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ProteomicsLeveraging Parameter Dependencies in High-Field Asymmetric Waveform Ion-Mobility Spectrometry and Size-exclusion Chromatography for Proteome-wide Crosslinking Mass Spectrometry_CLMS dataset
Ion mobility spectrometry shows great promise to tackle analytically challenging research questions by adding another separation dimension to liquid chromatography-mass spectrometry. The understanding of how analyte properties influence ion mobility has increased through recent studies but no clear ...
ORGANISM(S): Homo Sapiens (human) Cellular Organisms 
2022-12-16 | PXD022360 | JPOST Repository
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 
ProteomicsLeveraging Parameter Dependencies in High-Field Asymmetric Waveform Ion-Mobility Spectrometry and Size-exclusion Chromatography for Proteome-wide Crosslinking Mass Spectrometry_protein ID dataset
Ion mobility spectrometry shows great promise to tackle analytically challenging research questions by adding another separation dimension to liquid chromatography-mass spectrometry. The understanding of how analyte properties influence ion mobility has increased through recent studies but no clear ...
ORGANISM(S): Homo Sapiens (human) 
2022-12-16 | PXD022341 | JPOST Repository
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
ProteomicsOrbitrap mass spectrometry and high-field asymmetric waveform ion mobility spectrometry (FAIMS) enable the indepth analysis of human serum proteoforms
In this study, we describe a straightforward protocol for intact proteoform sample preparation based on depletion of albumin and immunoglobulins followed by simplified fractionation of remaining serum proteins via polyacrylamide gel electrophoresis. After molecular weight-based fractionation, we sup...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2023-08-02 | MSV000092574 | MassIVE
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
ProteomicsHigh Field Asymmetric Waveform Ion Mobility Spectrometry in Non-targeted Bottom-up Proteomics of Dried Blood Spot
Dried Blood Spots samples are a rich source of proteins and have therefore great potential for proteomics biomarker discovery studies. Only a few articles have used DBS samples for non-targeted bottom-up protein analysis, probably due to the complexity of the DBS samples. Gas-phase separation by ion...
ORGANISM(S): Homo sapiens (Human) 
2018-05-03 | PXD007926 | Pride
Faims Dried blood spot Non-targeted Bottom-up Proteomics 
ProteomicsCapillary Zone Electrophoresis-High Field Asymmetric Ion Mobility Spectrometry-Tandem Mass Spectrometry for Top-down Characterization of Histone Proteoforms
Characterization of histone proteoforms with various post-translational modifications (PTMs) is critical for a better understanding of functions of histone proteoforms in epigenetic control of gene expression. Mass spectrometry (MS)-based top-down proteomics (TDP) is a valuable approach for delineat...
ORGANISM(S): Bos taurus (Bovine) 
2023-12-07 | PXD041357 | Pride
Histone Top-down proteomics High-field asymmetric waveform ion mobility spectrometry Post-translational modification Capillary zone electrophoresis 
ProteomicsHigh Field Asymmetric Waveform Ion Mobility Spectrometry- Mass Spectrometry to Enhance Cardiac Muscle Proteome Coverage
Heart tissue sample preparation for mass spectrometry (MS) analysis that includes pre-fractionation reduces the cellular protein dynamic range and increases the relative abundance of non-sarcomeric proteins. We previously described “IN-Sequence” (IN-Seq) where heart tissue lysate is sequentially par...
ORGANISM(S): Mus musculus (Mouse) 
2023-07-20 | PXD039174 | Pride
Faims Dia-ms Cardiac In-seq 
ProteomicsAGP nLC-MS/MS and nLC-FAIMS-MS/MS
Bottom-up nLC-MS/MS glycoprotein mass spectrometry workflows rely on the generation of a mixture of unmodified and glycosylated peptides via proteolysis. Such methods are challenged by suppression of hydrophilic glycopeptide ions by more abundant, hydrophobic, and readily ionizable unmodified peptid...
ORGANISM(S): Homo sapiens (Human) 
2023-03-11 | PXD036667 | Pride
N-glycopeptide High-field asymmetric waveform ion mobility spectrometry Glycoproteomics Agp Alpha-1-acid glycoprotein Faims 
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