ライフサイエンスコーパス: Cys

1 Cys is present at the equivalent position in ~100 human

2 Cys(1978) S-palmitoylation regulates current amplitude u

3 man CD8(+) tumor-reactive T cells against 10 Cys-containing HLA class I-restricted minimal determinan

4 The conserved Cys(109)Cys(110) motif in ANKRD9 is required for the vesicle-to-

5 Three S-palmitoylation sites (Cys(1169), Cys(1170), and Cys(1978)) were identified.

6 ctural rearrangement that primes the Cys-122-Cys-66 disulfide for thioredoxin reduction and a reversi

7 ing the disulfide cascade expose the Cys-122-Cys-66 disulfide to recycling through thioredoxin.

8 at NaTrxh specifically reduces the Cys(155) -Cys(185) disulphide bond of S(C10) -Rnase, resulting in

9 Our findings suggest that the Cys-17-Cys-34 disulfide slows proteolysis by dampening conforma

10 Use of a MoFe protein variant, beta-188(Cys), which poises the P cluster in the oxidized P(+) st

11 tron-transfer sites in cupredoxins (CuHis(2) Cys) or rubredoxins (FeCys(4) ).

12 or heat and membrane integrity), a Zn(II)(2) Cys(6) (Gal4-like) family member, which regulates resist

13 are comparatively active to the native Pam(2)Cys containing constructs.

14 valently conjugated to the TLR2-ligand Pam(2)Cys to generate a self-adjuvanting lipopeptide vaccine.

15 Existing SAR studies of Pam(2)Cys with TLR2 indicate that the structural requirements

16 3-bis(palmitoyloxy)propyl]-l-cysteine (Pam(2)Cys) motif and exhibit potent immunostimulatory effects.

17 tween the two ester functionalities in Pam(2)Cys-conjugated lipopeptides on TLR2 activity.

18 Schizosaccharomyces pombe fission yeast Zn(2)Cys(6) transcriptional factor that drives a response to

19 2-Cys peroxiredoxins (Prxs) rapidly reduce H(2)O(2), there

20 Interestingly, eukaryotic 2-Cys Prxs lose their peroxidase activity at high H(2)O(2)

21 Many 2-Cys-peroxiredoxins (2-Cys-Prxs) are dual-function protei

22 cuses on Leishmania infantum mitochondrial 2-Cys-Prx, whose reduced, decameric subpopulation adopts c

23 hese studies revealed the participation of 2-Cys peroxiredoxin (2-Cys PRX), a thiol-dependent peroxid

24 The susceptibility of 2-Cys Prxs to hyperoxidation varies greatly and depends on

25 focusing on the functional relationship of 2-Cys PRXs with NTRC and the FDX-FTR-TRXs redox systems fo

26 the participation of 2-Cys peroxiredoxin (2-Cys PRX), a thiol-dependent peroxidase, in the control o

27 Many 2-Cys-peroxiredoxins (2-Cys-Prxs) are dual-function proteins, either acting as p

28 Typical 2-Cys peroxiredoxins are known to switch between different

29 The mechanism by which 2-Cys-Prxs switch functions remains to be defined.

30 However, encapsulation of [Au(25)(Cys)(18)] and CV into the polymer activates potent photo

31 ows that additional encapsulation of [Au(25)(Cys)(18)] into the CV treated polymer promotes redox rea

32 (CV) and thiolated gold nanocluster ([Au(25)(Cys)(18)]) activated at a low flux levels of white light

33 hat S-cyanylation of SBPase Cys(74), CYP20-3 Cys(259), and ENO2 Cys(346) residues affected their enzy

34 TLR2 signaling was induced with Pam(3)Cys-Ser-Lys(4), and the role of ERK signaling was interr

35 cysteines and one distant cysteine (Cys(3), Cys(4), and Cys(169)) per monomer.

