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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
Increasingly, biochemical co-fractionation-based approaches are used to study interactomes and protein complexes at high throughput. The devised methods facilitate the qualitative assignment and prediction of hundreds of putative cellular assemblies in one experiment and without dependency on geneti...
ORGANISM(S): Homo sapiens (Human) 
2019-01-11 | PXD007038 | Pride
directDIA proteomics raw data of plasma extracellular vesicles isolated by SEC and UC
ORGANISM(S): Homo Sapiens 
The aim of the study was to separate the proteins from Naja ashei venom with the use of SEC followed by IEX in order to obtain and functionally characterize purified toxins.
ORGANISM(S): Naja ashei 
2024-08-12 | PXD033540 | Pride
It has become increasingly clear that biological functions depend not only on the identity and quantity, but also the correct interplay among the biomolecules that constitute the cell. Importantly, proteins as the key effectors in the cell dynamically organize into complexes. This study describes a ...
ORGANISM(S): Homo sapiens (Human) 
2019-05-10 | PXD010288 | Pride
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
In living cells most proteins are organized in stable or transient functional assemblies known as protein complexes, which control a multitude of vital cellular processes such as cell cycle progression, metabolism, and signal transduction. System-wide workflows for analysis of protein complexes usin...
ORGANISM(S): Homo sapiens (Human) 
2022-05-06 | PXD018033 | Pride
Data from ProteomeXchange, PXD ID: PXD001220. File: PT1541S1F02.mzml. Published as part of Mol Cell Proteomics. 2013 Dec;12(12):3851-73 . From the Abstract: {{i}} Proteins form a diverse array of complexes that mediate cellular function and regulation. A largely unexplored feature of such protein c...
ORGANISM(S): Homo_sapiens_viruses, Human_female 
Chemical cross-linking in combination with mass spectrometry (XL-MS) has emerged as a useful method for structural elucidation of proteins and protein complexes. Efficient enrichment procedures are necessary to analyze cross-linked products due to their relatively low abundance. Currently, strong ca...
ORGANISM(S): Homo sapiens (Human) 
2022-06-16 | PXD023817 | Pride
Phaeodactylum tricornutum (UTEX 646) grown without silica were used to generate a native protein extract. Extraction involved multiple freeze/thaw cycles, sonication, and solubilization in buffer containing 1% NP40. Following chromatographic separation by SEC or IEX the fractions were reduced/alkyl...
ORGANISM(S): Phaeodactylum Tricornutum (ncbitaxon:2850) 
2023-04-03 | MSV000091621 | MassIVE
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