Quasi-bicliques: Complexity and Binding Pairs
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Domain-Domain Interaction Identification with a Feature Selection Approach
PRIB '08 Proceedings of the Third IAPR International Conference on Pattern Recognition in Bioinformatics
Brief communication: Operon prediction based on SVM
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Predicting protein-protein interactions using first principle methods and statistical scoring
ISB '10 Proceedings of the International Symposium on Biocomputing
Reconstructing the topology of protein complexes
RECOMB'07 Proceedings of the 11th annual international conference on Research in computational molecular biology
Interactive analysis and visualization of macromolecular interfaces between proteins
USAB'07 Proceedings of the 3rd Human-computer interaction and usability engineering of the Austrian computer society conference on HCI and usability for medicine and health care
Modeling Protein Interacting Groups by Quasi-Bicliques: Complexity, Algorithm, and Application
IEEE/ACM Transactions on Computational Biology and Bioinformatics (TCBB)
Transactions on computational systems biology VIII
Belief propagation estimation of protein and domain interactions using the sum-product algorithm
IEEE Transactions on Information Theory - Special issue on information theory in molecular biology and neuroscience
Near optimal solutions for maximum quasi-bicliques
COCOON'10 Proceedings of the 16th annual international conference on Computing and combinatorics
Modeling of multi domain contribution to protein interaction
Proceedings of the 2nd ACM Conference on Bioinformatics, Computational Biology and Biomedicine
A Computational Model for Predicting Protein Interactions Based on Multidomain Collaboration
IEEE/ACM Transactions on Computational Biology and Bioinformatics (TCBB)
International Journal of Bioinformatics Research and Applications
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Summary: There are many resources that contain information about binary interactions between proteins. However, protein interactions are defined by only a subset of residues in any protein. We have implemented a web resource that allows the investigation of protein interactions in the Protein Data Bank structures at the level of Pfam domains and amino acid residues. This detailed knowledge relies on the fact that there are a large number of multidomain proteins and protein complexes being deposited in the structure databases. The resource called iPfam is hosted within the Pfam UK website. Most resources focus on the interactions between proteins; iPfam includes these as well as interactions between domains in a single protein. Availability:iPfam is available on the Web for browsing at http://www.sanger.ac.uk/Software/Pfam/iPfam/; the source-data for iPfam is freely available in relational tables via the ftp site ftp://ftp.sanger.ac.uk/pub/databases/Pfam/database_files/ Contact: rdf@sanger.ac.uk