Sort   by:  
 Page size 
MetabolomicsQuantification of Dissolved Metabolites in Environmental Samples through Cation-Exchange Solid Phase Extraction (CX-SPE) paired with Liquid Chromatography-Mass Spectrometry
Not available
ST002292 | MetabolomicsWorkbench
TranscriptomicsThe protein disulfide isomerase AGR2 is essential for the production of intestinal mucus
Protein disulfide isomerases (PDIs) aid protein folding and assembly by catalyzing formation and shuffling of cysteine disulfide bonds in the endoplasmic reticulum (ER). Many members of the PDI family are expressed in mammals but the roles of specific PDIs in vivo are poorly understood. A recent hom...
ORGANISM(S): Mus musculus 
2010-05-19 | E-GEOD-12503 | biostudies-arrayexpress
UnknownThiol-Disulfide Exchange in Human Growth Hormone.
Not available
S-EPMC4854756 | biostudies-literature
UnknownThiol-disulfide exchange in peptides derived from human growth hormone.
Not available
S-EPMC4283463 | biostudies-literature
ProteomicsStructural characterization of intra- and intermolecular disulfide bonds in Voltage-Dependent Anion Channel 3 (VDAC3) protein from Rattus norvegicus by high-resolution mass spectrometry
Voltage-Dependent Anion Channels, the most abundant proteins of the mitochondrial outer membrane, are responsible for exchange of ions and metabolites between cytosol and mitochondria. They participate in the control of glycolytic metabolism through interaction with numerous enzymes and play a key r...
ORGANISM(S): Rattus norvegicus (Rat) 
2025-09-08 | PXD064110 | Pride
High-resolution mass spectrometry  intra- and intermolecular disulfide bonds  rattus voltage-dependent anion selective channel isoform 3 (rvdac3)  cysteine redox state  structural characterization 
UnknownBiomimetic selenocystine based dynamic combinatorial chemistry for thiol-disulfide exchange.
Not available
S-EPMC7794297 | biostudies-literature
ProteomicsGlobal Profiling of Human Proteome Cysteine Residues via Lipoic Acid-Mediated Disulfide Exchange
Lipoic acid, an endogenous small molecule, is widely utilized in metabolic regulation and disease intervention. While its mechanism of action has been largely attributed to protein lipoylation, the dynamic chemical properties of its five-membered cyclic disulfide moiety remain underexplored. Here, w...
ORGANISM(S): Homo sapiens (Human) 
2026-05-23 | PXD067385 | Pride
Covalent probe Cysteine Disulfide exchange Chemoproteomics Lipoic acid 
ProteomicsGlobal Profiling of Human Proteome Cysteine Residues via Lipoic Acid-Mediated Disulfide Exchange
Lipoic acid, an endogenous small molecule, is widely utilized in metabolic regulation and disease intervention. While its mechanism of action has been largely attributed to protein lipoylation, the dynamic chemical properties of its five-membered cyclic disulfide moiety remain underexplored. Here, w...
ORGANISM(S): Homo sapiens (Human) 
2026-05-23 | PXD067411 | Pride
Covalent probe Cysteine Disulfide exchange Chemoproteomics Lipoic acid 
ProteomicsGlobal Profiling of Human Proteome Cysteine Residues via Lipoic Acid-Mediated Disulfide Exchange
Lipoic acid, an endogenous small molecule, is widely utilized in metabolic regulation and disease intervention. While its mechanism of action has been largely attributed to protein lipoylation, the dynamic chemical properties of its five-membered cyclic disulfide moiety remain underexplored. Here, w...
ORGANISM(S): Homo sapiens (Human) 
2026-05-23 | PXD067366 | Pride
Covalent probe Cysteine Disulfide exchange Chemoproteomics Lipoic acid 
UnknownA single disulfide bond disruption in the β3 integrin subunit promotes thiol/disulfide exchange, a molecular dynamics study.
Not available
S-EPMC3601072 | biostudies-literature
Sort   by:  
 Page size