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ProteomicsProAlanase is an effective alternative to trypsin for proteomics applications and disulfide bond mapping
Trypsin is the protease of choice in bottom-up proteomics. However, its application can be limited by the amino acid composition of target proteins and the pH of digestion solution. In this study we characterized ProAlanase, a protease from the fungus Aspergillus niger that cleaves primarily on the ...
ORGANISM(S): Homo sapiens (Human) Loxodonta africana (African elephant) 
2020-10-19 | PXD019039 | Pride
Sequence coverage Proline-rich Disulfide mapping Low-ph Proteomics Phosphorylation De novo sequencing Disulfide bonds Proalanase 
ProteomicsProAlanase is an effective alternative to trypsin for proteomics applications and disulfide bond mapping_part2
Trypsin is the protease of choice in bottom-up proteomics. However, its application can be limited by the amino acid composition of target proteins and the pH of digestion solution. In this study we characterized ProAlanase, a protease from the fungus Aspergillus niger that cleaves primarily on the ...
ORGANISM(S): Homo sapiens (Human) 
2020-10-19 | PXD021191 | Pride
Sequence coverage Proline-rich Disulfide mapping Low-ph Proteomics Phosphorylation De novo sequencing Disulfide bonds Histone ptms Proalanase Histone variants 
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
ProteomicsProAlanase is an effective alternative to trypsin for proteomics applications and disulfide bond mapping_part3
Trypsin is the protease of choice in bottom-up proteomics. However, its application can be limited by the amino acid composition of target proteins and the pH of the digestion solution. In this study we characterize ProAlanase, a protease from the fungus Aspergillus niger that cleaves primarily on t...
ORGANISM(S): Homo sapiens (Human) 
2020-10-19 | PXD021703 | Pride
Sequence coverage Proline-rich Low-ph Histones Proteomics Phosphorylation De novo sequencing Disulfide bonds Proalanase 
ProteomicsA-to-I mRNA editing controls disulfide bond formation and the toxicity of the HokB toxin in bacteria
Protein disulfide bonds between cysteine residues serve a prominent role in bacterial protein function, virulence, and viability. Adenosine-to-inosine (A-to-I) mRNA editing changes the genetic information at the RNA level. Previously, we discovered that A-to-I mRNA editing occurs in bacteria (Escher...
ORGANISM(S): Escherichia coli 
2025-07-14 | PXD051162 | Pride
Tada Adenosine-to-inosine rna editing Toxin-antitoxin Disulfide bond Hokb Bacteria Dsba 
ProteomicsDisulfide Bond Shuffling Induces Molecular Crosstalk: Delayed Insulin Aggregation and Enhanced Neurotoxicity
Our study explores the novel concept of disulfide bond shuffling-provoked oligomer crosstalk in insulin. We demonstrate that this dynamic process not only modulates the aggregation kinetics of insulin but also significantly influences its cytotoxic potential. Through a combination of biophysical tec...
ORGANISM(S): Mus musculus (Mouse) 
2025-07-23 | PXD053868 | Pride
Disulfide Neurotoxicity Ion mobility-mass spectrometry Disulfide bond shuffling Insulin 
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 
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 
ProteomicsCysteine oxidation and disulfide formation in the ribosomal exit tunnel
Understanding the conformational sampling of translation-arrested ribosome nascent chain complexes is key to understand co-translational folding. Up to now, coupling of cysteine oxidation, disulfide bond formation and structure formation in nascent chains has remained elusive. Here, we investigate t...
ORGANISM(S): Bos taurus (Bovine) Escherichia coli 
2020-11-09 | PXD021574 | Pride
Glutathione Ribosomal exit tunnel Cysterine oxidation Disulfide formation 
ProteomicsRevealing disulfide bond formation in GSDME upon UVC irradiation under non-reducing conditions
It is widely acknowledged that gasdermin family proteins, which are known as the executors of pyroptosis, undergo protease-mediated cleavage prior to inducing pyroptosis. Here, we unexpectedly discovered a non-canonical form of pyroptosis mediated by full-length GSDME (FL-GSDME) without any proteoly...
ORGANISM(S): Homo sapiens (Human) 
2024-06-17 | PXD051840 | Pride
Uvc gsdme disulfide bond 
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