ライフサイエンスコーパス: disulfide bond

1 equence (K(d) = 1.8 nM) containing an i, i+4 disulfide bond.

2 f the structure by formation of a non-native disulfide bond.

3 of the corresponding consensus 7-8 LU domain disulfide bond.

4 isation of sema domain dimer formation via a disulfide bond.

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

6 ing the oxidation of the Sod1 intramolecular disulfide bond.

7 site that substitutes for a loop-stabilizing disulfide bond.

8 physicochemical attributes of this atypical disulfide bond.

9 tion and S-nitrosylation and form non-native disulfide bonds.

10 onditions, such as those containing critical disulfide bonds.

11 o alter post-translational modifications and disulfide bonds.

12 e proteins, glycoproteins, and proteins with disulfide bonds.

13 r XIIIa with six cysteines involved in three disulfide bonds.

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

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

16 n cells frequently requires the insertion of disulfide bonds.

17 ansiently interacts with CHCHD4 and acquires disulfide bonds.

18 al CSalphabeta motif stabilized by conserved disulfide bonds.

19 ue antiparallel beta-sheet stabilized by two disulfide bonds.

20 ToPI1, with 33 amino acid residues and three disulfide bonds.

21 ism for the isomerization of such non-native disulfide bonds.

22 llular milieu as a result of the cleavage of disulfide bonds.

23 DsbC reduces mis-formed disulfide bonds.

24 into a compact four-helix bundle with three disulfide bonds.

25 to characterize the cysteine connectivity of disulfide bonds.

26 rtiary structure, with the potential to form disulfide bonds.

27 and is stabilized by three highly conserved disulfide bonds.

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

29 t studies have reported that upregulation of disulfide-bond A oxidoreductase-like protein (DsbA-L) pr

30 osing beta-strands connected by two parallel disulfide bonds, a structure homologous to the N-termina

31 nformation by the introduction of artificial disulfide bonds: A501C/T605C (called SOS) and I201C/A433

32 The disulfide bond acts as a temporary covalent linkage betw

33 vitro data show that the redox state of the disulfide bond affects S. aureus biofilm formation and t

34 " can be altered by addition of cross-domain disulfide bonds, also visualized at atomic resolution.

35 rimers of gp140 Env that are stabilized by a disulfide bond, an isoleucine-to-proline substitution at

36 We synthesized the three possible 2-disulfide-bonded analogues using a targeted protecting g

37 sgp140 SOSIP.664) stabilized by a gp120-gp41 disulfide bond and a change (I559P) in gp41 have been st

38 reviously unappreciated means to stabilize a disulfide bond and highlight the utility of the n->pai*

39 tions including a membrane-distal interchain disulfide bond and negatively charged O-linked glycans n

40 Our data support a model whereby the disulfide bond and PAS domain of SrrB sense and respond

41 teines involved in intra- and intermolecular disulfide bonding and protein folding.

42 x-ERp57 complexes reduce these extracellular disulfide bonds and are essential for ECM degradation.

43 e learning to enable rapid identification of disulfide bonds and cysteine-related variants in an IgG1

44 e MEDI3726 protein scaffold lacks interchain disulfide bonds and has an average drug to antibody rati

45 inistic entanglements which can be formed by disulfide bonds and interactions via ions, a refined cha

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

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

48 on of oxidation products such as chain-chain disulfide bonds and sulfonic acid chains-ends.

49 ted by the formation of dimers stabilized by disulfide bonds and then proceeds via primary nucleation

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

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

52 sed of four alpha-helices stabilized by four disulfide bonds, and a long C-terminal tail.

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

54 re formed, and reduced, in which one or more disulfide bonds are broken.

55 Prior to the signal detection procedure, disulfide bonds are chemically cleaved, and the perfluor

56 bonds remain intact) and fully reduced (all disulfide bonds are cleaved) forms.