36 tachment of the doubly ligated PEB to Cys-48/Cys-59 of CpeB and together with other specific bilin ly

37 rologous host, CpeF can attach PEB to Cys-48/Cys-59 of CpeB, but only in the presence of the chaperon

38 ligation of the doubly linked PEB to Cys-48/Cys-59 residues of the CpeB subunit of PE.

39 al Lys and Arg residues with Ala and added a Cys residue at either position 289 or 275 to affix a flu

40 up contains a lipid-like alkyl chain - and a Cys-peptide modified by a lipid-like moiety.

41 wo pharmacophores-a zinc binding group and a Cys-reactive warhead-were designed to leverage both affi

42 d onto its substrate peptide by connecting a Cys-thiol group to the beta-carbon of an upstream Asn re

43 ffected by mutations required to construct a Cys-lite variant needed for site-specific fluorescence l

44 ad, a highly active cysteine-lipase having a Cys-His-Asp catalytic triad and additional mutations W10

45 interface consists of a converging helix, a Cys-Cys-bridge-linked IA, and extracellular loops (ECL).

46 ovalent labeling of the Cys residues using a Cys-reactive label that masks epitope residues, followed

47 Cpa, a pilus tip-end adhesin equipped with a Cys-Gln thioester bond.

48 Conformational changes that accompany Cys-domain rotation are conserved for SUMO and Ub E1s, b

49 2AR cysteine thiols to Cys-S-sulfenic acids (Cys-S-OH).

50 pocket, which may give rise to an additional Cys axial ligand at 20K (His/Cys coordination).

51 Cysteine-4-methylcatechol adduct (Cys-4MC) formation in meat added 1500 ppm 4-MC increased

52 The redox state across all Cys peptides was shifted toward reduction from 27.1% dow

53 purified from Escherichia coli binds an all-Cys-coordinated [2Fe-2S] cluster.

54 mitoylation sites (Cys(1169), Cys(1170), and Cys(1978)) were identified.

55 avage and indicate that Arg-56, His-123, and Cys-364 are critical SufS residues in this C-S bond clea

56 e framework of current models of 5-HT(3) and Cys-loop mechanisms are used to expand the understanding

57 nd one distant cysteine (Cys(3), Cys(4), and Cys(169)) per monomer.

58 hrough disulfide bonds formed by Cys(54) and Cys(347), which was essential for activation of the IKK

59 targeted by ERp57 and found that Cys(6) and Cys(23) in the N-terminal region of ficolin-3 form the i

60 (ProRS) misactivates and mischarges Ala and Cys, which are similar in size to cognate Pro.

61 C364A SufS variants to trap Cys-aldimine and Cys-ketimine intermediates of the cysteine desulfurase r

62 hiocarbamate (PDTC) on the efflux of GSH and Cys from HepG2 cells.

63 tion to other residues such as His, Lys, and Cys, providing very good structural resolution.

64 ss-induced damage (e.g., by reducing Met and Cys oxidation products) as well as adjusting metabolic f

65 t beta-strands of the N-domain (intra-N) and Cys pairs that bridged the external surface of the N-dom

66 CYP2B6 downregulation, and selected Tyr and Cys residues for mutation based on predicted solvent acc

67 ed that the C-terminal TnT region approached Cys-190 of tropomyosin as actin filaments transitioned t

68 Two compounds 19 (c(Bua-Cpa-Thi-Val-Asn-Cys)-Pro-Agm) and 38 (c(Bua-Cpa-Thi-Val-Asn-Cys)-Pro-d-A

69 -Cys)-Pro-Agm) and 38 (c(Bua-Cpa-Thi-Val-Asn-Cys)-Pro-d-Arg-NEt(2)) have been selected for clinical d

70 ttached a phosphorescent probe to F-actin at Cys-374 and performed transient phosphorescence anisotro

71 The single free thiol located at Cys-34 in domain I of albumin has been exploited for mon

72 in the frequency of Sec misincorporation at Cys codons in vivo We surmise that the His -> Asn variat

73 s, causing undesired incorporation of Sec at Cys codons due to the inability of cysteinyl-tRNA synthe

74 hagy mediated by the autophagy-related (ATG) Cys protease AtATG4a.

