ライフサイエンスコーパス: disulphide bond

1 between aromatic residues and by the single disulphide bond.

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

3 fragment is artificially dimerized through a disulphide bond.

4 dues has been identified that surrounds this disulphide bond.

5 t require the formation of an intramolecular disulphide bond.

6 h is further stabilised by a single internal disulphide bond.

7 n of an ion pair cluster and an intrasubunit disulphide bond.

8 ComGC was found to possess an intramolecular disulphide bond.

9 esidues and the redox state of the conserved disulphide bond.

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

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

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

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

14 ription activation domain is stabilized by a disulphide bond.

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

16 ully oxidised native protein containing four disulphide bonds.

17 and forms high molecular mass complexes via disulphide bonds.

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

19 inases-1 (TIMP-1), a 21-kDa protein with six disulphide bonds.

20 refore is enhanced by the formation of mixed disulphide bonds.

21 d cooking loss, accompanied by a decrease in disulphide bonds.

22 synergism of electrostatic interactions and disulphide bonds.

23 synergism of electrostatic interactions and disulphide bonds.

24 phosphatase/sulphatase fold containing three disulphide bonds.

25 ogether by an extensive hydrophobic core and disulphide bonds.

26 long extracellular loops stabilized by four disulphide bonds.

27 ight chain polypeptides covalently linked by disulphide bonds.

28 products that help cells reduce cytoplasmic disulphide bonds.

29 the oxidation-reduction state of cytoplasmic disulphide bonds.

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

31 cleases evolved from a progenitor with three disulphide bonds.

32 l responses to protein antigens that contain disulphide bonds.

33 more, the polymerization occurs only through disulphide bonds.

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

35 sent in hydrophobins and form intramolecular disulphide bonds.

36 on of helix-3, bounded by the intramolecular disulphide bond, 179-214.

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

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

39 -turns and surface hydrophobicity, promoting disulphide-bonded aggregation.

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

41 entation of the two domains, stabilized by a disulphide bond and a small hydrophobic patch within the

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

43 dues of Dr family structural subunits form a disulphide bond and that mutations of these residues abo

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

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

46 so as to facilitate the formation of correct disulphide bonds and c-type cytochromes in the latter co

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

48 IgE, but has differently located interchain disulphide bonds and external rather than interdomain N-

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

50 itions, CheAS appears to form intermolecular disulphide bonds and loses the ability to bind to CheZ.

51 e content, amino acid frequencies, number of disulphide bonds and size of the largest cleft.

52 of about 10 microM, required the presence of disulphide bonds and was mediated through protein (rathe

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

54 six cysteines that form three intramolecular disulphide bonds, and aromatic residues lining the catal

55 597 of the S5-P linker can form intersubunit disulphide bonds, and at least four of them (at 584, 585

56 these interactions is usually maintained by disulphide bonds, and it seems that the overall main cha

57 ing phase when an increase in intermolecular disulphide bonds, anti-parallel B-sheet and a-helix stru

58 ively reduce the formation of intermolecular disulphide bonds, anti-parallel B-sheet and a-helix stru

59 Disulphide bonds are donated directly to unfolded polype

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

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

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

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

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

65 gamma and Cdelta, and in the location of the disulphide bond between them, may enable gammadelta TCRs

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

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

68 This species has three of the four native disulphide bonds, but lacks the Cys76-Cys94 disulphide b

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

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

71 hat reduction of intramolecular cbEGF domain disulphide bonds by homocysteine and the resulting disru

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

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

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

75 essential and forms a high-molecular-weight disulphide-bonded complex in the outer membrane.

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

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

78 folding of BLA, in the presence of its four disulphide bonds, corresponds to one of the limiting cas

79 nstrate a previously undetermined role for a disulphide-bonded cystine in the epsilon subunit C-termi

80 All the disulphide-bonded dimers had flexible ligand-binding dom

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

82 likely results from a break in the conserved disulphide-bonded eighth module at the junction of CR1 a

83 hanism by constraining the coiled coils with disulphide bonds, either self-locking or bridged by a ch

84 Here, guided by AlphaFold2 models, we use disulphide bond engineering in an attempt to trap SurA i

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

86 le cysteine OmpF mutants, five of which form disulphide bonds fixing L3 in the conformation determine

