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Spiked proteomic standard dataset for testing label-free quantitative software and statistical methods

Authors :
Claire Ramus
Agnès Hovasse
Marlène Marcellin
Anne-Marie Hesse
Emmanuelle Mouton-Barbosa
David Bouyssié
Sebastian Vaca
Christine Carapito
Karima Chaoui
Christophe Bruley
Jérôme Garin
Sarah Cianférani
Myriam Ferro
Alain Van Dorssaeler
Odile Burlet-Schiltz
Christine Schaeffer
Yohann Couté
Anne Gonzalez de Peredo
Source :
Data in Brief, Vol 6, Iss , Pp 286-294 (2016)
Publication Year :
2016
Publisher :
Elsevier, 2016.

Abstract

This data article describes a controlled, spiked proteomic dataset for which the “ground truth” of variant proteins is known. It is based on the LC-MS analysis of samples composed of a fixed background of yeast lysate and different spiked amounts of the UPS1 mixture of 48 recombinant proteins. It can be used to objectively evaluate bioinformatic pipelines for label-free quantitative analysis, and their ability to detect variant proteins with good sensitivity and low false discovery rate in large-scale proteomic studies. More specifically, it can be useful for tuning software tools parameters, but also testing new algorithms for label-free quantitative analysis, or for evaluation of downstream statistical methods. The raw MS files can be downloaded from ProteomeXchange with identifier http://www.ebi.ac.uk/pride/archive/projects/PXD001819. Starting from some raw files of this dataset, we also provide here some processed data obtained through various bioinformatics tools (including MaxQuant, Skyline, MFPaQ, IRMa-hEIDI and Scaffold) in different workflows, to exemplify the use of such data in the context of software benchmarking, as discussed in details in the accompanying manuscript [1]. The experimental design used here for data processing takes advantage of the different spike levels introduced in the samples composing the dataset, and processed data are merged in a single file to facilitate the evaluation and illustration of software tools results for the detection of variant proteins with different absolute expression levels and fold change values.

Details

Language :
English
ISSN :
23523409
Volume :
6
Issue :
286-294
Database :
Directory of Open Access Journals
Journal :
Data in Brief
Publication Type :
Academic Journal
Accession number :
edsdoj.8b96cae40576401e99a13ced9dac4f1b
Document Type :
article
Full Text :
https://doi.org/10.1016/j.dib.2015.11.063