Evidence map›Paper›PMID 40524023›Full record

ArticleNature methods2025

Assessment of false discovery rate control in tandem mass spectrometry analysis using entrapment.

Bo Wen, Jack Freestone, Michael Riffle, Michael J MacCoss, William S Noble, Uri Keich

Abstract read
In one paragraph

Article in Nature methods, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing 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

39 citing papers in PubMed.

  1. Article
  2. Mapping the architecture of protein complexes inProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Carafe2 enables high qualitybioRxiv : the preprint server for biology · 2026
    Article
  14. Article
  15. Article
  16. Article
  17. Proteoforms as the true units of physiological function.European journal of applied physiology · 2026
    Review
  18. Article
  19. A Functional Metabolomics Framework to Track Microbiome Drug Metabolism.bioRxiv : the preprint server for biology · 2026
    Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Bo WenDepartment of Genome Sciences, University of Washington, Seattle, WA, USA.ORCID http://orcid.org/0000-0003-2261-3150
Jack FreestoneSchool of Mathematics and Statistics, University of Sydney, Sydney, New South Wales, Australia.
Michael RiffleDepartment of Genome Sciences, University of Washington, Seattle, WA, USA.ORCID http://orcid.org/0000-0003-1633-8607
Michael J MacCossDepartment of Genome Sciences, University of Washington, Seattle, WA, USA.ORCID http://orcid.org/0000-0003-1853-0256
William S NobleDepartment of Genome Sciences, University of Washington, Seattle, WA, USA. william-noble@uw.edu.ORCID http://orcid.org/0000-0001-7283-4715
Uri KeichSchool of Mathematics and Statistics, University of Sydney, Sydney, New South Wales, Australia. uri.keich@sydney.edu.au.ORCID http://orcid.org/0000-0002-3209-5011

Funding

Seattle Quant: A Resource for the Skyline Software EcosystemR24GM141156 · NIGMS · UNIVERSITY OF WASHINGTON · PI Michael MacCoss · 2021 to 2026
$6.7M
National Science Foundation (NSF) 2245300National Science Foundation (NSF) DGE-2140004NIGMS NIH HHS R24 GM141156ODNI | Intelligence Advanced Research Projects Activity (IARPA) W911NF2220059
6 · The paper itself

Abstract

A critical challenge in mass spectrometry proteomics is accurately assessing error control, especially given that software tools employ distinct methods for reporting errors. Many tools are closed-source and poorly documented, leading to inconsistent validation strategies. Here we identify three prevalent methods for validating false discovery rate (FDR) control: one invalid, one providing only a lower bound, and one valid but under-powered. The result is that the proteomics community has limited insight into actual FDR control effectiveness, especially for data-independent acquisition (DIA) analyses. We propose a theoretical framework for entrapment experiments, allowing us to rigorously characterize different approaches. Moreover, we introduce a more powerful evaluation method and apply it alongside existing techniques to assess existing tools. We first validate our analysis in the better-understood data-dependent acquisition setup, and then, we analyze DIA data, where we find that no DIA search tool consistently controls the FDR, with particularly poor performance on single-cell datasets.

Indexed as

ProteomicsTandem Mass SpectrometryAlgorithmsHumansReproducibility of ResultsSoftware

Identifiers

PMID40524023
PMCPMC12240826

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.