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UnknownOpt1 imports CoA precursors as glutathione mixed disulfides.
Not available
S-EPMC12406275 | biostudies-literature
UnknownConversion of S-phenylsulfonylcysteine residues to mixed disulfides at pH 4.0: utility in protein thiol blocking and in protein-S-nitrosothiol detection.
Not available
S-EPMC4365953 | biostudies-literature
UnknownSARS-CoV-2 ORF8 reshapes the ER through forming mixed disulfides with ER oxidoreductases.
Not available
S-EPMC9239706 | biostudies-literature
ProteomicsClients of membrane-bound PDI family members
The client-specificity of TMX3, TMX4 and TMX5 in cellula, was assessed by expressing mutant forms of the enzymes, where the last cysteine residue of the TMX’s CXXC catalytic sites has been mutated to alanine, which stabilizes the mixed disulfide that oxidoreductases establish with clients. Clients r...
ORGANISM(S): Homo sapiens (Human) 
2023-06-12 | PXD041156 | Pride
Trapping mutants Endoplasmic reticulum Oxidoreductases Mixed disulfides 
UnknownThioredoxin A active-site mutants form mixed disulfide dimers that resemble enzyme-substrate reaction intermediates.
Not available
S-EPMC2896474 | biostudies-literature
ProteomicsSARS-CoV-2 ORF8 interactome in the secretory pathway
The replication machinery of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is closely associated with the endoplasmic reticulum (ER) in host cells. Activation of the unfolded protein response (UPR) is a strategy hijacked by coronavirus to facilitate its replication and suppress ho...
ORGANISM(S): Homo sapiens (Human) 
2022-08-12 | PXD032035 | Pride
Orf8 2-d gel Endoplasmic reticulum Lc-ms/ms 
TranscriptomicsS-bacillithiolation of the OhrR repressor and the methionine synthase MetE protect against hypochlorite stress in Bacillus subtilis
Protein S-thiolation is a post-translational thiol-modification that controls redox-sensing transcription factors and protects active site cysteine residues against irreversible oxidation. In B. subtilis, the MarR-type repressor OhrR was shown to sense organic hydroperoxides via formation of mixed d...
ORGANISM(S): Bacillus subtilis subsp. subtilis str. 168 
2011-07-04 | E-GEOD-27637 | biostudies-arrayexpress
ProteomicsEndogenous interactors of the natural trapping mutant TMX5/TXNDC15
The endoplasmic reticulum (ER) is the organelle of nucleated cells that produces lipids, sugars and proteins. More than 20 ER-resident members of the Protein Disulfide Isomerase (PDI) family regulate formation, isomerization and disassembly of covalent bonds in newly synthesized polypeptides. The PD...
ORGANISM(S): Homo sapiens (Human) 
2024-09-27 | PXD054716 | Pride
Endoplasmic reticulum  erp44  mixed disulfides  pdi family  tmx5/txnd15 
UnknownAlternating Current Electrolysis for the Electrocatalytic Synthesis of Mixed Disulfide via Sulfur-Sulfur Bond Metathesis towards Dynamic Disulfide Libraries.
Not available
S-EPMC7079035 | biostudies-literature
ProteomicsIn situ identification of S-sulfenylation sites in Arabidopsis thaliana using the genetic YAP1 probe
Hydrogen peroxide (H2O2) reacts, directly or indirectly, with cysteines to form cysteine sulfenic acid, also known as S-sulfenylation. This cysteine oxidation steers diverse cellular processes by altering protein interactions, trafficking, conformation, and function. We present a method to identify ...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2020-12-15 | PXD016723 | Pride
S-sulfenylation Arabidopsis thaliana Post-translational modification Disulfide Cross-link Redox Cysteine oxidation Yap1c 
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