Evidence map›Paper›PMID 26100116›Full record

ArticleMolecular & cellular proteomics : MCP2015

Using Data Independent Acquisition (DIA) to Model High-responding Peptides for Targeted Proteomics Experiments.

Brian C Searle, Jarrett D Egertson, James G Bollinger, Andrew B Stergachis, Michael J MacCoss

Abstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing 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

36 citing papers in PubMed.

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  13. Mass spectrometry-based phosphoproteomics in clinical applications.Trends in analytical chemistry : TRAC · 2023
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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

5 authors.

Brian C SearleFrom the ‡Department of Genome Sciences, University of Washington, Seattle, Washington 98195; §Proteome Software Inc., Portland, OR 97219.
Jarrett D EgertsonFrom the ‡Department of Genome Sciences, University of Washington, Seattle, Washington 98195;
James G BollingerFrom the ‡Department of Genome Sciences, University of Washington, Seattle, Washington 98195;
Andrew B StergachisFrom the ‡Department of Genome Sciences, University of Washington, Seattle, Washington 98195;
Michael J MacCossFrom the ‡Department of Genome Sciences, University of Washington, Seattle, Washington 98195; maccoss@uw.edu.

Funding

TrainingP41GM103533 · NIGMS · UNIVERSITY OF WASHINGTON · PI MACCOSS, MICHAEL · 2012 to 2021
$20.7M
Self Correcting Nanoflow LC-MS for Clinical ProteomicsR01GM107142 · NIGMS · UNIVERSITY OF WASHINGTON · PI MACCOSS, MICHAEL · 2013 to 2016
$1.5M
NIGMS NIH HHS P41 GM103533NIGMS NIH HHS R01 GM107142
6 · The paper itself

Abstract

Targeted mass spectrometry is an essential tool for detecting quantitative changes in low abundant proteins throughout the proteome. Although selected reaction monitoring (SRM) is the preferred method for quantifying peptides in complex samples, the process of designing SRM assays is laborious. Peptides have widely varying signal responses dictated by sequence-specific physiochemical properties; one major challenge is in selecting representative peptides to target as a proxy for protein abundance. Here we present PREGO, a software tool that predicts high-responding peptides for SRM experiments. PREGO predicts peptide responses with an artificial neural network trained using 11 minimally redundant, maximally relevant properties. Crucial to its success, PREGO is trained using fragment ion intensities of equimolar synthetic peptides extracted from data independent acquisition experiments. Because of similarities in instrumentation and the nature of data collection, relative peptide responses from data independent acquisition experiments are a suitable substitute for SRM experiments because they both make quantitative measurements from integrated fragment ion chromatograms. Using an SRM experiment containing 12,973 peptides from 724 synthetic proteins, PREGO exhibits a 40-85% improvement over previously published approaches at selecting high-responding peptides. These results also represent a dramatic improvement over the rules-based peptide selection approaches commonly used in the literature.

Indexed as

AlgorithmsHumansMass SpectrometryNeural Networks, ComputerPeptidesProteomicsSoftwarePeptides

Identifiers

PMID26100116
PMCPMC4563719

What OpenQuestion holds

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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.