ライフサイエンスコーパス: disulfide

1 n spectra of a bare bilayer MoS2 (Molybdenum disulfide).

2 de, heptafluoroisopropyl iodide and diphenyl disulfide.

3 veral modifications, including an engineered disulfide.

4 c response of synthetic monolayer molybdenum disulfide.

5 g(-1) capacity based on the mass of titanium disulfide.

6 um monochloride cations in expanded titanium disulfide.

7 hiolated mixed disulfides and intramolecular disulfides.

8 bumin that displays 17 structurally relevant disulfides.

9 oxygen atmosphere yielding the corresponding disulfide analogue (disulfide-BPI).

10 , we further stabilized pre-F by adding both disulfide and cavity-filling mutations (DS-Cav1), and we

11 lectric tensors of nanometer-thin molybdenum disulfide and hexagonal boron nitride microcrystals, the

12 Dimethyl disulfide and methyl thioacetate were important precurso

13 We followed the isomerization of the SU-TM disulfide and subsequent SU release from Env with bioche

14 s the BG505 DS-SOSIP variant, comprising two disulfides and an Ile-to-Pro mutation of Env from strain

15 bly genuine examples of cis or trans vicinal disulfides and discuss their conformations, conservation

16 ge mechanism to reduce S-mycothiolated mixed disulfides and intramolecular disulfides.

17 Taking into account the steady state between disulfides and thiols in all living cells, the collapse

18 ation of glutathione persulfide, glutathione disulfide, and H2S.

19 Some vicinal disulfides are essential to large, functionally coupled

20 zed, but our understanding of how non-native disulfides are reduced so that the correct or native dis

21 ransfer reducing equivalents from flavins to disulfides as in NTRs but functions in the opposite dire

22 Vicinal disulfides between sequence-adjacent cysteine residues a

23 complex and is very likely involved in thiol-disulfide biochemistry at the thylakoid membrane.

24 y of N297G, we introduced a novel engineered disulfide bond at a solvent inaccessible location in the

25 tion activity is completely dependent on the disulfide bond between the two conserved cysteines.

26 g rate constant changed upon deletion of the disulfide bond by 10 orders of magnitude, from approxima

27 tivation involves reduction of an allosteric disulfide bond by thioredoxin-1 (TRX), but cellular and

28 Three cysteine residues and one disulfide bond conserved within known alpha-amylase inhi

29 The disulfide bond cross-link caused a >/=95% loss of cytoch

30 Thus, DsbB generates a protein disulfide bond de novo by transferring electrons to the

31 Rapid disulfide bond formation and cleavage is an essential me

32 nction; therefore, the enzymes that catalyze disulfide bond formation are involved in multiple biolog

33 Accurate and efficient disulfide bond formation can be vital for protein functi

34 nd the distinct biological settings in which disulfide bond formation can take place belie the simpli

35 h beta-mercaptoethanol, resulting in reduced disulfide bond formation in inositol 1, 4, 5-trisphospha

36 In conclusion, disulfide bond formation in oral bacteria is an emerging

37 es on hydrophobic packing, metal binding, or disulfide bond formation in the protein core.

38 reciating the mechanisms and consequences of disulfide bond formation in vivo by reviewing chemical p

39 We show that disulfide bond formation inhibits filament assembly and

40 oplasm, and this copper-induced mechanism of disulfide bond formation obviates the need for a thiol/d

41 Of relevance, the disulfide bond formation was much slower in Prx2 (k3 = 0

42 Dimerization of BslA, mediated by disulfide bond formation, depends on two conserved cyste

43 Activation by R655C did not require disulfide bond formation.

44 Moreover, introduction of a disulfide bond in the bridging sheet region further stab

45 enzyme in close proximity to an intersubunit disulfide bond interactions that covalently link thioest

46 hia coli, and for some of these proteins the disulfide bond is critical to their stability and functi

47 A disulfide bond is easily formed between the monomers of

48 tic cysteine, and finally, the rate-limiting disulfide bond is formed.

49 One protein found to contain a disulfide bond is the essential cell division protein Ft

50 results strongly suggest that FtsN lacking a disulfide bond is unstable, thereby making this disulfid

51 mprising an N-terminal catalytic domain (LC) disulfide bond linked to a C-terminal heavy chain (HC) w

52 Assembly is triggered by the formation of a disulfide bond linking two tailpieces.

53 domain is non-essential, suggesting that the disulfide bond might also be dispensable.

54 -rich peptides and the influence of a fourth disulfide bond on insulin bioactivity.