75 Substitution of a single residue in beta1, Cys-162, to alanine prevented palmitoylation, reduced th

76 resultant functional consequences of beta2AR Cys-redox in the receptors native, oxidized, and redox-d

77 o regulate the functions of free/metal-bound Cys and Zn sites in proteins.

78 Afterward, metal-bound Cys can be easily labeled in a nucleophilic addition rea

79 ge of NEMO through disulfide bonds formed by Cys(54) and Cys(347), which was essential for activation

80 asis of cellular excitation or inhibition by Cys-loop ligand-gated ion channels (LGICs), and is essen

81 , although the reversible trapping of MGO by Cys residues is initially kinetically favourable.

82 g lists of proteins potentially regulated by Cys oxidation/thioredoxin, Met-SO formation, phosphoryla

83 ith either of two cysteines in the canonical Cys-78-X-X-Cys-81 motif.

84 at is a part of the characteristic catalytic Cys-His-Asp triad of Cys proteases.

85 of IAA, specifically attacking the catalytic Cys 152.

86 As a result, the catalytic Cys becomes hydrated and optimally positioned to encount

87 consistent with the absence of the catalytic Cys in its sequence.

88 reaction entails ionization of the catalytic Cys.

89 ly, in known DHHC structures, this catalytic Cys appears to be exposed to the hydrophobic interior of

90 YbaK, a free-standing editing domain, clears Cys-tRNAPro in trans.

91 owing its mono-ubiquitination at a conserved Cys residue.

92 on between the DNA abasic site and conserved Cys 2 of HMCES.

93 The conserved Cys(109)Cys(110) motif in ANKRD9 is required for the ves

94 edict that redox modulation of the conserved Cys(290) of Aurora A may be an underappreciated regulato

95 Moreover, the presence of this conserved Cys predicted biochemical redox sensitivity among a coho

96 to more accurately rank peptides containing Cys anchor residues.

97 iensis with a naturally-occurring contracted Cys-Lys-Cys-His (CKCH) heme-binding motif, which is enco

98 and validated it by mutation of coordinating Cys and His residues, revealing that a triad of residues

99 s, which are covalently bound to a cysteine (Cys) residue in the chromophore-binding domain (CBD, com

100 The effect of added cysteine (Cys), which is known to greatly enhance Hg(II) biouptake

101 he glutamine (Gln) deamidation and cysteine (Cys) oxidation branches are both components of the plant

102 partate (Asp), glutamate (Glu) and cysteine (Cys) phosphorylation sites on human proteins by mass spe

103 one (GSH), homocysteine (Hcy), and cysteine (Cys), coexist in biological systems with diverse biologi

104 domain that contains the catalytic cysteine (Cys domain).

105 A1 isoform 2 lacking the catalytic cysteine (Cys-462), suggesting that CYP24A1's oncogenic potential

106 ion poorly for epitopes containing cysteine (Cys) residues, which can oxidize and form disulfide bond

107 vicinal cysteines and one distant cysteine (Cys(3), Cys(4), and Cys(169)) per monomer.

108 hiol precursors S-3-(hexan-1-ol)-l-cysteine (Cys-3MH) and S-3-(hexan-1-ol)-l-glutathione (GSH-3MH) we

109 the development of MFH290, a novel cysteine (Cys)-directed covalent inhibitor of CDK12/13.

110 dition of a NO moiety to a protein cysteine (Cys) thiol (-SH) to form an S-nitrosothiol (SNO).

111 type 3 receptor is a member of the cysteine (Cys)-loop receptor super family of ligand-gated ion chan

112 Although structurally similar to cysteine (Cys), the Sec selenol group has unique properties that a

113 ch is then resolved by a conserved cysteine, Cys-66, or by the nonconserved residue Cys-127.

