Constructing More Reliable Protein- Protein Interaction Maps

Progress in high-throughput experimental techniques in the past decade has resulted in a rapid accumulation of protein-protein interaction data [27, 17, 28]. High-quality protein-protein interaction maps are useful for a deeper understanding of how proteins may together to carry out specific functions. However, high-throughput methods are known to yield a non-negligible rate of false positives, and to miss a fraction of existing interactions [28, 26, 10]. As a result, further carefully-focused small-scale experiments are often needed to complement the large-scale methods to validate the detected interactions. Therefore computational analysis techniques for assessing and ranking the reliability of a protein-protein interaction are highly desirable.