55 s, suggesting a toxin-intrinsic mechanism of disulfide bond reduction and alpha/beta heterodimer diss

56 We found that the disulfide bond stabilizes self-complemented DraE (DraE-s

57 pathway involving CcmG and CcmH reduces this disulfide bond to allow covalent heme ligation.

58 Remarkably, the introduction of a non-native disulfide bond was critical for formation of beta-hairpi

59 te that eventually resolves to form the Sod1 disulfide bond with concomitant release of copper into t

60 tant of TRX, which formed a metastable mixed disulfide bond with TG2, we demonstrated that these prot

61 etween gp120 and gp41, an engineered 201-433 disulfide bond, and density corresponding to 22 N-glycan

62 olium-carbenes preferentially react with the disulfide bond, but not thiol group.

63 We previously identified a disulfide bond, I201C-A433C (DS), which stabilizes Env i

64 Through the introduction of a disulfide bond, we succeeded in arresting the enzyme ade

65 roteolytic fragments linked by more than one disulfide bond, we used electron transfer dissociation (

66 glycolide) polymeric core by redox-sensitive disulfide bond, while TET was physically capsulated spon

67 redox-responsiveness was achieved by using a disulfide bond-based crosslinker.

68 ucture-activity relationship (SAR) study, 25 disulfide bond-containing analogues were synthesized and

69 suited for studying the interactions between disulfide bond-folded proteins in the bacterial cytoplas

70 r simulations revealed that unfolding of the disulfide bond-lacking variant is initiated by strands A

71 C-terminus of mature human TRAIL leads to a disulfide bond-linked homotrimer which can be expressed

72 iant is initiated by strands A or G and that disulfide bond-mediated joining of strand A to the core

73 Sod1 is the predominant disulfide bond-requiring enzyme in the cytoplasm, and th

74 ing the oxidation of the Sod1 intramolecular disulfide bond.

75 and conopeptides, which have no or only one disulfide bond.

76 re we show that the expression levels of the disulfide-bond A oxidoreductase-like protein (DsbA-L) ar

77 lding in the ER requires core glycosylation, disulfide-bond formation and proline isomerization.

78 We conclude that in the cell, MAL is not disulfide-bonded and requires glutathionylation of C91 f

79 cturally stable and biologically active as a disulfide-bonded heterodimer, whereas it forms inactive

80 Pertussis-like toxins are secreted as disulfide-bonded heterohexamers in which the catalytic A

81 onded heterodimer, whereas it forms inactive disulfide-bonded oligomers at neutral pH that are caused

82 is structural difference, both two and three disulfide-bonded peptides drove proliferation of a human

83 gation behavior is the diminished ability of disulfide-bonded RRM2 dimers to refold and their increas

84 otein FimG from Gram-negative bacteria and a disulfide-bonded variant of the I91 human cardiac titin

85 isulfide-bonded) peptide, or when the double disulfide-bonded Wnt peptide contained Ala substituted f

86 th DTT, and did not occur with a linear (non-disulfide-bonded) peptide, or when the double disulfide-

87 easy identification of peptides involved in disulfide bonding from nonreduced proteolytic digests, d

88 facilities are currently lacking to include disulfide bonding in the MD models of protein folding.

89 Here, we use genetic tethering and disulfide bonding strategies to construct HslU pseudohex

90 Streptococcus gordonii, the ability to form disulfide bonds affected autolysis, extracellular DNA re

91 ells, probably secondary to the formation of disulfide bonds among Ca(2+) signaling-related proteins.

92 nds in human serum albumin, including nested disulfide bonds and motifs of adjacent cysteine residues

93 immunoblots, binding was dependent on intact disulfide bonds and N-glycans, and only two antibodies r

94 ingly, these 2 products remained linked with disulfide bonds and presented as a dimerized form, TSLP

95 ive bacteria, such as Enterococcus faecalis, disulfide bonds are formed in secreted bacteriocins and

96 Disulfide bonds are found in many proteins associated wi

97 isulfide mapping is challenged when multiple disulfide bonds are present in complicated patterns.

