A sampling framework for incorporating quantitative mass spectrometry data in protein interaction analysis.

ABSTRACT:

Background

Comprehensive protein-protein interaction (PPI) maps are a powerful resource for uncovering the molecular basis of genetic interactions and providing mechanistic insights. Over the past decade, high-throughput experimental techniques have been developed to generate PPI maps at proteome scale, first using yeast two-hybrid approaches and more recently via affinity purification combined with mass spectrometry (AP-MS). Unfortunately, data from both protocols are prone to both high false positive and false negative rates. To address these issues, many methods have been developed to post-process raw PPI data. However, with few exceptions, these methods only analyze binary experimental data (in which each potential interaction tested is deemed either observed or unobserved), ne

SUBMITTER: Tucker G 

PROVIDER: S-EPMC3851523 | biostudies-literature | 2013 Oct

REPOSITORIES: biostudies-literature