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MetabolomicsIntegrating two chromatographies in a co-fractionation mass spectrometry approach improved protein-metabolite interactions (PMIs) mapping capabilities and revealed novel protein-ligand pairings in Escherichia coli.
The protein-metabolite interactome remains understudied. We previously developed a co-fractionation mass-spectrometry-based approach called PROMIS to address this gap. PROMIS relies on size separation chromatography of protein-metabolite complexes from lysates, followed by proteomics and metabolomic...
2025-04-25 | MTBLS9098 | MetaboLights
ProteomicsCFdb: A harmonized resource of co-fractionation mass spectrometry data
A total of 411 co-fractionation mass spectrometry (CF-MS) experiments were downloaded from public proteomics repositories such as PRIDE and MassIVE, then re-analyzed with MaxQuant. This repository provides complete MaxQuant outputs from all 411 experiments.
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) Mus musculus (Mouse) Trypanosoma brucei Drosophila melanogaster (Fruit fly) Oryza sativa (Rice) Caenorhabditis elegans Dictyostelium discoideum (Slime mold) Zea mays (Maize) Homo sapiens (Human) Triticum aestivum (Wheat) Escherichia coli Rattus norvegicus (Rat) Xenopus laevis (African clawed frog) 
2024-01-26 | PXD042664 | Pride
Cf-ms Protein correlation profiling Protein complexes Co-fractionation mass spectrometry Interactome 
ProteomicsIn Situ Cross-linking Based Co-Fractionation Mass Spectrometry (XL-CoFrac-MS)
We developed an in situ cross-linking coupled reversed-phase liquid chromatography-based co-fractionation mass spectrometry (XL-CoFrac-MS) platform to analyze drug-induced protein complex changes. A software tool, ChromaQuant, was built to automate chromatographic peak quantification. Using RS4;11 l...
ORGANISM(S): Homo Sapiens 
2025-08-23 | PXD067673 |
ProteomicsSystematic reanalysis of co-fractionation mass spectrometry data
A total of 206 co-fractionation mass spectrometry (CF-MS) experiments were downloaded from public proteomics repositories such as PRIDE and MASSIVE, then re-analyzed with MaxQuant.
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) Zea mays (Maize) Homo sapiens (Human) Mus musculus (Mouse) Trypanosoma brucei Triticum aestivum (Wheat) Saccharomyces cerevisiae (Baker's yeast) Oryza sativa (Rice) Drosophila melanogaster (Fruit fly) Caenorhabditis elegans Dictyostelium discoideum (Slime mold) Xenopus laevis (African clawed frog) 
2021-04-20 | PXD022048 | Pride
Cf-ms 
ProteomicsAnalytical guidelines for co-fractionation mass spectrometry obtained through global profiling of gold standard Saccharomyces cerevisiae protein complexes
Co-fractionation mass spectrometry (CF-MS) is a technique with potential to characterise endogenous and unmanipulated protein complexes on an unprecedented scale. However this potential has been offset by a lack of guidelines for best-practice CF-MS data collection and analysis. To obtain such guide...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2020-08-24 | PXD019513 | Pride
Protein correlation profiling Co-fractionation mass spectrometry Protein complexes Reference complex profiling Protein-protein interactions 
UnknownCo-fractionation/mass spectrometry to identify protein complexes.
Not available
S-EPMC7960544 | biostudies-literature
UnknownMapping protein states and interactions across the tree of life with co-fractionation mass spectrometry.
Not available
S-EPMC10724252 | biostudies-literature
UnknownScalable multiplex co-fractionation/mass spectrometry platform for accelerated protein interactome discovery.
Not available
S-EPMC9279285 | biostudies-literature
ProteomicsProfiling protein-protein interactions in human brain by refined co-fractionation mass spectrometry
Proteins are essential regulators of biological processes and can have diverse functions depending on their interactions with other proteins. To understand deeply the interaction and their complexes, co-fractionation mass spectrometry (CF-MS) was used with ion exchange chromatography columns and dat...
ORGANISM(S): Homo sapiens (Human) 
2024-03-21 | PXD044084 | Pride
Protein-protein interaction Co-fractionation mass spectrometry Data-independent acquisition 
ProteomicsProfiling protein-protein interactions in human brain by refined co-fractionation mass spectrometry
Proteins are essential regulators of biological processes and can have diverse functions depending on their interactions with other proteins. To understand deeply the interaction and their complexes, co-fractionation mass spectrometry (CF-MS) was used with ion exchange chromatography columns and dat...
ORGANISM(S): Homo sapiens (Human) 
2024-03-21 | PXD044083 | Pride
Protein-protein interaction Co-fractionation mass spectrometry Data-independent acquisition 
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