114 S analyses revealed that the third cysteine, Cys-163, formed disulfide bonds with either of two cyste

115 Cystine (Cys(2)), methionine (Met), and sulfate were also detecte

116 ossess tRNA specificity, readily deacylating Cys-tRNACysin vitro.

117 anes or filaments) in which site-specific di-Cys mutation is feasible.

118 onjugated to an engineered anti-CD8 diabody (Cys-diabody) for in vivo molecular imaging of CD8+ cytot

119 By introducing site-directed Cys residues in bacterial iron transporters and modifyin

120 The PAS-Cys, GAF-Cys and double-Cys attachment each entails distinct configurational con

121 This protein with the unusual double-Cys attached BV showed the highest fluorescence quantum

122 in different secondary structures, enabling Cys labeling with Alexa Fluor 488 for quenching analysis

123 f SBPase Cys(74), CYP20-3 Cys(259), and ENO2 Cys(346) residues affected their enzymatic activity.

124 ifferent ages under an imposed extracellular Cys/CySS oxidative or reductive condition.

125 ctionally replaced by adding a synthetic [Fe(Cys)(CO)(2)(CN)] carrier in the maturation reaction.

126 Substitutions of AABA for Cys at putative MHC anchor positions often significantly

127 ysRS variant provides higher specificity for Cys as a mechanism for plants to grow in selenium-rich s

128 YbaK binds to ProRS to gain specificity for Cys-tRNAPro and avoid deacylation of Cys-tRNACys in the

129 ovided by IAM is more suitable to label free Cys residues, avoiding nonspecific metal dissociation.

130 ed model of the SufS-catalyzed reaction from Cys binding to C-S bond cleavage and indicate that Arg-5

131 The PAS-Cys, GAF-Cys and double-Cys attachment each entails distinct conf

132 in active hydrolases by introducing a Ser -> Cys exchange at the respective catalytic triads, but thi

133 This framework has Cys(I)-Cys(IV)/Cys(II)-Cys(V)/Cys(III)-Cys(VI) connectiv

134 ormation of the structures Hg(Mem-RS)(2), Hg(Cys)(Mem-RS), and Hg(Mem-RSRO) to be 39.1 +/- 0.2, 38.1

135 low molecular mass (LMM) thiols like Cys, Hg(Cys)(Mem-RS), or with neighboring O/N membrane functiona

136 ethylate the N, S, and O side chains of His, Cys, Glu, Asp, and Lys residues.

137 at a site defined by a conserved Asp-His-His-Cys motif.

138 d by conserved residues from CTD and the His-Cys-His (HCH) motif from the N-terminal segment of the n

139 coordinated hemes with His/Lys (heme 1), His/Cys (heme 2), and two His/His ligations (hemes 3 and 4).

140 o an additional Cys axial ligand at 20K (His/Cys coordination).

141 e active site Heme 1 in both enzymes has His/Cys ligation in the ferric and ferrous states and the mi

142 This framework has Cys(I)-Cys(IV)/Cys(II)-Cys(V)/Cys(III)-Cys(VI) connectivities,

143 We also identified Cys-314 as a potential S-acylation site.

144 mutagenesis and EPR spectroscopy identified Cys-261 on CblD as the sulfur donor.

145 We identified Cys(74) as the catalytic residue for both ubiquitination

146 Here we show that the HydG product [Fe(II)(Cys)(CO)(2)(CN)] synthon is the substrate of the radical

147 This framework has Cys(I)-Cys(IV)/Cys(II)-Cys(V)/Cys(III)-Cys(VI) connectivities, which have invar

148 f As(III) (11871.5 eV) or As(III)-S [As(III)-Cys, 11869.6 eV] solution in the cooked foods and in the

149 k has Cys(I)-Cys(IV)/Cys(II)-Cys(V)/Cys(III)-Cys(VI) connectivities, which have invariably been assoc

150 Remarkably, an imposed Cys/CySS reductive state rejuvenated the mitochondrial f

151 d the understanding of how ligand binding in Cys-loop receptors relates to channel gating.

