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MetabolomicsRapid chromatography combined with trapped ion mobility mass spectrometry for analysis of derivatized small molecules
Liquid chromatography (LC) separates biomolecules based on their physicochemical properties. Reproducible retention times support compound identification, while efficient separation of structurally similar compounds is essential for accurate quantification. However, conventional LC methods are often...
2026-06-30 | MTBLS14813 | MetaboLights
MetabolomicsTrapped ion mobilty improves annotation accuracy in LC-HRMS screening applications for exposomics

The widespread use of a large number of chemicals results in a significant exposure of humans and the environment, posing potential risks to human health and ecosystems. To assess the exposure to chemical mixtures, screening applications covering a large number of analytes based on liquid chromat...

2025-10-14 | MTBLS11753 | MetaboLights
MetabolomicsFour-dimensional trapped ion mobility spectrometry lipidomics for high throughput clinical profiling of human blood samples
Not available
ORGANISM(S): Homo sapiens 
ST002402 | MetabolomicsWorkbench
ProteomicsExtending the Separation Space with Trapped Ion Mobility Spectrometry Improves the Accuracy of Isobaric Tag-based Quantitation in Proteomic LC/MS/MS
Two-dimensional separation by nano-LC and trapped ion mobility spectrometry (TIMS) prior to Q-TOF tandem mass spectrometry significantly improves the accuracy of isobaric tag-based quantitation in proteome analysis without the need for additional measurement time for TIMS insertion. The obtained pea...
ORGANISM(S): Cellular Organisms 
2020-05-22 | PXD018650 | JPOST Repository
ProteomicsEffect of Phosphorylation on the Collision Cross Sections of Peptide Ions in Ion Mobility Spectrometry
The insertion of ion mobility spectrometry (IMS) between LC and MS can improve peptide identification in both proteomics and phosphoproteomics by providing structural information that is complementary to LC and MS, because IMS separates ions on the basis of differences in their shapes and charge sta...
ORGANISM(S): Homo Sapiens (human) 
2021-01-14 | PXD019746 | JPOST Repository
ProteomicsAlphaTims: Indexing unprocessed trapped ion mobility spectrometry - time of flight data for fast and easy accession and visualization
High resolution mass spectrometry-based proteomics generates large amounts of data, even in the standard liquid chromatography (LC) – tandem mass spectrometry configuration. Adding an ion mobility dimension vastly increases the acquired data volume, challenging both analytical processing pipe...
ORGANISM(S): Homo sapiens (Human) 
2021-07-30 | PXD027359 | Pride
Software. Time of flight Ion mobility spectrometry Data indexing Mass spectrometry Data visualization 
ProteomicsOnline parallel accumulation – serial fragmentation (PASEF) with a novel trapped ion mobility mass spectrometer
In bottom-up proteomics, peptides are separated by liquid chromatography with elution peak widths in the range of seconds, while mass spectra are acquired in about 100 microseconds with time-of-fight (TOF) instruments. This allows adding ion mobility as a third dimension of separation. Among several...
ORGANISM(S): Homo sapiens (Human) Escherichia coli 
2018-11-06 | PXD010012 | Pride
Tims Pasef Technological 
ProteomicsOptimizing single cell proteomics on a trapped ion mobility spectrometry for label-free experiments
Although single cell RNA-seq has had a tremendous impact on biological research, a corresponding technology for unbiased mass spectrometric analysis of single cells has only recently become available. Significant technological breakthroughs including miniaturized sample handling have enabled proteom...
ORGANISM(S): Homo sapiens (Human) 
2024-08-02 | PXD039066 | Pride
Dda-pasef Primary t cells Label-free 
ProteomicsIn-depth proteomic analysis of Plasmodium berghei sporozoites using trapped ion mobility spectrometry with parallel accumulation-serial fragmentation
We took advantage of a novel highly sensitive timsTOF PRO mass spectrometer, based on trapped ion mobility spectrometry with parallel accumulation-serial fragmentation. Combined with three alternative methods for sporozoite purification, this approach allowed us to identify the deep proteome of P. b...
ORGANISM(S): Plasmodium berghei ANKA 
2021-02-11 | PXD022735 | Pride
Malaria Mass spectrometry Sporozoites Proteome Plasmodium berghei Timstof pro 
ProteomicsIon Mobility-Tandem Mass Spectrometry of Mucin-type O-Glycans
The dense O-glycosylation of mucins plays an important role in the defensive properties of the mucus hydrogel. Aberrant glycosylation is often correlated with inflammation and pathology such as COPD, cancer, and Crohn’s disease. The inherent complexity of glycans and the diversity in the O-core stru...
ORGANISM(S): Homo sapiens (Human) Sus scrofa domesticus (domestic pig) 
2024-03-19 | PXD050530 | Pride
O-glycans  ion mobility  mass spectrometry  isomeric separation  dda  proteome 
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