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ProteomicsCharacterization of disulfide linkages in proteins by 193 nm ultraviolet photodissociation (UVPD)
Inter-linked disulfide bonds connecting peptide chains are homolytically cleaved with 193 nm ultraviolet photodissociation (UVPD). Analysis of insulin demonstrates the ability for UVPD to cleave multiple disulfide bonds and provide sequence coverage of multiple peptide chains in the same MS/MS event...
ORGANISM(S): Homo Sapiens (human) Gallus Gallus Bos Taurus 
2018-04-28 | PXD009460 | JPOST Repository
ProteomicsA Novel Mechanism Mediated by Allosteric Disulfide Bonds Fine-Tunes Thrombus Formation
Mapping of disulfide bonds and quantification of their redox state in the human histidine rich glycoprotein
ORGANISM(S): Homo sapiens (Human) 
2024-04-11 | PXD050718 | Pride
Histidine rich glycoprotein Hrg Disulfide bonds Redox state 
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
ProteomicsIdentification of intramolecular disulfide bonds in GrxS12
To investigate whether the conserved Cys residues of Grxs form intramolecular or intermolecular disulfide bonds, the recombinant GrxS12 proteins were purified, and subsequently separated using non-reducing SDS-PAGE. The gel revealed the presence of a monomer band but not a dimer band, indicating the...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2026-01-16 | PXD058877 | Pride
Grxs12 Identification Intramolecular disulfide bond 
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 
ProteomicsMultiple disulfide-bonded states confer conformational diversity in fibrinogen
Disulfide bonds constrain the polypeptide backbone and reduce conformational variability in proteins. The blood clotting protein fibrinogen is constitutively produced as multiple partially disulfide-bonded states, suggesting that individual fibrinogen molecules have a variety of conformational forms...
ORGANISM(S): Homo sapiens (Human) 
2026-04-13 | PXD076459 | Pride
Human Fibrinogen Disulfide bonds 
ProteomicsAllosteric disulfide control of ligand binding and endocytosis of KIR2DL4, the natural killer cell receptor for HLA-G
Mapping of disulfide bonds and quantification of their redox state in human KIR2DL4 receptor
ORGANISM(S): Homo sapiens (Human) 
2026-09-16 | PXD083525 | Pride
Hla-g Natural killer cell Protein disulfide isomerase Endocytosis Kir2dl4 
TranscriptomicsMuscleblind-like proteins dimerize by forming disulfide bonds to influence regulation of alternative splicing
Muscleblind-like (MBNL) RNA-binding proteins (RBPs) possess modular domains that contribute to their regulation of alternative splicing and RNA localization. MBNL dimerization may play a role in these functions, but the mechanism is not well understood. Here we identify a cysteine residue in the uns...
ORGANISM(S): Mus musculus 
2026-03-08 | GSE291521 | GEO
ProteomicsMechano-redox control of Mac-1 de-adhesion from ICAM-1 by protein disulfide isomerase promotes directional movement under flow
Quantification of the redox state of disulfide bonds in the beta 2 subunit of human recombinant Mac-1 integrin.
ORGANISM(S): Homo sapiens (Human) 
2023-04-09 | PXD032688 | Pride
Mac-1 Disulfide bonds Redox state 
ProteomicsDisulfide bonds are critical for stabilizing cell division, cell envelope biogenesis, and antibiotic resistance proteins in mycobacteria
Mycobacterium, including Mycobacterium tuberculosis, the etiological agent of tuberculosis, have a unique cell envelope critical for their survival and antibacterial resistance. The cell envelope's assembly and maintenance influence permeability, making it a key target against multidrug resistant st...
ORGANISM(S): Mycobacterium Smegmatis Str. Mc2 155 (ncbitaxon:246196) 
2025-01-16 | MSV000096877 | MassIVE
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