ArticleJACS Au2023
False-Positive Glycopeptide Identification via In-FAIMS Fragmentation.
Article in JACS Au, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers, 1 of them a synthesis that pooled it.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
11 citing papers in PubMed, 1 synthesis or guideline pooled it, 17 citations in OpenAlex.
- Properties, Origin, and Consistency of Truncated Proteoforms Across Top-Down Proteomic Studies.Molecular & cellular proteomics : MCP · 2025Pooled it
- Site-specific O-glycans influence lacritin structure and multimerization in tears.Protein science : a publication of the Protein Society · 2026Article
- Article
- Extracting informative glycan-specific ions from glycopeptide MS/MS spectra with GlyCounter.bioRxiv : the preprint server for biology · 2025Article
- PNGaseF-Generated N-Glycans Adduct onto Peptides in the Gas Phase.Journal of the American Society for Mass Spectrometry · 2025Article
- Quantification and Site-Specific Analysis of Co-occupied N- and O-Glycopeptides.Journal of proteome research · 2024Article
- A Tutorial Review of Labeling Methods in Mass Spectrometry-Based Quantitative Proteomics.ACS measurement science au · 2024Review
- Quantification and site-specific analysis of co-occupied N- and O-glycopeptides.bioRxiv : the preprint server for biology · 2024Article
- Glycoproteomics: Charting new territory in mass spectrometry and glycobiology.Journal of mass spectrometry : JMS · 2024Review
- Instrumentation at the Leading Edge of Proteomics.Analytical chemistry · 2024Review
- Software Design and Analytical Challenges for Confident Glycopeptide Identification With Data-Independent Acquisition.Mass spectrometry reviewsReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
High-field asymmetric waveform ion mobility spectrometry (FAIMS) separates glycopeptides in the gas phase prior to mass spectrometry (MS) analysis, thus offering the potential to analyze glycopeptides without prior enrichment. Several studies have demonstrated the ability of FAIMS to enhance glycopeptide detection but have primarily focused on N-glycosylation. Here, we evaluated FAIMS for O-glycoprotein and mucin-domain glycoprotein analysis using samples of varying complexity. We demonstrated that FAIMS was useful in increasingly complex samples as it allowed for the identification of more glycosylated species. However, during our analyses, we observed a phenomenon called "in FAIMS fragmentation" (IFF) akin to in source fragmentation but occurring during FAIMS separation. FAIMS experiments showed a 2- to 5-fold increase in spectral matches from IFF compared with control experiments. These results were also replicated in previously published data, indicating that this is likely a systemic occurrence when using FAIMS. Our study highlights that although there are potential benefits to using FAIMS separation, caution must be exercised in data analysis because of prevalent IFF, which may limit its applicability in the broader field of O-glycoproteomics.
Identifiers
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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.