ArticleJournal of the American Society for Mass Spectrometry2025
Hyphenation of Trapped Ion Mobility to Two-Dimensional Mass Spectrometry for Protein Analysis in Complex Biomixtures.
Article in Journal of the American Society for Mass Spectrometry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The analysis of complex biological mixtures remains a significant challenge in mass spectrometry (MS), particularly when using conventional direct infusion MS/MS approaches due to inherent limitations in resolving power and spectral complexity. Here, we demonstrate the integration of trapped ion mobility spectrometry (TIMS) with two-dimensional mass spectrometry (2DMS) to enable high-resolution TIMS-MS/2DMS experiments for detailed protein characterization within mixtures. TIMS provides separation based on the ion's size-to-charge ratio, effectively reducing the occurrence of chimeric tandem mass spectra containing fragments from more than one precursor ion. This coupling allows for an improved peak capacity and reduced ambiguity in tandem spectral interpretation. When applied to a model protein mixture, the TIMS-MS/2DMS method allows resolution of near
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.