Large-scale mapping of human protein interactome using structural complexes

Although the identification of protein interactions by high‐throughput (HTP) methods progresses at a fast pace, ‘interactome’ data sets still suffer from high rates of false positives and low coverage. To map the human protein interactome, we describe a new framework that uses experimental evidence...

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Bibliographic Details
Published inEMBO reports Vol. 13; no. 3; pp. 266 - 271
Main Authors Tyagi, Manoj, Hashimoto, Kosuke, Shoemaker, Benjamin A, Wuchty, Stefan, Panchenko, Anna R
Format Journal Article
LanguageEnglish
Published Chichester, UK John Wiley & Sons, Ltd 01.03.2012
Nature Publishing Group UK
Springer Nature B.V
Nature Publishing Group
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ISSN1469-221X
1469-3178
1469-3178
DOI10.1038/embor.2011.261

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Summary:Although the identification of protein interactions by high‐throughput (HTP) methods progresses at a fast pace, ‘interactome’ data sets still suffer from high rates of false positives and low coverage. To map the human protein interactome, we describe a new framework that uses experimental evidence on structural complexes, the atomic details of binding interfaces and evolutionary conservation. The structurally inferred interaction network is highly modular and more functionally coherent compared with experimental interaction networks derived from multiple literature citations. Moreover, structurally inferred and high‐confidence HTP networks complement each other well, allowing us to construct a merged network to generate testable hypotheses and provide valuable experimental leads. This study describes a new framework that utilizes experimental evidence on structural complexes, the atomic details of binding interfaces and evolutionary conservation to map the human protein interactome.
Bibliography:istex:A9625C4F1385C12A123FA1230DCDC45593CA0DCA
ark:/67375/WNG-0DF0NR6S-H
ArticleID:EMBR2011261
Supplementary Information
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These authors contributed equally to this work
ISSN:1469-221X
1469-3178
1469-3178
DOI:10.1038/embor.2011.261