Access to unified datasets of protein and genetic interactions is critical for interrogation of gene/ protein function and analysis of global network properties. BioGRID is a freely accessible database of physical and genetic interactions available at

We develop a model for examining data that consists of pairwise measurements, for example, presence or absence of links between pairs of objects. Examples include protein interactions and gene regulatory networks, collections of author-recipient email, and social networks. Analyzing such data with probabilistic models requires special assumptions, since the usual independence or exchangeability assumptions no longer hold. We introduce a class of latent variable models for pairwise measurements: mixed membership stochastic blockmodels. Models in this class combine a global model of dense patches of connectivity (blockmodel) and a local model to instantiate nodespecific variability in the connections (mixed membership). We develop a general variational inference algorithm for fast approximate posterior inference. We demonstrate the advantages of mixed membership stochastic blockmodels with applications to social networks and protein interaction networks.

Abstract. The interpretation of large-scale protein network data depends on our ability to identify significant sub-structures in the data, a computationally intensive task. Here we adapt and extend efficient techniques for finding paths in graphs to the problem of identifying pathways in protein interaction networks. We present linear-time algorithms for finding paths in networks under several biologically-motivated constraints. We apply our methodology to search for protein pathways in the yeast protein-protein interaction network. We demonstrate that our algorithm is capable of reconstructing known signaling pathways and identifying functionally enriched paths in an unsupervised manner. The algorithm is very efficient, computing optimal paths of length 8 within minutes and paths of length 10 in less than two hours. 1

integrated biological knowledge resource for plant genomics

associations, integrated and transferred across organisms

Abstract not found

Defining protein complexes is critical to virtually all aspects of cell biology. Two recent affinity purification/mass spectrometry studies in Saccharomyces cerevisiae have vastly increased the available protein interaction data. The practical utility of such high throughput interaction sets, however, is substantially decreased by the presence of false positives. Here we created a novel probabilistic metric that takes advantage of the high density of these data, including both the presence and absence of individual associations, to provide a measure of the relative confidence of each potential protein-protein interaction. This analysis largely overcomes the noise inherent in high throughput immunoprecipitation experiments. For example, of the 12,122 binary interactions in the general repository of interaction data (BioGRID) derived from these two

Motivation: Identifying protein-protein interactions is critical for understanding cellular processes. Because protein domains represent binding modules and are responsible for the interactions between proteins, computational approaches have been proposed to predict protein interactions at the domain level. The fact that protein domains are likely evolutionarily conserved allows us to pool information from data across multiple organisms for the inference of domain-domain and protein-protein interaction probabilities. Results: We use a likelihood approach to estimating domain-domain interaction probabilities by integrating large-scale protein interaction data from three organisms, S. cerevisiae, C. elegans, and D. melanogaster. The estimated domain-domain interaction probabilities are then used to predict protein-protein interactions in S. cerevisiae. Based on a thorough comparison of sensitivity and specificity, Gene Ontology term enrichment and gene expression profiles, we have demonstrated that it may be far more informative to predict protein-protein interactions from diverse organisms than that based on a single organism. Availability: The program for computing the protein-protein interaction probabilities and supplementary material are available at

for cytoplasmic membrane transport systems and outer membrane channels

Summary: Metabolomics, in particular gas chromatography–mass spectrometry (GC–MS) based metabolite profiling of biological extracts, is rapidly becoming one of the cornerstones of functional genomics and systems biology. Metabolite profiling has profound applications in discovering the mode of action of drugs or herbicides, and in unravelling the effect of altered gene expression on metabolism and organism performance in biotechnological applications. As such the technology needs to be available to many laboratories. For this, an open exchange of information is required, like that already achieved for transcript and protein data. One of the key-steps in metabolite profiling is the unambiguous identification of metabolites in highly complex metabolite preparations from biological samples. Collections of mass spectra, which comprise frequently observed metabolites of either known or unknown exact chemical structure, represent the most