Evidence map›Paper›PMID 40391882›Full record

ArticleMolecular omics2025

Analysis of FAIMS for the study of affinity-purified protein complexes using the orbitrap ascend tribrid mass spectrometer.

Pratik Goswami, Joseph Cesare, Michaella J Rekowski, Zachary Clark, Janet Thornton, Michael P Washburn

Abstract read
In one paragraph

Article in Molecular omics, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

4 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Pratik GoswamiDepartment of Cancer Biology, University of Kansas Medical Center, Kansas City, KS, 66160, USA. mwashburn4@kumc.edu.
Joseph CesareDepartment of Cancer Biology, University of Kansas Medical Center, Kansas City, KS, 66160, USA. mwashburn4@kumc.edu.
Michaella J RekowskiDepartment of Cancer Biology, University of Kansas Medical Center, Kansas City, KS, 66160, USA. mwashburn4@kumc.edu.
Zachary ClarkDepartment of Cancer Biology, University of Kansas Medical Center, Kansas City, KS, 66160, USA. mwashburn4@kumc.edu.
Janet ThorntonDepartment of Cancer Biology, University of Kansas Medical Center, Kansas City, KS, 66160, USA. mwashburn4@kumc.edu.
Michael P WashburnDepartment of Cancer Biology, University of Kansas Medical Center, Kansas City, KS, 66160, USA. mwashburn4@kumc.edu.ORCID http://orcid.org/0000-0001-7568-2585

Funding

Decoding the Assembly and Function of Paralogue Specific SIN3A and SIN3B Human Chromatin Remodeling Complexes and NetworksR35GM145240 · NIGMS · UNIVERSITY OF KANSAS MEDICAL CENTER · PI MICHAEL P WASHBURN · 2022 to 2026
$1.9M
Kansas Medical Scientist Training ProgramT32GM138077 · NIGMS · UNIVERSITY OF KANSAS MEDICAL CENTER · PI TIMOTHY A FIELDS · 2020 to 2026
$1.6M
NIGMS NIH HHS R35 GM145240NIGMS NIH HHS T32 GM138077
6 · The paper itself

Abstract

In this study, we analyzed the combination of affinity purification mass spectrometry (AP-MS) with high-field asymmetric waveform ion mobility spectrometry (FAIMS), integrated between nanoLC-MS and an Orbitrap Ascend tribrid mass spectrometer. Our primary objective was to evaluate the application of the FAIMS interface for detecting affinity purified SAP25 protein complexes with enhanced sensitivity and robustness. As a result, we observed that nanoLC-FAIMS-MS (with FAIMS) significantly improved the sensitivity and detection limits at the protein level, peptide level and significantly reduced chemical contaminants compared to nanoLC-MS alone without FAIMS (No FAIMS). This FAIMS configuration resulted in 42% and 92% increases for the total proteins and unique proteins, respectively, and 44% and 88% increases for total peptides and unique peptides compared to the No FAIMS configuration. Our in-depth comparison of FAIMS and No FAIMS shows that FAIMS outperforms by significantly reducing the missing value by <15% in datasets and plays a significant role in filtering chemical contaminants. Lastly, we searched the datasets for multiple post-translational modifications important in chromatin remodeling and found several arginine methylation sites on the bait protein SAP25. Our findings highlight the potential of FAIMS with Orbitrap Ascend tribrid mass spectrometer to enhance the depth of AP-MS analysis. The data were deposited with the MASSIVE repository with the identifier MSV000096548.

Indexed as

Ion Mobility SpectrometryMass SpectrometrySaccharomyces cerevisiae ProteinsChromatography, AffinityPeptidesProtein Processing, Post-TranslationalProteomicsPeptidesSaccharomyces cerevisiae Proteins

Identifiers

PMID40391882
PMCPMC12234230

What OpenQuestion holds

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LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

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.