ライフサイエンスコーパス: disulfide bond

1 redox switch' centered on an inter-molecular disulfide bond.

2 f hSCGN via the formation of a Cys193-Cys193 disulfide bond.

3 y through the formation of an intermolecular disulfide bond.

4 ly, formation of a reversible intermolecular disulfide bond.

5 nd the lack of the conserved Cys-139-Cys-206 disulfide bond.

6 ic subunit and one basic subunit linked by a disulfide bond.

7 earrangements that result in cleavage of the disulfide bond.

8 a Ca(2+)binding site and a vicinal cysteine disulfide bond.

9 el and a direct tether via an intermolecular disulfide bond.

10 ng anchored by a pair of cysteines forming a disulfide bond.

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

12 n the reactive center loop to form a vicinal disulfide bond.

13 ing the oxidation of the Sod1 intramolecular disulfide bond.

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

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

16 mation of nonnative intra- or intermolecular disulfide bonds.

17 be done in species containing closely spaced disulfide bonds.

18 structure through the formation of a pair of disulfide bonds.

19 g into gluten aggregates through inter-chain disulfide bonds.

20 domain through a beta-hairpin stabilized by disulfide bonds.

21 ttached to cysteine residues in peptides via disulfide bonds.

22 of alpha-La lead to a gel more dependent on disulfide bonds.

23 ols generated by the reduction of interchain disulfide bonds.

24 e ions with readily oxidized groups, such as disulfide bonds.

25 PvRBPs highlight the conserved placement of disulfide bonds.

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

27 reatment results in very limited cleavage of disulfide bonds.

28 nous trimerization motifs and intermolecular disulfide bonds.

29 and leads to formation of novel interprotein disulfide bonds.

30 n cells frequently requires the insertion of disulfide bonds.

31 ansiently interacts with CHCHD4 and acquires disulfide bonds.

32 these confirmed the formation of engineered disulfide bonds.

33 ormal biological function and that are often disulfide bonded.

34 a loop (residues 864 to 881) stabilized by a disulfide bond ((869)CKWGGNWTCV(878), named FPII) in est

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

36 Our simulations show how an engineered disulfide bond across the NBD dimer interface reduces co

37 We found that this disulfide bond acts as a redox switch that precludes the

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

39 Here, we investigated how this disulfide bond affects the stability and folding/unfoldi

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

41 0C/S407C pair and a CuPh- and Cd(2+)-induced disulfide bond and complex, respectively, for the Q45C/L

42 s can pair with cysteines to afford extended disulfide bonds and allow cross-linking of more distant

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

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

45 wo protein post-translational modifications, disulfide bonds and phosphorylation, was investigated.

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

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

48 protein stability and folding via forming a disulfide bond, and Cys(6) and Cys(111) as free thiols.

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

50 .5 +/- 5.1 GPa for proteins with interfacial disulfide bonds, and 1.6 +/- 1.5-2.5 +/- 2.3 GPa for the

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

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

53 oral bacteria also have the ability to from disulfide bonds, and this ability has an effect on a ran

54 lacking metal and a stabilizing intrasubunit disulfide bond, apoSOD1(2SH), is dynamic and hypothesize

55 ide, and formation of this Cys(201)-Cys(203) disulfide bond appears to disrupt the DNA binding activi

56 Disulfide bonds are a common posttranslational modificat

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

58 Disulfide bonds are found in many proteins associated wi

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

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

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

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

63 lectrospray ionization process to facilitate disulfide bond assignments.

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

65 n the oxidation of cysteine residues to form disulfide bonds at a highly conserved zinc site.

66 articles capable of spontaneous intersubunit disulfide bonds at the interhexamer interface in the cap

67 d Panx1 function temporarily by formation of disulfide bonds at the thiol group of its terminal cyste

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

69 However, disulfide bonds being an additional covalent bond in the

70 The structures reveal the presence of a disulfide bond between conserved cysteines that is posit

71 Previous work has identified a disulfide bond between Cys-45 residues within the homodi

72 llel beta strands stabilized by the hallmark disulfide bond between the B and F strands.