57 ted redox states: oxidized, in which all the disulfide bonds are formed, and reduced, in which one or

58 Disulfide bonds are found in many proteins associated wi

59 Four pairs of distal, intramonomeric disulfide bonds are found to be coupled to the stability

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

61 h d-alpha-tocopherol succinate (TOS) using a disulfide bond as the linker (HA-SS-TOS, HSST), which co

62 KO cells, whose gamma subunits are linked by disulfide bonds, as well as in cells expressing monomeri

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

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

65 thione by the formation of an intramolecular disulfide bond between Cys149 and Cys153 reinforces the

66 (hereafter referred to as GH-C53S) lacks the disulfide bond between p.Cys-53 and p.Cys-165, which is

67 ursor protein (APPI) that incorporated a new disulfide bond between residues 17 and 34 reduced proteo

68 ove plasticity through the introduction of a disulfide bond between the alpha(1)/alpha(2) helices abr

69 nd Fc constant regions, adding a stabilizing disulfide bond between the constant domains and disrupti

70 Here, we find that disulfide bonding between a native cysteine pair at the

71 clusters followed by subsequent formation of disulfide bonds between conserved active-site cysteines

72 Disulfide bonds between cysteine residues are commonly i

73 s that can cross-link sigma1 by establishing disulfide bonds between structurally adjacent sites in t

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

75 of three peptides bearing two intramolecular disulfide bonds but different cysteine connectivity have

76 cific radiation damage at RT was observed at disulfide bonds but not at acidic residues, increasing a

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

78 a highly conserved region stabilized by two disulfide bonds, but it captures RSV G in a conformation

79 e release of glycans via the cleavage of the disulfide bond by dithiothreitol.

80 A-O16B, a lipid nanoparticle integrated with disulfide bonds, can efficiently deliver Cas9 mRNA and s

81 nels by a unique glycosyl moiety and loss of disulfide-bonding capability at the Na(V)beta subunit-in

82 hiol function site, for forming longitudinal disulfide bond chains.

83 accompanied by the generation of large mixed disulfide bonded complexes, including ERp44.

84 In bacteria, disulfide bonds confer stability on many proteins export

85 for the ToxS periplasmic domain than the non-disulfide bonded conformation.

86 u rubripes, presumably through maintaining a disulfide-bonded conformation.

87 Disulfide bond connectivity characterization is still ch

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

89 e nanoparticles (GPUs) using a GSH-cleavable disulfide bond containing polyurethane that responds to

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

91 d combinatorial library of cholesteryl-based disulfide bond-containing biodegradable cationic lipidoi

92 o investigate whether a straight versus bent disulfide bond-containing CDRH3 is specific to particula

93 ed from HCV-infected individuals, revealed a disulfide bond-containing CDRH3 that adopts straight (in

94 for MHC class II-restricted presentation of disulfide bond-containing proteins, including the self-a

95 Disulfide bonds contribute to protein stability, activit

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

97 , side-chain-to-tail cyclization (C2), and a disulfide bond cross-linkage (C3).

98 Using disulfide-bond crosslinking, we find that the first beta

99 fold that includes a set of three conserved disulfide bonds, denoted the "SARAF-fold." The structure

100 evented FeEnt uptake, whereas most inter-N-C disulfide bonds did not prevent FeEnt uptake.

101 l disruption, indicating that the introduced disulfide bonds did not significantly affect protein fol

102 phimurium (S Typhimurium) contains a complex disulfide bond (Dsb) catalytic machinery.

103 Analysis of the disulfide bonds (DSBs) is vital to ensuring the correct

104 omain of neurexins by forming intermolecular disulfide bonds during transport through the secretory p

105 n, the oxidation of two cysteine thiols to a disulfide bond, during the catalytic cycle of the N-term

106 volve the iRhoms, such as regulation through disulfide bond exchange or through interaction with char

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

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

109 al peptidase that requires an intramolecular disulfide bond for in vitro activity.

110 zyl group and particle cross-linking through disulfide bond formation accompanied by the shrinkage of

111 Rapid disulfide bond formation and cleavage is an essential me

112 Regulated proinsulin biosynthesis, disulfide bond formation and ER redox homeostasis are es

113 Up to now, coupling of cysteine oxidation, disulfide bond formation and structure formation in nasc

114 d that S-sulfhydration affected intraprotein disulfide bond formation and was required for the mainte

115 ese important biomolecules because incorrect disulfide bond formation and/or presence of cysteine-rel

116 ructure, which is constructed by consecutive disulfide bond formation between a large number of pepti

117 No disulfide bond formation between cysteine groups on the

118 In our study, we used disulfide bond formation between pairs of engineered cys

119 We previously showed that disruption of disulfide bond formation by Disulfide Disrupting Agents

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

121 nd to a model ER protein exhibiting improper disulfide bond formation during reductive ER stress but

122 able ligation/desulfurization and subsequent disulfide bond formation in a one-pot process.