98 oral bacteria, the enzymes that catalyze the disulfide bonds are quite diverse and share little seque

99 Once inside the cell, the disulfide bonds are reduced to produce a linear, biologi

100 , and results in formation of intermolecular disulfide bonds between conserved cysteine residues in n

101 Notably, introducing disulfide bonds between subdomains SD2 and SD3 modulated

102 , underscoring the importance of considering disulfide bonds both computationally and experimentally

103 ctroscopy confirms the proposed mechanism of disulfide bonds breaking to form a S-Li thiolate species

104 Our results show that disulfide bonds can alter the mechanical stability of pr

105 Disulfide bonds contribute to protein stability, activit

106 r dissociation (ETD) to partially dissociate disulfide bonds followed by high-energy collisional diss

107 nstrating that NAC was efficient in reducing disulfide bonds in circulating VWF multimers.

108 rce spectroscopy (smFS) to study the role of disulfide bonds in different mechanical proteins in term

109 four disulfide bonds in lysozyme and all 17 disulfide bonds in human serum albumin, including nested

110 e basis of these findings, we identified the disulfide bonds in IL-12alpha that are critical for asse

111 demonstrated by complete mapping of all four disulfide bonds in lysozyme and all 17 disulfide bonds i

112 This includes the presence of disulfide bonds in nested patterns and closely spaced cy

113 In summary, our results indicate that disulfide bonds in proteins act in a context-dependent m

114 gy for TTP, as it was demonstrated to reduce disulfide bonds in VWF, thereby decreasing VWF multimers

115 Mapping of disulfide bonds is an essential part of protein characte

116 Peptides that contained only two native disulfide bonds lack the characteristic granulin beta-ha

117 Reduction of the disulfide bonds led to a marked increase in charge state

118 these nucleases and lacks the characteristic disulfide bonds of the superfamily.

119 structure, little is known about the role of disulfide bonds on DNA condensation in the mammalian spe

120 The released PDI reduces disulfide bonds on plasma vitronectin, enabling vitronec

121 The effect of internal disulfide bonds on the extent of supercharging was probe

122 Disulfide bonds play a crucial role in proteins, modulat

123 s an emerging field, and the ability to form disulfide bonds plays an important role in dental plaque

124 The prevalent in vivo strategy to form disulfide bonds requires the presence of dedicated enzym

125 l bonds such as hydrophobic interactions and disulfide bonds than those at 5 degrees C for 6min.

126 The identification of essential disulfide bonds that underlie this process lays the basi

127 ring peptides and proteins often use dynamic disulfide bonds to impart defined tertiary/quaternary st

128 nas gingivalis and Tannerella forsythia, use disulfide bonds to stabilize their outer membrane porin

129 Unambiguous mapping of such disulfide bonds typically requires advanced MS approache

130 indicated both hydrophobic interactions and disulfide bonds were significantly enhanced during gelat

131 en Cys residues in murine Meteorin form five disulfide bonds with Cys7 (C1) linked to Cys28 (C2), Cys

132 s accelerated by the disruption of conserved disulfide bonds within the substrate.

133 nistic links (with loops closed, e.g. by two disulfide bonds), links formed probabilistically and mac

134 a conserved set of eight Cys residues (four disulfide bonds), whereas C6 evasins have only three of

135 , which are short polypeptides stabilized by disulfide bonds, and conopeptides, which have no or only

136 re engineer E dimers locked by inter-subunit disulfide bonds, and show by X-ray crystallography and b

137 d cysteine residues that form intramolecular disulfide bonds, are a family of mucin-associated secret

138 d cells via cysteine-mediated intermolecular disulfide bonds, leading to receptor dimerization.

139 d H2O2-induced IP3R1 dysfunction by reducing disulfide bonds, rather than quenching ROS.

140 tensibility lies in the presence of covalent disulfide bonds, which significantly enhance protein sti

141 ansiently interacts with CHCHD4 and acquires disulfide bonds.

142 these confirmed the formation of engineered disulfide bonds.

143 me, each of which contains multiple internal disulfide bonds.

144 re but, instead, misfolds, forming incorrect disulfide bonds.

145 whereas C6 evasins have only three of these disulfide bonds.

146 n cells frequently requires the insertion of disulfide bonds.

147 elding the corresponding disulfide analogue (disulfide-BPI).

148 onomer in redox communication with an active disulfide bridge in a variant of the fold adopted by NTR

149 onent of a low-density lipoprotein through a disulfide bridge to form lipoprotein(a).

150 facilitates the detailed characterization of disulfide-bridged peptides by mass spectrometry.

151 Subsequently, reductant is removed and all disulfide bridges are reoxidized to reform covalent inte

152 Because of this, ZmTrxh is unable to reduce disulfide bridges but possesses a strong molecular chape

153 tion, resulting in formation of adventitious disulfide bridges in cell proteins.