73 bA is thought to catalyze the formation of a disulfide bond between the Cys residues at the apocytoch

74 tion of factors, including the presence of a disulfide bond between the Cysteines at 131 and 157, whi

75 nsistent with the formation of a spontaneous disulfide bond between the N90C/S407C pair and a CuPh- a

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

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

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

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

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

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

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

83 ormation of a disulfide bond, induction of a disulfide bond by oxidization with dichloro(1,10-phenant

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

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

86 les was tuned by controlling the kinetics of disulfide bond cleavage, and the rate of regeneration of

87 Heating triggered the disruption of the disulfide bonds connecting the acidic and basic chains o

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

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

90 These species correspond to disulfide bond-containing dimeric and monomeric PMEL iso

91 mation, exemplified by the synthesis of four-disulfide bond-containing insulin analogs.

92 Disulfide bonds contribute to protein stability, activit

93 m which unambiguous assignment of individual disulfide bonds could be done in species containing clos

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

95 P through the formation of an intramolecular disulfide bond (Cys(318)-Cys(326)), known to act as a re

96 ates VWF dimerization by forming the first 2 disulfide bonds Cys2771-2773' and Cys2771'-2773.

97 the nucleotide-binding site with one of the disulfide bond cysteines coordinating the AMP with its m

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

99 nnections demands advances in techniques for disulfide bond determination.

100 eine-rich Kringle-like domain stabilizes the disulfide-bonded dimer and impairs fibril formation as d

101 Under oxidizing conditions RRM2 forms disulfide-bonded dimers that experience unfolding and th

102 (pre-F) conformation by previously described disulfide bond (DS) and hydrophobic cavity-filling (Cav1

103 We previously modified RSV F with a designed disulfide bond (DS) to increase stability in the prefusi

104 e FtsN levels in strains incapable of making disulfide bonds (dsb(-) ) exposed to anaerobic condition

105 was applied in order to inhibit formation of disulfide bonds during gel formation.

106 y, we exploited in-source reduction (ISR) of disulfide bonds during the electrospray ionization proce

107 ain conserved cysteines that are oxidized to disulfide bonds during their import.

108 p75 stabilizes the receptor dimers through a disulfide bond, essential for the NGF signaling.

109 ved cysteine residues that form a structural disulfide bond exposed to the intermembrane space (IMS).

110 Specifically, disulfide-bonded FimG undergoes a 30% increase in its me

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

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

113 fensin 3 (HBD-3), the latter requiring three disulfide bonds for proper folding.

114 ss hERG1b currents (and vice versa), 2) that disulfide bonds form between single cysteine residues ex

115 Rapid disulfide bond formation and cleavage is an essential me

116 kine recognition, stable protein expression, disulfide bond formation and glycosylation that are crit

117 e endoplasmic reticulum (ER), Ero1 catalyzes disulfide bond formation and promotes glutathione (GSH)

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

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

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

121 Therefore, inhibitors of disulfide bond formation enzymes could have profound eff

122 Finally, we discuss disulfide bond formation in a cellular context and ident

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

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

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

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

127 We show that disulfide bond formation inhibits filament assembly and

128 In Actinomyces oris, disulfide bond formation is needed for pilus assembly, c

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

130 nally closed structure to allow cross-domain disulfide bond formation or cross-linking by bismaleimid

131 In the Escherichia coli disulfide bond formation pathway, the periplasmic protei

132 bitors at the IspD binding site, followed by disulfide bond formation through attack of an active sit

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

134 e found that copper phenanthroline catalyzed disulfide bond formation within five cysteine pairs and

135 volve ROS-induced protein dysfunction due to disulfide bond formation, and H2 can protect oxidation o

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

137 ach based on stepwise, sequentially directed disulfide bond formation, exemplified by the synthesis o

138 altered glycosylation, additional pH-induced disulfide bond formation, increased percentage of nonvol

139 cosylation to protein processing and correct disulfide bond formation, we investigated whether the co

140 folding reveal a surprising, biased order of disulfide bond formation, with early formation of the C-

141 cattering profiles consistent with incorrect disulfide bond formation.

142 r cell division in E. coli is dependent upon disulfide bond formation.

143 -sn-glycerol-3-phospho-(1'rac-glycerol)) via disulfide bond formation.

144 Activation by R655C did not require disulfide bond formation.

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

146 nd differentially accelerate the kinetics of disulfide-bond formation of several conotoxins.

147 of apocytochrome c and also resolve a mixed disulfide bond formed between apocytochrome c and CcmH.