152 ase activities in vitro, are nitrosylated in Cys residues in vivo, and scavenge NO in the stomatal ce

153 in place of the sulfhydryl group present in Cys, for the native Cys residues.

154 -chain conformation on charge selectivity in Cys-loop receptors.

155 These included Cys pairs on adjacent beta-strands of the N-domain (intr

156 Interestingly, Cys(1978) is exclusive to Nav1.6 among all Nav isoforms

157 and fluorescent tags can be introduced into Cys-containing peptides and proteins.

158 activity, reverts the oxidation of invariant Cys residues in FNIP1 and allows CUL2(FEM1B) to recogniz

159 intermolecular disulfides without losing its Cys-coordinated Zn(2+), and only the nonconserved Cys-12

160 This framework has Cys(I)-Cys(IV)/Cys(II)-Cys(V)/Cys(III)-Cys(VI) connectivities, which ha

161 parately further modified with l-cysteine (l-Cys) and l-serine (l-Ser).

162 c responses were produced by A-MWCNT/Hyalu/l-Cys and A-MWCNT/Hyalu/l-Ser modified electrodes.

163 0.015 ug L(-1) (Pb(II)) for A-MWCNT/Hyalu/l-Cys/GCE and 0.057 ug L(-1) (Cd(II)) and 0.034 ug L(-1) (

164 ) and 3.5 uA/nM (Pb(II)) for A-MWCNT/Hyalu/l-Cys/GCE and 0.6 uA/nM (Cd(II)) and 2.6 uA/nM (Pb(II)) fo

165 er with low molecular mass (LMM) thiols like Cys, Hg(Cys)(Mem-RS), or with neighboring O/N membrane f

166 an FN3K, which contains an equivalent P-loop Cys, was also redox sensitive, whereas ancestral bacteri

167 bacterial FN3K homologs, which lack a P-loop Cys, were not.

168 ith a naturally-occurring contracted Cys-Lys-Cys-His (CKCH) heme-binding motif, which is encoded in t

169 investigated the effect of OA-NO(2)-mediated Cys-319 alkylation on ABL1 binding and found that OA-NO(

170 sensing of 85 scalemic samples of Pro, Met, Cys, Ala, methylpyrrolidine, 1-(2-naphthyl)amine, and mi

171 ic couplings introduced via a (13)C(3),(15)N-Cys-labeled synthetic carrier.

172 fhydryl group present in Cys, for the native Cys residues.

173 oordinated Zn(2+), and only the nonconserved Cys-127 reacted with the low-molecular-weight (LMW) thio

174 The Nt-Cys ETHYLENE RESPONSE FACTOR VII transcription factor su

175 cated that the predicted affinity for 25% of Cys-containing epitopes was underestimated by a factor o

176 QJ1), a PEARL that catalyzes the addition of Cys to the C-terminus of the peptide TglA in the biosynt

177 HOS catalyst system allows the allylation of Cys-containing peptides and proteins with complete chemo

178 sesses an unusual catalytic dyad composed of Cys(145) and His(41) residues.

179 es aimed at identifying the S-cyanylation of Cys as a posttranslational modification of proteins.

180 ity for Cys-tRNAPro and avoid deacylation of Cys-tRNACys in the cell.

181 monly used reagents to link thiol groups (of Cys) to drugs and labels.

182 s achieved by the generation of a library of Cys mutations in Env glycoprotein on the viral surface,

183 Oxidative modification of Cys residues by NO results in S-nitrosylation, a ubiquit

184 nitrosylation, the oxidative modification of Cys residues to form S-nitrosothiols (SNOs).

185 strated to be CDK12-dependent as mutation of Cys-1039 rendered the kinase refractory to MFH290 and re

186 A large number of Cys peptides (412) were redox switched, representing cen

187 In proteins with more than one pair of Cys residues, there is the potential for formation of no

188 We genetically introduced pairs of Cys residues in different regions of the FepA tertiary s

189 Conversely, introducing Val in place of Cys(93) stabilized the hydrophobic core and increased th

190 aluate MHC binding and T cell recognition of Cys-containing peptides under conditions that prevent Cy

191 effect on Hg(II) methylation, regardless of Cys addition.

