Evidence map›Paper›PMID 36328188›Full record

ArticleMolecular & cellular proteomics : MCP2022

Reanalysis of ProteomicsDB Using an Accurate, Sensitive, and Scalable False Discovery Rate Estimation Approach for Protein Groups.

Matthew The, Patroklos Samaras, Bernhard Kuster, Mathias Wilhelm

Abstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. With or without a CaPlanta · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. AI-Assisted Processing Pipeline to Boost Protein Isoform Detection.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Matthew TheChair of Proteomics and Bioanalytics, Technical University of Munich (TUM), Freising, Germany. Electronic address: matthew.the@tum.de.
Patroklos SamarasChair of Proteomics and Bioanalytics, Technical University of Munich (TUM), Freising, Germany.
Bernhard KusterChair of Proteomics and Bioanalytics, Technical University of Munich (TUM), Freising, Germany; Bavarian Biomolecular Mass Spectrometry Center (BayBioMS), Technical University of Munich (TUM), Freising, Germany.
Mathias WilhelmChair of Proteomics and Bioanalytics, Technical University of Munich (TUM), Freising, Germany; Computational Mass Spectrometry, Technical University of Munich (TUM), Freising, Germany. Electronic address: mathias.wilhelm@tum.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Estimating false discovery rates (FDRs) of protein identification continues to be an important topic in mass spectrometry-based proteomics, particularly when analyzing very large datasets. One performant method for this purpose is the Picked Protein FDR approach which is based on a target-decoy competition strategy on the protein level that ensures that FDRs scale to large datasets. Here, we present an extension to this method that can also deal with protein groups, that is, proteins that share common peptides such as protein isoforms of the same gene. To obtain well-calibrated FDR estimates that preserve protein identification sensitivity, we introduce two novel ideas. First, the picked group target-decoy and second, the rescued subset grouping strategies. Using entrapment searches and simulated data for validation, we demonstrate that the new Picked Protein Group FDR method produces accurate protein group-level FDR estimates regardless of the size of the data set. The validation analysis also uncovered that applying the commonly used Occam's razor principle leads to anticonservative FDR estimates for large datasets. This is not the case for the Picked Protein Group FDR method. Reanalysis of deep proteomes of 29 human tissues showed that the new method identified up to 4% more protein groups than MaxQuant. Applying the method to the reanalysis of the entire human section of ProteomicsDB led to the identification of 18,000 protein groups at 1% protein group-level FDR. The analysis also showed that about 1250 genes were represented by ≥2 identified protein groups. To make the method accessible to the proteomics community, we provide a software tool including a graphical user interface that enables merging results from multiple MaxQuant searches into a single list of identified and quantified protein groups.

Indexed as

PeptidesTandem Mass SpectrometryAlgorithmsDatabases, ProteinHumansProteomeSoftwarePeptidesProteomelarge-scale proteomicspicked protein FDRprotein false discovery rate estimationprotein inferenceProteomicsDB

Identifiers

PMID36328188
PMCPMC9718969

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.