123 titutions successfully promoted intersubunit disulfide bond formation in HeV F.

124 ty of MP, corresponding to disulfide and non-disulfide bond formation in protein aggregates, was mark

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

126 We show that disulfide bond formation inhibits filament assembly and

127 Disulfide bond formation is a common mechanism to stabil

128 Disulfide bond formation is a critical post-translationa

129 n dimer-decamer transitions and intersubunit disulfide bond formation is more complex than previously

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

131 minants: a protein folding switch coupled to disulfide bond formation regulates chaperone-mediated re

132 Thus, proteins involved in disulfide bond formation represent good targets for the

133 potentially destabilizing or preventing the disulfide bond formation required for proper protein fun

134 ysteine residues in pairs is a result of the disulfide bond formation system, which functions to oxid

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

136 it tunnel provides sufficient space even for disulfide bond formation which can guide protein folding

137 Pfs48/45 has 16 cysteines involved in disulfide bond formation, and the correct formation is c

138 We have investigated the interplay between disulfide bond formation, lipids, and pH in the folding

139 ations used the natural macrocycle tether of disulfide bond formation, metal-mediated or lactam group

140 Activation by R655C did not require disulfide bond formation.

141 ic ends of the MA-helices, are conducive for disulfide bond formation.

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

143 oper posttranslational processing, incorrect disulfide-bond formation, protein aggregation, changes i

144 ermolecular covalent linkage of NEMO through disulfide bonds formed by Cys(54) and Cys(347), which wa

145 Disulfide bonds formed by cysteine residues have been in

146 Here, we present evidence that the disulfide bond forming enzymes, DsbB and VKOR, are requi

147 traditionally relied on lactam, lactone and disulfide bond-forming reactions that aim at introducing

148 its receptor XCR1, whereas residues near the disulfide bond-forming residue Cys(11) modulate XCR1 act

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

150 e of parameters, including primary sequence, disulfide bonding, glycosylation patterns, biotransforma

151 etic role, but a growing subset of cleavable disulfide bonds has been shown to control the function o

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

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

154 Depending on the location of these disulfide bonds, HeV F can still fold properly and bind

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

156 e bonds, when the absence of this particular disulfide bond impairs the correct folding of other sing

157 the oxidation of the conserved intrasubunit disulfide bond in SOD1.

158 cture shows a unique intramolecular cysteine disulfide bond in the ATP-binding domain that significan

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

160 part by ensuring formation of an intra-chain disulfide bond in the C-terminal periplasmic domain of T

161 ctodomain trimer, covalently stabilized by a disulfide bond in the closed conformation.

162 In summary, elimination of the 7-8 consensus disulfide bond in the first LU domain of uPAR did have s

163 ts highlight the critical structural role of disulfide bond in ToxR and along with VtrA define a doma

164 the evolutionary deletion of this particular disulfide bond in uPAR DI may have enabled the assembly

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

166 t studies evidenced a role for K14-dependent disulfide bonding in the organization and dynamics of ke

167 nd accurate workflow in mapping-out expected disulfide bonds in both half antibodies and bispecific a

168 We further demonstrate the disulfide bonds in cbEGF domains uniquely orchestrate pr

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

170 suppresses complement activation by cleaving disulfide bonds in ficolin-3 and reducing its multimer s

171 region of ficolin-3 form the intermolecular disulfide bonds in ficolin-3 multimers that are reduced

172 These cysteine residues did not form disulfide bonds in HBx expressed in human cells.

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

174 lement activation by cleaving intermolecular disulfide bonds in large ficolin-3 multimers, thereby re

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

176 suggesting that the elimination of multiple disulfide bonds in NOTCH3 accelerates its fragmentation.

177 The formation of disulfide bonds in proteins is an essential process in b

178 redoxin (Trx), which also reduces allosteric disulfide bonds in proteins, including mAbs.

179 asticity of bronchial secretions by reducing disulfide bonds in proteins.

180 be reversibly oxidized, forming interprotein disulfide bonds in the holoenzyme complex.

