ArticleBMC systems biology2017
A two-step framework for inferring direct protein-protein interaction network from AP-MS data.
Article in BMC systems biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Article
- CoVMBiomolecules · 2022Article
- Computational analyses of mechanism of action (MoA): data, methods and integration.RSC chemical biology · 2022Review
- Inferring Protein-Protein Interaction Networks From Mass Spectrometry-Based Proteomic Approaches: A Mini-Review.Computational and structural biotechnology journal · 2019Review
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Authors and funding
4 authors.
Funding
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Abstract
backgroundAffinity purification-mass spectrometry (AP-MS) has been widely used for generating bait-prey data sets so as to identify underlying protein-protein interactions and protein complexes. However, the AP-MS data sets in terms of bait-prey pairs are highly noisy, where candidate pairs contain many false positives. Recently, numerous computational methods have been developed to identify genuine interactions from AP-MS data sets. However, most of these methods aim at removing false positives that contain contaminants, ignoring the distinction between direct interactions and indirect interactions.
resultsIn this paper, we present an initialization-and-refinement framework for inferring direct PPI networks from AP-MS data, in which an initial network is first generated with existing scoring methods and then a refined network is constructed by the application of indirect association removal methods. Experimental results on several real AP-MS data sets show that our method is capable of identifying more direct interactions than traditional scoring methods.
conclusionsThe proposed framework is sufficiently general to incorporate any feasible methods in each step so as to have potential for handling different types of AP-MS data in the future applications.
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