148 Moreover, the structure contained a disulfide bond formed with an active-site Cys residue re

149 including the hormonogenic tyrosines and the disulfide bond-forming cysteines critical for Tg functio

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

151 Electrochemical (EC) reduction of disulfide bonds has recently been demonstrated to provid

152 oxidized state by forming an intramolecular disulfide bond, HePTP uses an unexpected mechanism, name

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

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

155 must/wine upon heating cleaves intraprotein disulfide bonds, hinders thiol-disulfide exchange during

156 second transmembrane domain (TM2) and that a disulfide bond holds the resulting two fragments togethe

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

158 development due to their small cores, whose disulfide bonds impart extraordinary chemical and biolog

159 We also show that the disulfide bond in DraE is recognized by the DraB chapero

160 as one of clearest examples of an allosteric disulfide bond in mammals.

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

162 bond and cysteinylation is between the first disulfide bond in the hinge region.

163 do not interact directly, nor do they form a disulfide bond in the intact S. cerevisiae GPIT.

164 mbrane helix-helix interactions, including a disulfide bond in the long isoform of the receptor.

165 ide relay, though the mechanism by which the disulfide bond in Tim17 is formed differs considerably f

166 The disulfide bond in Tim17 is formed during insertion of th

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

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

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

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

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

172 omodimeric structure with two intermolecular disulfide bonds in its oxidized state.

173 proved mucolytic drug) can reduce intrachain disulfide bonds in large polymeric proteins.

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

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

176 ponsible for the reduction of intermolecular disulfide bonds in protamines and their eviction from sp

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

178 Formation of correct disulfide bonds in the endoplasmic reticulum is a crucia

179 r cysteines that can form two intramolecular disulfide bonds in the oxidized forms.

180 macodynamics and potential scrambling of the disulfide bonds in vivo.

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

182 were assessed for spontaneous formation of a disulfide bond, induction of a disulfide bond by oxidiza

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

184 ble inactivation) or a stable sulfenamide or disulfide bond intermediate (reversible inactivation).

185 way, the periplasmic protein DsbA introduces disulfide bonds into substrates, and then the cytoplasmi

186 this strategy, we have incorporated multiple disulfide bonds into the interfaces of a Zn-templated cy

187 s redox-regulated through the formation of a disulfide bond involving a highly reactive cysteine uniq

188 This disulfide bond is critical for efficient protein translo

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

190 A disulfide bond is easily formed between the monomers of

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

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

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

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

195 The formation of disulfide bonds is of the utmost importance for a wide r

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

197 nd unfolding rate constants of DraE-sc and a disulfide bond-lacking DraE-sc variant.

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

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

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

201 ue is especially valuable in determining the disulfide bond linkage of complicated molecules such as

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

203 d synthetic ligands to ZZ domain facilitates disulfide bond-linked aggregation of p62 and p62 interac

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

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

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

207 GPC composed of JUNV GP1 containing a small disulfide bonded loop (loop 10) unique to MACV GPC, sugg

208 ed cysteines is a chemoattractant, whereas a disulfide bond makes it a proinflammatory cytokine.

209 crucial role in HJ cleavage, consistent with disulfide-bond mediated dimerization being essential for

210 hanges, arising from disulfide or sulfhydryl-disulfide bond-mediated aggregation of whey protein mole

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

212 tter understanding of the mechanism by which disulfide bond-mediated PHD2 dimerization and inactivati

213 Furthermore, we demonstrated that disulfide bond-mediated PHD2 dimerization is associated

214 Here, we identified disulfide bond-mediated PHD2 homo-dimer formation in res

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

216 eling of quaternary structures, DOPE scores, disulfide bond modeling and choice of heteroatoms to be

217 orrect conformation, with the three critical disulfide bonds observed in native pINSL3, although part

218 blished that CcmG can efficiently reduce the disulfide bond of apocytochrome c and also resolve a mix

219 disease and establish the Cys(370)-Cys(371) disulfide bond of TG2 as one of clearest examples of an

220 d in between the light chain and heavy chain disulfide bond of the A and A/B forms.

221 eactive oxygen species, mediated through the disulfide bond of the prosthetic lipoyl moiety.