181 the breakage, formation, and exchange of the disulfide bonds in the molecular system occur spontaneou

182 on assays indicated that the introduction of disulfide bonds in the mutants prohibited fusion events.

183 teins DsbA and DsbB mediate the formation of disulfide bonds in the periplasm.

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

185 in which spontaneously formed intermolecular disulfide bonds initiate amyloid fibril formation by rec

186 664 trimer variants containing newly created disulfide bonds intended to stabilize the V2 loop in an

187 dition, by introducing a stimulus-responsive disulfide bond into the linker molecule, the on-demand d

188 We introduced single disulfide bonds into NPC1 and NPC1L1 to explore the impo

189 t and reversible binding, we have introduced disulfide bonds into opposite sides of a flexible loop c

190 In this study, we demonstrate that disulfide bonds introduced between the HeV F transmembra

191 endocarditis model, we demonstrate that the disulfide bond is a critical regulatory element of SrrB

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

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

194 We find that the disulfide bond is stabilized by two n->pai* interactions

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

196 Specific damage to disulfide bonds is evident early on at RT and proceeds a

197 es involving the cleavage and reformation of disulfide bonds is revealed by material/structural chara

198 The differentiation of individual disulfide-bonded isomers by traditional high-performance

199 Three of the 15 possible 3-disulfide-bonded isomers have been identified, which sha

200 ass spectrometry (TIMS-MS), several 2- and 3-disulfide-bonded isomers of the mu-conotoxin PIIIA were

201 4's codon 373 (C373A) exhibit alterations in disulfide-bonded K14 species and a barrier defect second

202 th six conserved cysteine residues forming a disulfide-bonded knottin scaffold that creates a contigu

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

204 all interruptions of D2 loop intramolecular disulfide bonding lead to haploinsufficiency-related RP,

205 e 213, which is engaged in an intramolecular disulfide bond, leads to butterfly-shaped pattern dystro

206 Protein disulfide bonds link pairs of cysteine residues in polyp

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

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

209 ary, the unpaired Cys-165 in GH-C53S forms a disulfide bond linking two hGH molecules in pituitary ce

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

211 first time the ability to efficiently cleave disulfide bonds linking heavy and light chains of mAbs u

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

213 is the potential for formation of non-native disulfide bonds, making it necessary for the cell to hav

214 While ETD retains modifications and cleaves disulfide bonds-making it attractive for mAb characteriz

215 the bovine IgG1 hinge region and a predicted disulfide bonding motif linking the upper hinge region,

216 strate protein unfolding by showing that MFS disulfide bond mutations markedly disrupt normal mechano

217 nd two helical turns stabilized by a complex disulfide bond network that creates an embedded ring aro

218 dies have shown that S-glutathionylation and disulfide bonding of titin fragments could alter the ela

219 We found that Trx reduces the interchain disulfide bonds of the mAbs, after which they remain int

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

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

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

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

224 roteins, peptides and other biopolymers with disulfide bonds or ions interactions giving rise to the

225 ostability and disruptions to alpha helices, disulfide bonds, or the permeation pore.

226 d by a dimer of the heavily glycosylated and disulfide-bonded OSTM1, which serves to protect CLC-7 fr

227 ence of glycosylation, and containing proper disulfide bond pairings.

228 ulfide bonding pattern; an unexpected Cys3-4 disulfide bonding pattern is observed in AspH-EGFD subst

229 ished fold with a conserved Cys1-3, 2-4, 5-6 disulfide bonding pattern; an unexpected Cys3-4 disulfid

230 We used MS to identify the disulfide-bonding pattern in ficolin-3 multimers and the

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 thesis, while retaining the functionality of disulfide-bonded peptides, has been demonstrated with ou

234 ely, confirmed the formation of well-ordered disulfide bonds positioned to stabilize the binding loop

235 Such conversion is dependent on the unique disulfide bonding properties of the hIgG2 hinge.

236 te lysate to identify known sulfenylated and disulfide-bonded proteins, including elongation factor 1

237 ses a solid support, free radical precursor, disulfide bond, pyridyl, and hydrazine moieties.

238 The interdomain disulfide bond raises the possibility of oxidative regul

239 ell proteins and beta3 integrin intraprotein disulfide bond rearrangement.