192 tantly, our work uncovers a critical role of Cys-322 in determining Tau toxicity and dysfunction.SIGN

193 s by hydrogen bonding with the sulfhydryl of Cys-aldimine.

194 haracteristic catalytic Cys-His-Asp triad of Cys proteases.

195 eine results in accumulation of an Ile(*) or Cys(*) radical, respectively.

196 americ ligand-gated ion channels (pLGICs) or Cys-loop receptors are involved in fast synaptic signali

197 but to identify metal-binding sites in other Cys-containing proteins.

198 oxidize and form disulfide bonds with other Cys residues under oxidizing conditions, thus potentiall

199 ole of TM2 in TM signaling, we use oxidative Cys cross-linking to demonstrate that TM2 extends over t

200 dative environments can irreversibly oxidize Cys-S-OH to Cys-S-sulfinic (Cys-SO(2)H) or S-sulfonic (C

201 ks the disulfide bond between p.Cys-53 and p.Cys-165, which is highly conserved among species.

202 GH-C53S) lacks the disulfide bond between p.Cys-53 and p.Cys-165, which is highly conserved among sp

203 study, we discovered that substitution of p.Cys-53 in hGH significantly increased formation of hGH d

204 The PAS-Cys, GAF-Cys and double-Cys attachment each entails dist

205 fenic acid derivative of the Prx peroxidatic Cys (C(P)SOH) to the sulfinate (C(P)SO(2) (-)) and sulfo

206 ining peptides under conditions that prevent Cys oxidation, and to adjust current prediction binding

207 Furthermore, mutation of pUL36 Cys(131) abrogated MLKL degradation and restored necropt

208 RAD51 Cys-319 resides within the SH3-binding site of ABL proto

209 In conclusion, RAD51 Cys-319 is a functionally significant site for adduction

210 er, consists of a cysteine-tyrosine radical (Cys-Tyr(*)) as a copper ligand.

211 Introducing Trp(85) or Phe(29) to replace Cys or Leu, respectively, disrupts packing in the hydrop

212 dues near the disulfide bond-forming residue Cys(11) modulate XCR1 activation.

213 eine, Cys-66, or by the nonconserved residue Cys-127.

214 show that the conserved nucleophilic residue Cys-122 is S-sulfenylated after substrate reduction, whi

215 e oxidation of a conserved cysteine residue (Cys(290)) that lies adjacent to Thr(288), a critical pho

216 that NS3-4A cleaves DHCR24 between residues Cys(91) and Thr(92) and show that this reduces the intra

217 erface, together with two specific residues (Cys-246 and Ser-256) present exclusively in m4-1BBL, are

218 nt to a novel "thiol-blocked" [(PDT)Mo(V)O(S(Cys))(thiolate)](-) structure, which is supported by new

219 enzymes showed that S-cyanylation of SBPase Cys(74), CYP20-3 Cys(259), and ENO2 Cys(346) residues af

220 lized fast reacting cysteine/selenocysteine (Cys/Sec) residues.

221 the loop's N-terminus to the active site Ser-Cys-Thr-Sec sequence.

222 sidues are not structurally equivalent since Cys-322 is incorporated into the core of the fibril, whe

223 Active site Cys peptides of glutathione reductase 2, NADPH-thioredox

224 t C. bicolor THI4, which has the active-site Cys needed to operate suicidally, may be capable of suic

225 prokaryotic THI4s that lack the active-site Cys residue on which suicide activity depends, and (ii)

226 Three S-palmitoylation sites (Cys(1169), Cys(1170), and Cys(1978)) were identified.

227 Mutagenesis of all six Cys residues in ATIII to Ala resulted in its efficient s

228 ar) that has three amino acid substitutions (Cys(27), Gly(608), and Pro(671)) within the full-length