154 Surprisingly, two of the three disulfide bridges in IL-12alpha are dispensable for IL-1

155 a 35-amino acid peptide cross-linked by two disulfide bridges named tau-AnmTX Ms 9a-1 (short name Ms

156 AtSLP2 and is dependent on the formation of disulfide bridges on AtSLP2.

157 Nature uses interchain disulfide bridges to stabilize collagen trimers.

158 y of dendrimers displaying internally queued disulfide bridges were synthesized and exploited as flaw

159 ins and is shown to be fully compatible with disulfide bridges, as evidenced by the selective modific

160 Engineered disulfide bridges, computationally predicted to interfer

161 ompartments generally rely on intramolecular disulfide bridging to maintain conformation (e.g., album

162 ducing conditions, the cysteines do not form disulfides, but under oxidizing conditions they are high

163 es are reduced so that the correct or native disulfides can form is poor.

164 yzes the rapid reduction of the redox-active disulfide center of the antioxidant protein peroxiredoxi

165 report that the interplay between reversible disulfide chemistry and self-assembly can give rise eith

166 ntly thio-Michael chemistry to predominantly disulfide chemistry, as well as to any intermediate stat

167 Using PDI variants that form mixed disulfide complexes with their substrates, we identify b

168 Constrained by the disulfide, conformational selection between weak and tig

169 four cysteines that can have three possible disulfide connectivities: globular (Cys(I)-Cys(III) and

170 ing the epitope maps of diverse mAbs and the disulfide connectivity underlying E1E2 native conformati

171 difficult to produce, owing to their complex disulfide connectivity.

172 is not just capable of dissolving thiol- and disulfide-containing compounds, but is able to chemicall

173 rolones (DTPs) are an underexplored class of disulfide-containing natural products, which exhibit pot

174 digests, due to the concurrent detection of disulfide-containing peptide species and their composing

175 Disulfide-cored peptide dendrons featuring carbomethoxy

176 ulfide bond is unstable, thereby making this disulfide critical for function.

177 a phytofirmans coupled with structure-guided disulfide cross-linking in P. aeruginosa suggest that Pe

178 angular trimers are stabilized through three disulfide cross-links between the monomer subunits.

179 Hydrogen-deuterium exchange, disulfide crosslinking and molecular dynamics studies su

180 ere has the goal of examining whether carbon disulfide (CS2) may play a role as an endogenously gener

181 ntified the presence of different species of disulfide-dependent TDP-43 aggregates in cortex and spin

182 n equilibrium with the corresponding thiuram disulfide dimer.

183 we have termed DO peptides, are involved in disulfide-dithiol exchange reaction, resulting in format

184 f proteins that are known to form non-native disulfides during their folding.

185 by Glu47-carboxylate and (ii) a second thiol-disulfide exchange between the Cys56-thiolate and the mi

186 protein disulfide isomerase (PDI) and thiol-disulfide exchange is mostly enthalpy-driven (entropy ch

187 We also found that Rv2466c uses a monothiol-disulfide exchange mechanism to reduce S-mycothiolated m

188 addition of Osm1 and fumarate completes the disulfide exchange pathway that results in Tim13 oxidati

189 recruit/release monomeric RRM2 through thiol-disulfide exchange reactions.

190 reaction proceeds in two stages: (i) a thiol-disulfide exchange through nucleophilic attack of the Cy

191 the Gibbs energy barrier of the first thiol-disulfide exchange.

192 uctural and electronic control of molybdenum disulfide foam to synergistically promote the hydrogen e

193 The optimized three-dimensional molybdenum disulfide foam with uniform mesopores, vertically aligne

194 lic attack of the Cys53-thiolate to the GSSG-disulfide followed by the deprotonation of Cys56-thiol b

195 The pathways for disulfide formation are well characterized, but our unde

196 In conclusion, disulfide formation at Cys(43) does not directly activat

197 the ER, which is required to ensure correct disulfide formation in proteins entering the secretory p

198 at folding of the polypeptide chain precedes disulfide formation within a cellular context and highli

199 ship between protein synthesis, folding, and disulfide formation within the endoplasmic reticulum (ER

200 iverse players in intracellular pathways for disulfide formation, and the distinct biological setting

201 t within the ER, that is, protein folding or disulfide formation, we studied folding events at the ea

202 ersely, that protein folding occurs prior to disulfide formation.

203 ns were carried out on both its aromatic and disulfide forming amino acids.

204 ormations of organic compounds (e.g., carbon disulfide, halogenated organic compounds).

