Evidence map›Paper›PMID 21813416›Full record

ArticleMolecular & cellular proteomics : MCP2011

CONSeQuence: prediction of reference peptides for absolute quantitative proteomics using consensus machine learning approaches.

Claire E Eyers, Craig Lawless, David C Wedge, King Wai Lau, Simon J Gaskell, Simon J Hubbard

Abstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing 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

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3 · Its place in the literature

Who cites it

56 citing papers in PubMed.

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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

6 authors.

Claire E EyersMichael Barber Centre for Mass Spectrometry, The University of Manchester, Manchester, M1 7DN, UK.
Craig Lawless
David C Wedge
King Wai Lau
Simon J Gaskell
Simon J Hubbard

Funding

Biotechnology and Biological Sciences Research Council BB/C007735/1Biotechnology and Biological Sciences Research Council BB/F004605/1Biotechnology and Biological Sciences Research Council BB/G009058/1
6 · The paper itself

Abstract

Mass spectrometric based methods for absolute quantification of proteins, such as QconCAT, rely on internal standards of stable-isotope labeled reference peptides, or "Q-peptides," to act as surrogates. Key to the success of this and related methods for absolute protein quantification (such as AQUA) is selection of the Q-peptide. Here we describe a novel method, CONSeQuence (consensus predictor for Q-peptide sequence), based on four different machine learning approaches for Q-peptide selection. CONSeQuence demonstrates improved performance over existing methods for optimal Q-peptide selection in the absence of prior experimental information, as validated using two independent test sets derived from yeast. Furthermore, we examine the physicochemical parameters associated with good peptide surrogates, and demonstrate that in addition to charge and hydrophobicity, peptide secondary structure plays a significant role in determining peptide "detectability" in liquid chromatography-electrospray ionization experiments. We relate peptide properties to protein tertiary structure, demonstrating a counterintuitive preference for buried status for frequently detected peptides. Finally, we demonstrate the improved efficacy of the general approach by applying a predictor trained on yeast data to sets of proteotypic peptides from two additional species taken from an existing peptide identification repository.

Indexed as

Amino Acid SequenceArtificial IntelligenceCaenorhabditis elegans ProteinsComputer SimulationDrosophila ProteinsMass SpectrometryModels, MolecularNeural Networks, ComputerPeptidesProteomeProteomicsReference StandardsSaccharomyces cerevisiae ProteinsSupport Vector MachineCaenorhabditis elegans ProteinsDrosophila ProteinsPeptidesProteomeSaccharomyces cerevisiae Proteins

Identifiers

PMID21813416
PMCPMC3226394

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Registered trials

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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.