229 versibly oxidize Cys-S-OH to Cys-S-sulfinic (Cys-SO(2)H) or S-sulfonic (Cys-SO(3)H) acids, which are

230 o Cys-S-sulfinic (Cys-SO(2)H) or S-sulfonic (Cys-SO(3)H) acids, which are incapable of further partic

231 disintegrin-like (D), thrombospondin-1 (T), Cys-rich (C), and spacer (S) domains (proximal domains),

232 disintegrin-like (D), thrombospondin-1 (T), Cys-rich (C), and spacer (S) domains, followed by 7 addi

233 what attained by acrylamides when targeting Cys residues.

234 l acidic residues, as well as the C-terminal Cys residue of the TP53INP1 LIR peptide, are required fo

235 N-degron pathway is oxidation of N-terminal Cys residues.

236 tilized an sGCbeta reporter construct, tetra-Cys sGCbeta, whose heme insertion can be followed by flu

237 ferential affinity sites for Cu(II) and that Cys(163) is an active site for FMN binding.

238 an immediate demonstration, we clarify that Cys is not the source of the carbon and nitrogen atoms i

239 lfide bonds targeted by ERp57 and found that Cys(6) and Cys(23) in the N-terminal region of ficolin-3

240 Of note, we propose that Cys-364 is essential for positioning the Cys-aldimine fo

241 The Cys(93) residue of the beta subunit is the primary site

242 The Cys/Ser mutation does not affect NO dioxygenase activity

243 te binding, as a general acid to advance the Cys-quinonoid PLP intermediate, as a nucleophile to form

244 ects the coupling between the C-loop and the Cys-loop, vestibular loop, and beta1-beta2 loops.

245 The cis conformation at the Cys(6)-Pro(7) peptide bond was essential for alpha3beta4

246 onical EGFD disulfide connectivity (i.e. the Cys 1-2, 3-4, 5-6 disulfide pattern).

247 nges during the disulfide cascade expose the Cys-122-Cys-66 disulfide to recycling through thioredoxi

248 tor is a homopentameric ion channel from the Cys-loop receptor superfamily targeted for psychiatric i

249 e ligands, MN(2) S(2) (2-) prepared from the Cys-X-Cys biomimetic, ema(4-) ligand (ema=N,N'-ethyleneb

250 Open conformations of the Cys domain are associated with adenylation and thioester

251 the viral surface, covalent labeling of the Cys residues using a Cys-reactive label that masks epito

252 hat Cys-364 is essential for positioning the Cys-aldimine for Calpha deprotonation, His-123 acts to p

253 jor structural rearrangement that primes the Cys-122-Cys-66 disulfide for thioredoxin reduction and a

254 vidence that NaTrxh specifically reduces the Cys(155) -Cys(185) disulphide bond of S(C10) -Rnase, res

255 mass-spectrometry experiments show that the Cys backbone is converted to pyruvate, consistent with a

256 Our findings suggest that the Cys-17-Cys-34 disulfide slows proteolysis by dampening c

257 e sensing of oxygen availability through the Cys/Arg N-degron pathway functions alongside ROS product

258 titer IgG, IgM, and IgA Ab responses to the Cys-like protease from SARS-CoV-2, also known as 3CLpro

259 e encompassed by protein degradation via the Cys/Arg branch of the N-degron pathway-part of the PROTE

260 ulfinic acid, triggering degradation via the Cys/Arg branch of the N-degron pathway.

261 t relevant properties of peptide thioesters, Cys peptides, and common solvents, reagents, additives,

262 was responsible for 58% loss of free thiols (Cys residues).