205 S being incapable of sensing H2O2 Similarly, disulfide heterodimer formation was abolished in H9C2 ce

206 d with de novo brain and blood generation of disulfide high mobility group box 1 (HMGB1), a neuroinfl

207 le and liver regeneration via CXCR4, whereas disulfide HMGB1 and its receptors TLR4/MD-2 and RAGE (re

208 uced reduction of oxidative stress prevented disulfide HMGB1 generation, thus highlighting a potentia

209 animal data, we observed early expression of disulfide HMGB1 in patients with newly diagnosed epileps

210 The pathologic disulfide HMGB1 isoform progressively increased in blood

211 the NAD(+)-binding site by an intramolecular disulfide in the oxidized state dissociate upon the redu

212 activity of therapeutic proteins containing disulfides in their structures.

213 the significant reduction in the sulfhydryl-disulfide interchange reaction during denaturation of be

214 nge between the Cys56-thiolate and the mixed disulfide intermediate formed in the first step.

215 heory level is a requisite to form the mixed disulfide intermediate.

216 ers led to selective formation of the ribbon disulfide isomer without requiring orthogonal protection

217 The human protein disulfide isomerase (hPDI), is an essential four-domain

218 hours in this model was dependent on protein disulfide isomerase (PDI) and TF expression by myeloid c

219 s also suggest that the catalysis by protein disulfide isomerase (PDI) and thiol-disulfide exchange i

220 Thiol isomerases such as protein-disulfide isomerase (PDI) direct disulfide rearrangement

221 Protein-disulfide isomerase (PDI) is a ubiquitous dithiol-disulf

222 C1 interacts with the oxidoreductase protein-disulfide isomerase, we hypothesized that thioredoxin-1

223 ncing vector in maize indicated that protein disulfide isomerase-like and phosphoglycerate kinase wer

224 tion in the ER lumen is prevented by protein disulfide isomerase.

225 Protein disulfide isomerases (PDIs) support endoplasmic reticulu

226 cond K1-K10-2B heterodimer via a Cys401(K10) disulfide link, although the bond angle is unanticipated

227 ntified several pockets, one adjacent to the disulfide linkage and conserved in K5-K14.

228 r agonistic IL-1beta signaling, and that the disulfide linkage indirectly affects signaling by blocki

229 to POEG-b-PCCDas micelles, incorporation of disulfide linkage into POEG-b-PSSDas micelles facilitate

230 A disulfide linkage is present in IL1RN, but is not in IL-

231 We studied whether the disulfide linkage plays a role in agonistic action of IL

232 Meteorin and Cometin, it is likely that the disulfide linkages are also conserved.

233 nal groups in proteins, and their pairing in disulfide linkages is a common post-translational modifi

234 collisional dissociation (HCD) to determine disulfide linkages.

235 -selectin as a monomer (sP-selectin) or as a disulfide-linked dimer fused to the Fc portion of mouse

236 that only some human and mouse Siglecs form disulfide-linked dimers.

237 The pre-TCR is a disulfide-linked heterodimer composed of an invariant pr

238 r-a-specific mAb, we characterize Clr-a as a disulfide-linked homodimeric cell surface glycoprotein.

239 show that although both VKOR and VKORL form disulfide-linked oligomers, the cysteine residues involv

240 longed antigen presentation when compared to disulfide-linked peptide.

241 pseudohexamers with six active subunits, but disulfide-linked pseudohexamers do not have these defect

242 ous studies have suggested that pre-existing disulfide links are absolutely required to allow protein

243 One conformation closely resembled the "disulfide-locked" Rgg2Sd secondary and tertiary structur

244 Mutation of the cysteines forming the disulfide loop of the platelet GPIbalpha adhesive A1 dom

245 However, MS-based disulfide mapping is challenged when multiple disulfide

246 activate TP053, preferentially via a dithiol-disulfide mechanism.

247 h as methanethiol, diethyl sulfide, dimethyl disulfide, methional and dimethyl trisulfide, in contrib

248 Compounds bearing disulfide moiety can directly interact with glutathione

249 ked hydrogels from defect-rich 2D molybdenum disulfide (MoS2 ) nanoassemblies and polymeric binder is

250 The emerging molybdenum disulfide (MoS2 ) offers intriguing possibilities for re

251 nd basal-plane sites of monolayer molybdenum disulfide (MoS2 ) synthesized by chemical vapor depositi

252 large area growth of high quality molybdenum disulfide (MoS2) and other types of 2D dichalcogenides.

