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ProteomicsExploring How Workflow Variations in Denaturation-Based Assays Impact Global Protein-Protein Interaction Predictions
Denaturation-based assays such as thermal proximity coaggregation (TPCA) and ion-based proteome-integrated solubility alteration (I-PISA) are powerful tools for mapping global protein-protein interaction (PPI) networks. These workflows utilize different denaturation methods to probe PPIs, however, h...
ORGANISM(S): Homo sapiens (Human) 
2026-02-02 | PXD058773 | Pride
Human Tpca I-pisa Tpp 
ProteomicsExploring How Workflow Variations in Denaturation-Based Assays Impact Global Protein-Protein Interaction Predictions (Influenza A Data)
Denaturation-based assays such as thermal proximity coaggregation (TPCA) and ion-based proteome-integrated solubility alteration (I-PISA) are powerful tools for mapping global protein-protein interaction (PPI) networks. These workflows utilize different denaturation methods to probe PPIs, however, h...
ORGANISM(S): Homo sapiens (Human) Influenza A virus 
2026-02-02 | PXD068620 | Pride
Tpca Infuneza a 
ProteomicsAnalysis of bilirubin-induced bovine serum albumin stability using protein denaturation and quantitative cross-linking mass spectrometry
We report the combination of protein-denaturation stability principles with quantitative cross-linking mass spectrometry using isobaric quantitative protein interaction reporter technologies. This method enables the evaluation of ligand-induced protein engagement through analysis of cross-link rela...
ORGANISM(S): Bos taurus (Bovine) 
2024-07-03 | PXD036649 | Pride
Quantitative cross-linking Protein stability Mass spectrometry 
ProteomicsChemical Denaturation and Protein Precipitation (CPP) on E. coli lysate
Chemical Denaturation and Protein Precipitation (CPP) was performed on an E. coli lysate in order to determine the precipitaiton midpoint for the proteome
ORGANISM(S): Escherichia coli 
2023-01-03 | PXD036219 | Pride
Cpp E. coli Precipitation 
UnknownHyperthermophile protein behavior: partially-structured conformations of Pyrococcus furiosus rubredoxin monomers generated through forced cold-denaturation and refolding.
Not available
S-EPMC3945965 | biostudies-literature
UnknownTemperature and urea induced denaturation of the TRP-cage mini protein TC5b: A simulation study consistent with experimental observations.
Not available
S-EPMC2786973 | biostudies-literature
UnknownStudying Protein-Ligand Interactions by Protein Denaturation and Quantitative Cross-Linking Mass Spectrometry.
Not available
S-EPMC10848897 | biostudies-literature
UnknownThermodynamics of protein denaturation at temperatures over 100 °C: CutA1 mutant proteins substituted with hydrophobic and charged residues.
Not available
S-EPMC4620440 | biostudies-literature
UnknownRecipes for Inducing Cold Denaturation in an Otherwise Stable Protein.
Not available
S-EPMC9052743 | biostudies-literature
UnknownIn-Vial Detection of Protein Denaturation Using Intrinsic Fluorescence Anisotropy.
Not available
S-EPMC9909669 | biostudies-literature
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