263 Although this Cys is conserved from worms to mammals, a two amino acid

264 cal SAM (RS)-cluster is coordinated by three Cys, and the adjacent K1- and K2-clusters, representing

265 of purified wild-type Apd1 and three His to Cys variants demonstrated that Cys207 and Cys216 are the

266 onments can irreversibly oxidize Cys-S-OH to Cys-S-sulfinic (Cys-SO(2)H) or S-sulfonic (Cys-SO(3)H) a

267 e first time that beta2AR can be oxidized to Cys-S-OH in situ, moreover, using both clonal cells and

268 hat CpeF likely ligates the A ring of PEB to Cys-48 prior to the attachment of the D ring to Cys-59.

269 for attachment of the doubly ligated PEB to Cys-48/Cys-59 of CpeB and together with other specific b

270 a heterologous host, CpeF can attach PEB to Cys-48/Cys-59 of CpeB, but only in the presence of the c

271 lly for ligation of the doubly linked PEB to Cys-48/Cys-59 residues of the CpeB subunit of PE.

272 -48 prior to the attachment of the D ring to Cys-59.

273 tionally oxidizes beta2AR cysteine thiols to Cys-S-sulfenic acids (Cys-S-OH).

274 An adaptive Tyr-to-Cys substitution at amino acid 42 was discovered using e

275 pothesis that the specificity of YbaK toward Cys-tRNAPro is determined by the formation of a three-co

276 ployed H123A and C364A SufS variants to trap Cys-aldimine and Cys-ketimine intermediates of the cyste

277 (CARS) encodes the enzyme that charges tRNA(Cys) with cysteine in the cytoplasm.

278 ices, truncated versions of full-length tRNA(Cys) that contain the acceptor stem, were also accepted.

279 enzyme recognizes the acceptor stem of tRNA(Cys), as micro- and minihelices, truncated versions of f

280 ore, are each coordinated by one His and two Cys.

281 g di- and trisulfide cross-links between two Cys residues, to derepress the mexAB-oprM operon.

282 as in the wild-type, i.e., Cu(II)-(Cl-Tyr(*)-Cys) or Cu(II)-(F-Tyr(*)-Cys).

283 , Cu(II)-(Cl-Tyr(*)-Cys) or Cu(II)-(F-Tyr(*)-Cys).

284 In summary, the unpaired Cys-165 in GH-C53S forms a disulfide bond linking two hG

285 pe (Env) at single-residue resolution, using Cys labeling, viral neutralization assays, and deep sequ

286 framework has Cys(I)-Cys(IV)/Cys(II)-Cys(V)/Cys(III)-Cys(VI) connectivities, which have invariably b

287 Further validation of [(68)Ga]DO3A-VS-Cys(40)-Exendin-4 as an islet imaging probe for future c

288 ibited significant uptake of [(68)Ga]DO3A-VS-Cys(40)-Exendin-4 compared to the livers of untreated mi

289 evealed that liver uptake of [(68)Ga]DO3A-VS-Cys(40)-Exendin-4 was approximately 6-fold higher in mic

290 [(68)Ga]DO3A-VS-Cys(40)-Exendin-4, a glucagon-like peptide 1 receptor ag

291 porated into the core of the fibril, whereas Cys-291 projects away from the core to form the fuzzy co

292 adopts a zwitterionic reactive form in which Cys(145) is in the negatively charged thiolate state and

293 encoded cytochrome P411 enzymes (P450s whose Cys axial ligand to the heme iron has been replaced with

294 l acceptor forming an irreversible bond with Cys 215 in the ATP-binding pocket, a residue that is not

295 MFH290 forms a covalent bond with Cys-1039 of CDK12, exhibits excellent kinome selectivity

296 ever, covalent Michael adduct formation with Cys-18, a residue present at the N terminus of SIRT6 but

297 al ligation of beta-annulus-SBz peptide with Cys-containing S-peptide that self-assembled into artifi

298 der conditions of high MeHg production (with Cys addition).

299 nds, MN(2) S(2) (2-) prepared from the Cys-X-Cys biomimetic, ema(4-) ligand (ema=N,N'-ethylenebis(mer

300 of two cysteines in the canonical Cys-78-X-X-Cys-81 motif.