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ProteomicsOrbitrap mass spectrometry and high-field asymmetric waveform ion mobility spectrometry (FAIMS) enable the in-depth analysis of human serum proteoforms
After molecular weight-based fractionation, we supplemented the traditional liquid chromatography tandem mass spectrometry (LC-MS2) data acquisition with high-field asymmetric waveform ion mobility spectrometry (FAIMS), which served as an additional separation dimension to further simplify serum pro...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2023-02-16 | MSV000091309 | MassIVE
ProteomicsIMPROVED N- AND O-GLYCOPEPTIDE IDENTIFICATION USING HIGH-FIELD ASYMMETRIC WAVEFORM ION MOBILITY SPECTROMETRY (FAIMS)
Mass spectrometry is the premier tool for identifying and quantifying site-specific protein glycosylation globally. Analysis of intact glycopeptides often requires an enrichment step, after which the samples remain highly complex and exhibit a broad dynamic range of abundance. Here, we evaluated th...
ORGANISM(S): Homo sapiens (Human) 
2023-10-24 | PXD038673 | Pride
Faims N-glycopeptides Mass spectrometry O-glycopeptides Glycoproteomics 
ProteomicsFAIMS enhances the detection of PTM crosstalk sites
Protein post-translational modification (PTMs) enable cells to rapidly change in response to biological stimuli. With over 400 PTMs, understanding these control mechanisms is complex. To date, efforts have focused on investigating the effect of single PTMs on protein function. Yet, many proteins con...
ORGANISM(S): Homo sapiens (Human) 
2025-03-11 | PXD026448 | Pride
Faims Lc-ms Post-translational modifications Interplay Crosstalk 
ProteomicsAccurate quantitative proteomic analyses using metabolic labeling and High Field Asymmetric Waveform Ion Mobility Spectrometry (FAIMS)
Stable isotope labeling by amino acids in cell culture (SILAC) is routinely used to profile changes in protein and peptide abundance across different experimental paradigms. As with other quantitative proteomic approaches, the detection of peptide isotopomers can be limited by the presence of interf...
ORGANISM(S): Homo sapiens (Human) 
2019-05-28 | PXD012924 | Pride
Phosphorylation High field asymmetric waveform ion mobility spectrometry (faims) Stable isotope labeling by amino acids in culture (silac) Quantitative proteomics 
ProteomicsFalse positive glycopeptide identification through in-FAIMS glycan fragmentation.
Glycosylation is an important post-translational modification characterized by extensive heterogeneity. While mass spectrometry (MS) is the premier technique to characterize glycoproteins, the study of intact glycopeptides presents challenges often not observed in the study of unmodified species. Hi...
ORGANISM(S): Homo sapiens (Human) 
2023-09-11 | PXD041217 | Pride
Glycoproteomics Mucinomics faims Mucin-domain glycoproteomics Enrichment. Ion mobility separation 
ProteomicsA Compact Quadrupole-Orbitrap Mass Spectrometer with FAIMS Interface Improves Proteome Coverage in Short LC Gradients
State-of-the-art proteomics-grade mass spectrometers can measure peptide precursors and their fragments with ppm mass accuracy at sequencing speeds of tens of peptides per second with attomolar sensitivity. Here we describe a compact and robust quadrupole-orbitrap mass spectrometer equipped with a f...
ORGANISM(S): Homo sapiens (Human) Rattus norvegicus (Rat) 
2020-02-17 | PXD016662 | Pride
Faims Dia Tmt Bottom-up shotgun proteomics Phosphoproteomics Orbitrap Dda 
ProteomicsHigh-field asymmetric waveform ion mobility spectrometry interface enhances parallel reaction monitoring on an Orbitrap mass spectrometer
High-field asymmetric waveform ion mobility spectrometry (FAIMS) enables gas phase separations on a chromatographic timescale and has become a useful tool for proteomic applications. Despite its emerg-ing utility, however, the molecular determinants underlying peptide separation by FAIMS have not be...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2022-03-07 | MSV000089014 | MassIVE
ProteomicsFAIMS-GPF XL-MS: crosslinking-mass spectrometry based on gas-phase fractionation
Protein-protein interactions (PPIs) underpin nearly all cellular processes; therefore, mapping PPI and protein-protein association networks is critical for understanding how biological systems function in health and disease. However, many functionally relevant PPIs are transient and mediated by weak...
ORGANISM(S): Homo sapiens (Human) 
2026-05-27 | PXD064228 | Pride
Faims Cross-linking mass spectrometry Structural biology Interactomics 
UnknownFalse-Positive Glycopeptide Identification via In-FAIMS Fragmentation.
Not available
S-EPMC10523363 | biostudies-literature
ProteomicsGetting more out of co-immunoprecipitation mass spectrometry experiments by reducing interference using FAIMS
Co-immunoprecipitation of proteins coupled to mass spectrometry has transformed modern biology’s understanding of protein interaction networks. These approaches exploit the selective isolation of tagged proteins by affinity enrichment / purification to identify protein binding partners at scale and ...
ORGANISM(S): Homo sapiens (Human) Rabies virus Nishigahara RCEH 
2025-10-15 | PXD026637 | Pride
Faims Co-ip mass spectrometry Proteomics Ion mobility 
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