253 heets of two-dimensional metallic molybdenum disulfide (MoS2) on thin plastic substrates can generate

254 created on the basal plane of 2H-molybdenum disulfide (MoS2) using argon plasma exposure exhibited h

255 key to anisotropic silica coating, with the disulfide, not the thiol, leading to side silica coating

256 tal and computational studies suggest that a disulfide-olefin charge-transfer complex is possibly res

257 njugated to nanoparticles utilizing either a disulfide or a thioether linkage.

258 Immunization with either disulfide or thioether linked vaccine constructs effecti

259 bond formation obviates the need for a thiol/disulfide oxidoreductase in that compartment.

260 fide isomerase (PDI) is a ubiquitous dithiol-disulfide oxidoreductase that performs an array of cellu

261 l cis-proline, signature features of a thiol-disulfide oxidoreductase.

262 gative bacteria carry genes coding for thiol-disulfide oxidoreductases in their genomes.

263 ides stems from their (moderate) activity as disulfide oxidoreductases.

264 oth "left-arm" and "right-arm" HL interchain disulfide peptides and observed that native HL pairing w

265 ess restrained through mutation, loss of the disulfide preferentially diverts binding through an indu

266 as protein-disulfide isomerase (PDI) direct disulfide rearrangements required for proper folding of

267 cts included Cys34 oxidation products, mixed disulfides, rearrangements, and truncations.

268 as influencing metabolic pathways and thiol/disulfide redox balance.

269 and quantify the energetics of the cysteine disulfide redox-reaction (reversible potentials for both

270 rane complex, a cell-permeable intracellular disulfide-reducing drug, slowed the onset and velocity o

271 henotype could be reproduced by intra-axonal disulfide reduction in wild-type axons and reversed by e

272 Cyclotides are ultra-stable cyclic disulfide-rich peptides from plants.

273 Here, we demonstrate that Hi1a, a disulfide-rich spider venom peptide, is highly neuroprot

274 us biotransmitter hydrogen sulfide (H2S) and disulfides (RSSR) and/or sulfenic acids (RSOH).

275 a technology based on cell-penetrating poly(disulfide)s that solves this problem: we deliver about 7

276 st potent aroma components include: dipropyl disulfide, S-propyl thioacetate, dimethyl trisulfide, 1-

277 ion, using mass spectrometry combined with a disulfide searching algorithm DBond.

278 ted Si/graphene anode paired with a selenium disulfide (SeS2) cathode with high capacity and long-ter

279 As a result of disulfide shuffling in its terminal domains, hPDI exists

280 ugh a palmitoylated N-terminal "thumb" and a disulfide-stabilized C-terminal "index finger," yet how

281 ribe a Pap1-Oxs1 pathway for diamide-induced disulfide stress in Schizosaccharomyces pombe, where the

282 This disulfide structure information should facilitate struct

283 We demonstrate a novel crosslinked disulfide system as a cathode material for Li-S cells th

284 nd that in the absence of the intermolecular disulfide, the Rgg2Sd dimer interface is destabilized an

285 can be oxidized into catalytically inactive disulfides, the isomerization rates can be controlled vi

286 r, the wide variety of proteins that contain disulfides, the profound impact of cross-linking on the

287 Complex 6 represents the first alkyl disulfide thorium species and illustrates the ability of

288 uctural probes from radiolytic footprinting, disulfide trapping, and mutagenesis to map the structure

289 s-alkylation of cysteine residues present as disulfides under mild and biocompatible conditions.

290 t-generation "sulflower." In this novel PAH, disulfide units establish an all-sulfur periphery around

291 the release of dimethyl sulfide and dimethyl disulfide was related to the total aerobic bacteria coun

292 The cleavage kinetics of a number of disulfides were investigated using a fluorescent reporte

293 he hydrogen evolution reaction on molybdenum disulfide, where it is shown that the basal plane posses

294 ia redox processes, including oxidation to a disulfide with a neighboring cysteine or dissociation up

295 theory calculations indicate that molybdenum disulfide with moderate cobalt doping content possesses

296 ocyclohexyl acetate or Angeli's salt induced disulfides within cGMP-dependent protein kinase I-alpha

297 We consider it unlikely that the disulfide would form under intracellular reducing condit

298 , the growth of oxidation-resistant tungsten disulfide (WS2 ) monolayers on graphene is demonstrated,

299 ge Bloch-Siegert shift in monolayer tungsten disulfide (WS2) under infrared optical driving.

300 Especially, single-layer tungsten disulfides (WS2) is a direct band gap semiconductor with