240 ts in both the partially reduced (intrachain disulfide bonds remain intact) and fully reduced (all di

241 t without alkylation, Trx-reduced interchain disulfide bonds reoxidize, and ADCC activity is restored

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

243 Reduction of the Cys1-Cys7 disulfide bond resulted in faster fibrillation with invo

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

245 S that allow the production of thermostable, disulfide-bonded S-protein trimers that are trapped in t

246 ite cell-surface ENG being a dimer linked by disulfide bonds, sENG purified from human placenta and p

247 ach complemented E. coli strain expressing a disulfide-bond sensitive beta-galactosidase reported pre

248 G505 SOSIP.664, incorporates an intersubunit disulfide bond (SOS) to covalently link the gp120 and gp

249 er 3,3'-dithiodipropionic acid (DDPA) with a disulfide bond (SS) extended by short-chain polyethylene

250 the oxidation of sulfhydryl groups (-SH) to disulfide bonds (-SS-) of extracted proteins at 0.6 mu w

251 oxRp crystal structure showed this is due to disulfide bond stabilization.

252 Mutants targeting the disulfide-bond stabilized LRX dimer interface fail to re

253 rate that RALF peptides fold into bioactive, disulfide bond-stabilized proteins that bind the LRR dom

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

255 g these LU domains contains five plesiotypic disulfide bonds stabilizing its prototypical three-finge

256 sensitivity of the internal friction to the disulfide bond status suggests that one or both of the c

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

258 alpha isoform, particularly in relation to a disulfide bond structure that is specifically reduced by

259 nding pattern in ficolin-3 multimers and the disulfide bonds targeted by ERp57 and found that Cys(6)

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

261 s the second variant, E153C/R178C, had a new disulfide bond that cross-linked V2 and V1.

262 s, the diketopiperazine ring is spanned by a disulfide bond that is constrained in a high-energy ecli

263 teine residues, generating an intermolecular disulfide bond that promotes dimerization and fibrilliza

264 on, allowing the formation of intermolecular disulfide bonds that result in TFEB oligomerization.

265 tion is characterized by strained interchain disulfide bonds that stabilize the P-loop in an extended

266 ontain conserved cysteine residues that form disulfide bonds that stabilize their structures.

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

268 mposed of proteinogenic amino acids and lack disulfide bonds; they are also known in several genera o

269 otein building blocks are linked by a single disulfide bond to create diverse metal coordination envi

270 Either introducing single disulfide bonds to constrain lumenal/extracellular domai

271 s at neutral pH, allowing the engineering of disulfide bonds to cross-link spikes.

272 imported into Escherichia coli can transfer disulfide bonds to cytoplasmic proteins.

273 The strategy of selectively reducing disulfide bonds to facilitate large-scale synthesis, whi

274 or PNGase F, and (3) reduction of interchain disulfide bonds to generate ~25 kDa ADC subfragments, wh

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

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

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

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

279 However, a unique interdomain disulfide bond was found in the FhGST-S1 which could sta

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

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

282 unsuccessful, suggesting that the introduced disulfide bonds were likely buried in the membrane.

283 omain in uPAR (DI) lack one of its consensus disulfide bonds, when the absence of this particular dis

284 ains two HRMs whose cysteine residues form a disulfide bond; when reduced, these cysteines are availa

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

286 the bond is substituted by a salt bridge or disulfide bond, whereas disruption of the contact by mut

287 meric networks via the formation of covalent disulfide bonds, which govern the viscoelastic propertie

288 BisAbs contain engineered disulfide bonds, which have been demonstrated to form pr

289 methods consistently showed that the intra-N disulfide bonds, which restrict conformational motion wi

290 nfected cells, forming incorrect cross-chain disulfide bonds, which results in impaired GPC processin

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

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

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

294 led that the third cysteine, Cys-163, formed disulfide bonds with either of two cysteines in the cano

295 has been used as a mucolytic to reduce mucin disulfide bonds with little, if any, therapeutic effects

296 e (Cys) residues, which can oxidize and form disulfide bonds with other Cys residues under oxidizing

297 first variant, I184C/E190C, contained a new disulfide bond within the V2 loop, whereas the second va

298 Disulfide bonds within cysteine-rich peptides are import

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

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