Literature DB >> 26572953

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

Quentin Giai Gianetto1,2,3, Florence Combes1,2,3, Claire Ramus1,4,2,3, Christophe Bruley1,2,3, Yohann Couté1,2,3, Thomas Burger1,4,2,3.   

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).
© 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Keywords:  False discovery rate; Relative quantification experiments; Statistical significance

Mesh:

Substances:

Year:  2016        PMID: 26572953     DOI: 10.1002/pmic.201500189

Source DB:  PubMed          Journal:  Proteomics        ISSN: 1615-9853            Impact factor:   3.984


  12 in total

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Journal:  Sci Rep       Date:  2018-03-26       Impact factor: 4.379

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