D materials including graphene, molybdenum disulphide (MoS2) and black phosphorus.

255 A nanocomposite formed from molybdenum disulphide (MoS2) and graphene quantum dots (GQDs) was p

256 tal dichalcogenide family such as molybdenum disulphide (MoS2) and tungsten diselenide (WSe2), as wel

257 ch wafer-scale films of monolayer molybdenum disulphide (MoS2) and tungsten disulphide, grown directl

258 Two-dimensional (2D) molybdenum disulphide (MoS2) atomic layers have a strong potential

259 Ultrathin molybdenum disulphide (MoS2) has emerged as an interesting layered

260 lution reaction (HER; refs ,,,,), molybdenum disulphide (MoS2) is known to contain active edge sites

261 en demonstrated for the growth of molybdenum disulphide (MoS2) on insulating substrates, but to date,

262 the Fdx [2Fe-2S] cluster to the active-site disulphide of Trxs.

263 rmediate which reacts to form either a mixed-disulphide or a protein sulphenamide.

264 either prevents the formation of these mixed disulphides or resolves these adducts subsequently.

265 Thiol-disulphide oxidoreductases catalyse the formation or bre

266 We show that intrinsic defects in tungsten disulphide play an important role in this proximity effe

267 ion of point defects in monolayer molybdenum disulphide prepared by mechanical exfoliation, physical

268 The glutathione: glutathione disulphide ratio was also lower, showing increased oxida

269 e effects of the biologically relevant thiol-disulphide redox molecule, glutathione, and Zn2+-binding

270 indicated that it functioned as a coenzyme A disulphide reductase (CoADR) (specific activity approxim

271 The cdr gene encodes a coenzyme A disulphide reductase (CoADR) that reduces CoA-disulphide

272 is a nuclear-cytoplasmic pyridine nucleotide-disulphide reductase (PNDR).

273 not act as an apocytochrome c or c(1) CXXCH disulphide reductase in vitro.

274 which we show encodes an EDEM2/3-associated disulphide reductase.

275 framework for understanding the mechanism of disulphide reduction by an iron-sulphur enzyme and descr

276 ia coli, we show that a conserved N-terminal disulphide region of the PapC and FimD ushers, as well a

277 his enzyme was specific for coenzyme A (CoA) disulphide, required NADH and had no significant activit

278 present a new member of the family, rhenium disulphide (ReS2), where such variation is absent and bu

279 c residues and the transmembrane pore lies a disulphide-rich 'thumb' domain poised to couple the bind

280 membrane helices, a bound chloride ion and a disulphide-rich, multidomain extracellular region enrich

281 g transistors where two-dimensional tungsten disulphide serves as an atomically thin barrier between

282 sulation, while the pyrazines, thiazoles and disulphides showed opposite trend.

283 We uncover that molybdenum disulphide shows superior carbon dioxide reduction perfo

284 e family of bacteria and is regulated by the disulphide stress-response sigma factor, sigma(R), in St

285 y an evolutionarily conserved canonical four-disulphide structural domain [whey four disulphide core

286 e structural plasticity of the immature SOD1 disulphide sub-loop, a characteristic which contributes

287 omplexation specifically stabilises the SOD1 disulphide sub-loop, priming it and the active site for

288 h exceptional strength, monolayer molybdenum disulphide subjected to biaxial strain can embed wide ba

289 nd had no significant activity against other disulphides, such as oxidized glutathione or thioredoxin

290 The structure shows that a disulphide-tethered Rad4 flips out normal nucleotides an

291 ing two-dimensional layered transition metal disulphides that possess a combination of high conductiv

292 an electronic phase transition in molybdenum disulphide, there has been a lack of experimental eviden

293 isulphide reductase (CoADR) that reduces CoA-disulphides to CoA in an NADH-dependent manner.

294 lying that the redox potential for the thiol/disulphide transition in gamma(2) is substantially highe

295 crystalline islands of monolayer molybdenum disulphide up to 120 mum in size with optical and electr

296 ctural properties of multilayered molybdenum disulphide up to 35 GPa.

297 ion potential (E degrees') of the regulatory disulphides was calculated to be approximately -275 mV m

298 The stable regulatory disulphides were only partially reduced by PDI (E degree

299 Single-layered molybdenum disulphide with a direct bandgap is a promising two-dime

300 activity of PrxIV depends on reduction of a disulphide within the active site to form a free thiol,