Reference: Krause R, et al. (2003) A comprehensive set of protein complexes in yeast: mining large scale protein-protein interaction screens. Bioinformatics 19(15):1901-8

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Abstract


Motivation: The analysis of protein-protein interactions allows for detailed exploration of the cellular machinery. The biochemical purification of protein complexes followed by identification of components by mass spectrometry is currently the method, which delivers the most reliable information--albeit that the data sets are still difficult to interpret. Consolidating individual experiments into protein complexes, especially for high-throughput screens, is complicated by many contaminants, the occurrence of proteins in otherwise dissimilar purifications due to functional re-use and technical limitations in the detection. A non-redundant collection of protein complexes from experimental data would be useful for biological interpretation, but manual assembly is tedious and often inconsistent.

Results: Here, we introduce a measure to define similarity within collections of purifications and generate a set of minimally redundant, comprehensive complexes using unsupervised clustering.

Availability: Programs and results are freely available from http://www.bork.embl-heidelberg.de/Docu/purclust/

Reference Type
Comparative Study | Evaluation Study | Journal Article | Validation Study
Authors
Krause R, von Mering C, Bork P
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Gene Ontology Annotations


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Gene/Complex Qualifier Gene Ontology Term Aspect Annotation Extension Evidence Method Source Assigned On Reference

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Gene Disease Ontology Term Qualifier Evidence Method Source Assigned On Reference

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Interactor Interactor Allele Assay Annotation Action Phenotype SGA score P-value Source Reference

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Gene Species Gene ID Strain background Direction Details Source Reference