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Braun, P.

Interactome mapping for analysis of complex phenotypes: Insights from benchmarking binary interaction assays.

Proteomics 12, 1499-1518 (2012)
DOI PMC
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
Protein interactions mediate essentially all biological processes and analysis of proteinprotein interactions using both large-scale and small-scale approaches has contributed fundamental insights to the understanding of biological systems. In recent years, interactome network maps have emerged as an important tool for analyzing and interpreting genetic data of complex phenotypes. Complementary experimental approaches to test for binary, direct interactions, and for membership in protein complexes are used to explore the interactome. The two approaches are not redundant but yield orthogonal perspectives onto the complex network of physical interactions by which proteins mediate biological processes. In recent years, several publications have demonstrated that interactions from high-throughput experiments can be equally reliable as the high quality subset of interactions identified in small-scale studies. Critical for this insight was the introduction of standardized experimental benchmarking of interaction and validation assays using reference sets. The data obtained in these benchmarking experiments have resulted in greater appreciation of the limitations and the complementary strengths of different assays. Moreover, benchmarking is a central element of a conceptual framework to estimate interactome sizes and thereby measure progress toward near complete network maps. These estimates have revealed that current large-scale data sets, although often of high quality, cover only a small fraction of a given interactome. Here, I review the findings of assay benchmarking and discuss implications for quality control, and for strategies toward obtaining a near-complete map of the interactome of an organism.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Review
Schlagwörter Protein-protein Interactions; Genome-wide Association; Bimolecular Fluorescence Complementation; Molecular Interaction Database; Domain-domain Interactions; Yeast 2-hybrid System; Signal-to-noise; Interaction Network; Human-disease; C-elegans; Biomolecular Interaction Analysis; Interaction Networks; Interactome; Protein-protein Interaction; Quality Control; Systems Biology
Sprache
Veröffentlichungsjahr 2012
HGF-Berichtsjahr 2012
ISSN (print) / ISBN 1615-9853
e-ISSN 1615-9861
Zeitschrift Proteomics
Quellenangaben Band: 12, Heft: 10, Seiten: 1499-1518 Artikelnummer: , Supplement: ,
Verlag Wiley
Begutachtungsstatus Peer reviewed
Institut(e) CF Metabolomics & Proteomics (CF-MPC)
POF Topic(s) 30203 - Molecular Targets and Therapies
Forschungsfeld(er) Enabling and Novel Technologies
PSP-Element(e) G-505700-001
PubMed ID 22589225
DOI 10.1002/pmic.201100598
WOS ID WOS:000305474400003
Scopus ID 84862703457
Erfassungsdatum 2012-07-12
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