ArticleThe Analyst2023
Characterizing the top-down sequencing of protein ions prior to mobility separation in a timsTOF.
Article in The Analyst, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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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.
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Who cites it
11 citing papers in PubMed.
- Stabilizing Proteins by Chemical Cross-Linking: Insights into Conformation, Unfolding, and Aggregation Using Native Ion Mobility Mass Spectrometry.Analytical chemistry · 2025Article
- Top-Down Proteomics: Why and When?Proteomics · 2025Article
- Collision-Induced Unfolding of High-Journal of the American Society for Mass Spectrometry · 2025Article
- Untargeted Discovery and Localization of Isomerized Residues in Neuropeptides.Analytical chemistry · 2025Article
- Adapting a Trapped Ion Mobility Spectrometry-Q-TOF for HighAnalytical chemistry · 2025Article
- Ion Mobility-Assisted Free Radical-Initiated Peptide Sequencing.International journal of mass spectrometry · 2025Article
- Improved Annotation of Internal Fragments via Trapped-Ion Mobility Enhanced Top-Down Sequencing of Protein Ions.Journal of mass spectrometry : JMS · 2025Article
- A Conformation-Specific Approach to Native Top-down Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2024Article
- Mobility-Assisted Pseudo-MSJournal of the American Society for Mass Spectrometry · 2024Article
- Crossing epigenetic frontiers: the intersection of novel histone modifications and diseases.Signal transduction and targeted therapy · 2024Review
- The path forward for protein footprinting, covalent labeling, and mass spectrometry-based protein conformational analyses.Journal of mass spectrometry : JMS · 2024Review
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Mass spectrometry (MS)-based proteomics workflows of intact protein ions have increasingly been utilized to study biological systems. These workflows, however, frequently result in convoluted and difficult to analyze mass spectra. Ion mobility spectrometry (IMS) is a promising tool to overcome these limitations by separating ions by their mass- and size-to-charge ratios. In this work, we further characterize a newly developed method to collisionally dissociate intact protein ions in a trapped ion mobility spectrometry (TIMS) device. Dissociation occurs prior to ion mobility separation and thus, all product ions are distributed throughout the mobility dimension, enabling facile assignment of near isobaric product ions. We demonstrate that collisional activation within a TIMS device is capable of dissociating protein ions up to 66 kDa. We also demonstrate that the ion population size within the TIMS device significantly influences the efficiency of fragmentation. Lastly, we compare CIDtims to the other modes of collisional activation available on the Bruker timsTOF and demonstrate that the mobility resolution in CIDtims enables the annotation of overlapping fragment ions and improves sequence coverage.
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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.