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Calibration plot for proteomics: A graphical tool to visually check the assumptions underlying FDR control in quantitative experiments

Authors :
Yohann Couté
Christophe Bruley
Thomas Burger
Florence Combes
Quentin Giai Gianetto
Claire Ramus
Source :
PROTEOMICS. 16:29-32
Publication Year :
2016
Publisher :
Wiley, 2016.

Abstract

In MS-based quantitative proteomics, the FDR control (i.e. the limitation of the number of proteins that are wrongly claimed as differentially abundant between several conditions) is a major postanalysis step. It is classically achieved thanks to a specific statistical procedure that computes the adjusted p-values of the putative differentially abundant proteins. Unfortunately, such adjustment is conservative only if the p-values are well-calibrated; the false discovery control being spuriously underestimated otherwise. However, well-calibration is a property that can be violated in some practical cases. To overcome this limitation, we propose a graphical method to straightforwardly and visually assess the p-value well-calibration, as well as the R codes to embed it in any pipeline. All MS data have been deposited in the ProteomeXchange with identifier PXD002370 (http://proteomecentral.proteomexchange.org/dataset/PXD002370).

Details

ISSN :
16159853
Volume :
16
Database :
OpenAIRE
Journal :
PROTEOMICS
Accession number :
edsair.doi...........87f294a4f1e8f1881fe2f8c718bc4f89