87 Redox stress induces disulphide bond formation amongst zinc-ligating residues

88 edox-sensitive cysteine residues involved in disulphide bond formation and oligomerisation of NDP52 o

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

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

91 While disulphide bond formation between the Cys residues of th

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

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

94 Now two pathways involved in disulphide bond formation have been well characterized,

95 Ten years ago it was thought that disulphide bond formation in prokaryotes occurred sponta

96 Oxidative stress induces intramolecular disulphide bond formation in RsrA, which causes it to lo

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

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

99 y the electron transport chain, showing that disulphide bond formation is actually driven by electron

100 -43 cross-linking via cysteine oxidation and disulphide bond formation leading to decreased TDP-43 so

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

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

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

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

105 ctor regulation by reversible intramolecular disulphide bond formation.

106 er form of this protein is not stabilized by disulphide bond formation.

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

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

109 is reversibly inactivated by oxygen through disulphide bond formation.

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

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

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

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

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

115 We generated stable disulphide-bonded full-length RPTPalpha homodimers by ex

116 Here we show that DAP12, a disulphide-bonded homodimer containing an immunoreceptor

117 tates and blends consist of a combination of disulphide bonds, hydrophobic and electrostatic interact

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

119 redominantly reduce the Cys6-Cys1O4 terminal disulphide bond in PSP.

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

121 ectrometry analysis detected a newly created disulphide bond in the mutant CADM3 potentially modifyin

122 V fimbria because of the essential role of a disulphide bond in the stability of the major structural

123 rificans CcmG acts in vivo to reduce protein-disulphide bonds in certain protein substrates including

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

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

126 the acids caused reduction in the amount of disulphide bonds in the most stable conformation (g-g-g)

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

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

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

130 Kinetic analyses of the disulphide bonding indicate that EGF binding induces fle

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

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

133 the protein's sequence which were linked by disulphide bonds into structures of ~ 5-6 kDa.

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

135 sms other than the formation of intersubunit disulphide bonds involving p50 residue C62.

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

137 ion of a stable, non-reducible linker into a disulphide bond is a commonly used approach for cyclizin

138 concomitant with formation of this critical disulphide bond is a major restructuring of the protein

139 ired for haem attachment, possibly because a disulphide bond is an intermediate.

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

141 tion activator activity, suggesting that the disulphide bond is not necessary for either dimer stabil

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

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

144 protein; a minor conformer generated through disulphide bond isomerisation; an alternative hydrogen b

145 Disulphide-bonded KCNQ1/KCNE1 constructs reported prefer

146 rease in solvent accessibility of one of the disulphide bonds (linking the second and sixth cysteine

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

148 y-terminal cysteine-rich domain is masked by disulphide-bond-mediated interactions with a conserved a

149 mutation causes a G270E change in the third disulphide-bonded module of CR1, and causes no phenotype

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

151 SDS-PAGE showed that neither disulphide bonds nor CC coupling were involved in the fo

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

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

154 Mild reduction and alkylation of the hinge disulphide bonds of scFvhCH2 greatly decreased its capac

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

156 The disulphide bond pattern has been further altered by the

157 The disulphide bonding pattern was determined and is consist

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

159 ighest strength, possibly because of greater disulphide-bonded polymerisation.

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

161 Knottins are a group of small, disulphide-bonded proteins that bind with high specifici

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

163 e suggests that it may act in vivo to reduce disulphide bonds rather than to form them.

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

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

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

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

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

169 d NMR studies indicate that this is the only disulphide bond that can be removed without perturbing t

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

171 predicted to cause misfolding by removal of disulphide bonds that stabilize the native domain fold.

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

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

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

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

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

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

178 disulphide bonds, but lacks the Cys76-Cys94 disulphide bond which connects the two folding domains i

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

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

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

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

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

184 diated by intracellular exchange of a single disulphide bond within the third, and only the third, TB

185 I), facilitates the formation of the correct disulphide bonds within newly synthesised polypeptides,

186 hyl)phosphine (TCEP) was then used to reduce disulphide bonds within proteins to confirm the importan

187 Formation of disulphide bonds within the mammalian endoplasmic reticu

188 Upon reduction of the disulphide bonds, Yap1 undergoes a change to an unstruct