Evidence map›Paper›PMID 24255132›Full record

ArticleMolecular & cellular proteomics : MCP2014

Statistical approach to protein quantification.

Sarah Gerster, Taejoon Kwon, Christina Ludwig, Mariette Matondo, Christine Vogel, Edward M Marcotte, Ruedi Aebersold, Peter Bühlmann

Open access · hybridAbstract readEvaluation Study
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.1field-weighted citation impact, top 14% of its field
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

15 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Article
  3. Peptidomics Methods Applied to the Study of Flower Development.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  4. Multi-Omics Methods Applied to Flower Development.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Quantifying Homologous Proteins and Proteoforms.Molecular & cellular proteomics : MCP · 2019
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. 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

8 authors at 3 institutions in 2 countries.

Sarah GersterSeminar for Statistics, Eidgenössische Technische Hochschule (ETH) Zurich, Rämistrasse 101, 8092 Zurich, Switzerland;
Taejoon Kwon
Christina Ludwig
Mariette Matondo
Christine Vogel
Edward M Marcotte
Ruedi Aebersold
Peter Bühlmann
ETH Zurich · CHThe University of Texas at Austin · USBoard of the Swiss Federal Institutes of Technology · CH

Funding

Next-Generation Proteomics: Massively Parallel Single-Molecule Protein IdentificaDP1GM106408 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI MARCOTTE, EDWARD M · 2012 to 2016
$3.8M
Proteomics of widespread, reversible protein assemblies in aging and aggregationR01GM076536 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI MARCOTTE, EDWARD M · 2006 to 2014
$2.9M
NIGMS NIH HHS DP1 GM106408NIGMS NIH HHS R01 GM076536
6 · The paper itself

Abstract

A major goal in proteomics is the comprehensive and accurate description of a proteome. This task includes not only the identification of proteins in a sample, but also the accurate quantification of their abundance. Although mass spectrometry typically provides information on peptide identity and abundance in a sample, it does not directly measure the concentration of the corresponding proteins. Specifically, most mass-spectrometry-based approaches (e.g. shotgun proteomics or selected reaction monitoring) allow one to quantify peptides using chromatographic peak intensities or spectral counting information. Ultimately, based on these measurements, one wants to infer the concentrations of the corresponding proteins. Inferring properties of the proteins based on experimental peptide evidence is often a complex problem because of the ambiguity of peptide assignments and different chemical properties of the peptides that affect the observed concentrations. We present SCAMPI, a novel generic and statistically sound framework for computing protein abundance scores based on quantified peptides. In contrast to most previous approaches, our model explicitly includes information from shared peptides to improve protein quantitation, especially in eukaryotes with many homologous sequences. The model accounts for uncertainty in the input data, leading to statistical prediction intervals for the protein scores. Furthermore, peptides with extreme abundances can be reassessed and classified as either regular data points or actual outliers. We used the proposed model with several datasets and compared its performance to that of other, previously used approaches for protein quantification in bottom-up mass spectrometry.

Indexed as

Data Interpretation, StatisticalCell Line, TumorComputational BiologyDatabases, ProteinHumansIsotope LabelingLeptospira interrogansLeukemia, Myeloid, AcuteMarkov ChainsProteinsProteomicsResearch DesignSoftwareProteins

Identifiers

PMID24255132
PMCPMC3916661
OpenAlexW2165925503

What OpenQuestion holds

Textmetadata
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.