222 ide bonds are associated with the interchain disulfide bonds of both A isoform and A/B isoform and cy

223 s a partial reduction approach in mapping of disulfide bonds of intact human insulin (HI) and lysozym

224 We found that two of the four disulfide bonds of pIII are required for its interaction

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

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

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

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

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

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

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

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

233 s PilB or PilT, blocked in vivo formation of disulfide-bonded PilNO heterodimers, suggesting that bot

234 Disulfide bonds play a crucial role in proteins, modulat

235 Disulfide bonds play an important role in protein foldin

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

237 le-like domain facilitates the resolution of disulfide-bonded PMEL dimers and promotes PMEL functiona

238 ven without the corresponding intermolecular disulfide bonds present in hIntL-1, the carbohydrate rec

239 monomer or multimer (where all Cys formed a disulfide bond) primarily bound up to 2 Cu(II) ions.

240 ort that STM3997, which encodes a homolog of disulfide bond protein A (dsbA) of Escherichia coli, is

241 lfide characterization of complex and highly disulfide-bonded proteins such as human serum albumin (H

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

243 ndoplasmic reticulum exit and is resolved by disulfide bond rearrangement into a monomeric form withi

244 we have measured previously uncharacterized disulfide bond redox chemistry in Escherichia coli HypD.

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

246 reagents combined with heavy and light chain disulfide bond reduction followed by light chain analysi

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

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

249 nt linkage of thioesterase domains through a disulfide bond, revealing structural similarities with A

250 nthetic IGF-1 analogs are unique examples of disulfide bonds' rich proteins with intra main-chain tri

251 Multiple myeloma cells secrete more disulfide bond-rich proteins than any other mammalian ce

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

253 ich accelerates the cleavage of more exposed disulfide bond sand intracellular drug release.

254 he thioredoxin-like a and a' domains mediate disulfide bond shuffling and b and b' domains are substr

255 ntation velocity revealed two native high Mr disulfide-bonded species that contain Golgi-modified for

256 ted to optimize (CCIZN17)3, a representative disulfide bond-stabilized chimeric NHR-trimer, by incorp

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

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

259 e structural rearrangement compared with the disulfide-bonded structure, which includes the relocatio

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

261 show that the TIM23 subunit Tim17 contains a disulfide bond that is crucial for protein translocation

262 e trisulfide was also located in between the disulfide bond that is formed by the second pair of cyst

263 ke domain-containing proteins is a conserved disulfide bond that joins their A and B strands.

264 steine residues that have been shown to form disulfide bonds that are crucial for the three-dimension

265 e defined at the molecular level, allosteric disulfide bonds that are modified by thiol isomerases ha

266 oTx-II is a 30-amino acid peptide with three disulfide bonds that has been reported to adopt a well-d

267 We further identified two pairs of potential disulfide bonds that reside outside the beta-sheet catal

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

269 sed for complexing siRNA contained reducible disulfide bonds that underwent intracellular reduction o

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

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

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

273 The selective gas-phase oxidation of disulfide bonds to their thiosulfinate form using ion/io

274 ATIII has three disulfide bonds, two near the N terminus and one near th

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

276 Complete reduction of the intraprotamine disulfide bonds ultimately leads to decondensation, sugg

277 cysteine pair Cys-87/Cys-285 of ClyA forms a disulfide bond under oxidizing conditions and that both

278 acted from udon or bread witout severing the disulfide bonds under reducing condition.

279 Species containing an intermolecular disulfide bond undergo separation of the two chains upon

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

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

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

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

284 lly reduced species containing only a single disulfide bond were also generated, from which unambiguo

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

286 two active site cysteines readily forming a disulfide bond when not coordinating zinc.

287 in the DNA binding domain of LasR do form a disulfide bond when treated with hydrogen peroxide, and

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

289 a neighbouring thiol to create a protective disulfide bond, which assists the functional folding of

290 ochrome c are most likely to form this mixed disulfide bond, which is consistent with the stereo-spec

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

292 nehydrazide cargo by formation/breakage of a disulfide bond, while dynamic hydrazone chemistry contro

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

294 f spider toxins reveals that (55)Cys forms a disulfide bond with (910)Cys in the Nav1.2 domain II por

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

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

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

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

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

300 The critical feature is the use of a double disulfide-bonded Wnt peptide that mimics the two-dimensi