ライフサイエンスコーパス: disulphide

1 nt grain boundary reconstruction in tungsten disulphide.

2 ed sites in tungsten diselenide and tungsten disulphide.

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

4 aphene and few-layer semiconducting tungsten disulphide.

5 performance of vertically aligned molybdenum disulphide.

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

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

8 isulphide bonds or protein-glutathione mixed disulphides.

9 Zeeman effect in monolayer transition-metal disulphides.

10 that Ero1alpha is regulated by non-catalytic 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 RIalpha knock-in mice fully resistant to PKA disulphide-activation have deficient angiogenesis in mod

14 Disulphide-activation of PKA represents a new therapeuti

15 reacts with substrate proteins to form mixed disulphide adducts.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

42 Spx requires formation of an intramolecular disulphide bond between two cysteine residues that resid

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

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

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

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

47 While disulphide bond formation between the Cys residues of th

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 The disulphide bond pattern has been further altered by the

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

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

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

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

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

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

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

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

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

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

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

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

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

86 ription activation domain is stabilized by a disulphide bond.

87 between aromatic residues and by the single disulphide bond.

88 el fold, a new zinc-coordination motif and a disulphide bond.

89 o the correct and highly conserved C110-C187 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 hat reduction of intramolecular cbEGF domain disulphide bonds by homocysteine and the resulting disru

106 sis that homocysteine attacks intramolecular disulphide bonds causing reduction of cystine and domain

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

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

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

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

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

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

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

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

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

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

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

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

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

120 of them (at 584, 585, 588 and 589) can form disulphide bonds with counterparts from neighbouring sub

121 Formation of disulphide bonds within the mammalian endoplasmic reticu

122 597 of the S5-P linker can form intersubunit disulphide bonds, and at least four of them (at 584, 585

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

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

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

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

127 ogether by an extensive hydrophobic core and disulphide bonds.

128 long extracellular loops stabilized by four disulphide bonds.

129 ight chain polypeptides covalently linked by disulphide bonds.

130 products that help cells reduce cytoplasmic disulphide bonds.

131 the oxidation-reduction state of cytoplasmic disulphide bonds.

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

133 cleases evolved from a progenitor with three disulphide bonds.

134 l responses to protein antigens that contain disulphide bonds.

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

136 sent in hydrophobins and form intramolecular disulphide bonds.

137 more, the polymerization occurs only through disulphide bonds.

138 ully oxidised native protein containing four disulphide bonds.

139 phosphatase/sulphatase fold containing three disulphide bonds.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

155 critically linked by a conserved but labile disulphide bridge.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

170 which crosslink the cysteines with metal and disulphide bridges, respectively.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

188 se the effects of homocysteine on the native disulphide (cystine) bonds of these domains.

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

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

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

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

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

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

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

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

197 olymerisation of hydrated gluten proteins by disulphide exchange.

198 ential for normal peroxide-induced Tpx1-Sty1 disulphide formation and Tpx1-dependent regulation of pe

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

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

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

202 Disulphide formation in the endoplasmic reticulum (ER) i

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

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

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

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

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

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

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

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

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

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

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

214 Our results reveal that disulphide interactions enhance intracellular accumulati

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

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

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

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

229 all forms of PCSK9 co-localize with protein disulphide isomerase in the ER whether or not they can b

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

231 doplasmic reticulum luminal protein, protein disulphide isomerase.

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

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

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

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

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

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

238 ion under highly denaturing conditions of 5'-disulphide-linked conjugates of 3'-fluorescein labelled

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

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

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

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

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

244 PapC disulphide loop mutants were able to bind PapDG chaperon

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

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

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

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

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

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

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

252 2D materials including graphene, molybdenum disulphide (MoS2) and black phosphorus.

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

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

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

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

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

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

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

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

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

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

263 Thiol-disulphide oxidoreductases catalyse the formation or bre

264 mical characteristics typical of these flavo disulphide oxidoreductases.

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

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

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

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

269 This disulphide reducing system is present in Cryptococcus ne

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 able for survival of Bacillus subtilis under disulphide stress.

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

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

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

289 cine-rich repeat (LRR) domains, connected by disulphide-tethered linkers.

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,