Evidence map›Paper›PMID 31235637›Full record

ArticleMolecular & cellular proteomics : MCP2019

MS-EmpiRe Utilizes Peptide-level Noise Distributions for Ultra-sensitive Detection of Differentially Expressed Proteins.

Constantin Ammar, Markus Gruber, Gergely Csaba, Ralf Zimmer

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

28 citing papers in PubMed, 50 citations in OpenAlex.

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  9. Metabolic control of glycosylation forms for establishing glycan-dependent protein interaction networks.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  15. Single-nucleus proteomics identifies regulators of protein transport.bioRxiv : the preprint server for biology · 2024
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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 at 1 institution in 1 country.

Constantin Ammar‡Ludwig-Maximilians-Universität München, Department of Informatics, Amalienstrasse 17, 80333 München, Germany; §Graduate School of Quantitative Biosciences (QBM), Ludwig-Maximillians-Universität München, Feodor-Lynen-Strasse 25, 81377 Munich, Germany.
Markus Gruber‡Ludwig-Maximilians-Universität München, Department of Informatics, Amalienstrasse 17, 80333 München, Germany.
Gergely Csaba‡Ludwig-Maximilians-Universität München, Department of Informatics, Amalienstrasse 17, 80333 München, Germany.
Ralf Zimmer‡Ludwig-Maximilians-Universität München, Department of Informatics, Amalienstrasse 17, 80333 München, Germany; §Graduate School of Quantitative Biosciences (QBM), Ludwig-Maximillians-Universität München, Feodor-Lynen-Strasse 25, 81377 Munich, Germany. Electronic address: zimmer@ifi.lmu.de.
Ludwig-Maximilians-Universität München · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mass spectrometry based proteomics is the method of choice for quantifying genome-wide differential changes of protein expression in a wide range of biological and biomedical applications. Protein expression changes need to be reliably derived from many measured peptide intensities and their corresponding peptide fold changes. These peptide fold changes vary considerably for a given protein. Numerous instrumental setups aim to reduce this variability, whereas current computational methods only implicitly account for this problem. We introduce a new method, MS-EmpiRe, which explicitly accounts for the noise underlying peptide fold changes. We derive data set-specific, intensity-dependent empirical error fold change distributions, which are used for individual weighing of peptide fold changes to detect differentially expressed proteins (DEPs).In a recently published proteome-wide benchmarking data set, MS-EmpiRe doubles the number of correctly identified DEPs at an estimated FDR cutoff compared with state-of-the-art tools. We additionally confirm the superior performance of MS-EmpiRe on simulated data. MS-EmpiRe requires only peptide intensities mapped to proteins and, thus, can be applied to any common quantitative proteomics setup. We apply our method to diverse MS data sets and observe consistent increases in sensitivity with more than 1000 additional significant proteins in deep data sets, including a clinical study over multiple patients. At the same time, we observe that even the proteins classified as most insignificant by other methods but significant by MS-EmpiRe show very clear regulation on the peptide intensity level. MS-EmpiRe provides rapid processing (< 2 min for 6 LC-MS/MS runs (3 h gradients)) and is publicly available under github.com/zimmerlab/MS-EmpiRe with a manual including examples.

Indexed as

SoftwareAlzheimer DiseaseBenchmarkingDatabases, FactualFrancisellaFungal ProteinsHeLa CellsHumansMass SpectrometryParkinson DiseasePeptidesPlant ProteinsProteomeProteomicsReproducibility of ResultsSignal-To-Noise RatioFungal ProteinsPeptidesPlant ProteinsProteomebioinformaticsbioinformatics softwaredifferential expressiondifferential quantificationlabel-free quantificationmass spectrometryQuantificationstatisticsTMT

Identifiers

PMID31235637
PMCPMC6731086
OpenAlexW2955735026

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.