| Literature DB >> 26572953 |
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).Keywords: False discovery rate; Relative quantification experiments; Statistical significance
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Year: 2016 PMID: 26572953 DOI: 10.1002/pmic.201500189
Source DB: PubMed Journal: Proteomics ISSN: 1615-9853 Impact factor: 3.984