Journal
FEBS LETTERS
Volume 586, Issue 17, Pages 2723-2731Publisher
WILEY
DOI: 10.1016/j.febslet.2012.03.065
Keywords
Interaction networks; Affinity purification coupled to mass spectrometry; Protein-protein interactions; Quantitative proteomics; Regulated interactions
Funding
- CIHR [MOP-84314, MOP-81268, MOP-119289]
- NIH [R01RR024031]
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The past 10 years have witnessed a dramatic proliferation in the availability of protein interaction data. However, for interaction mapping based on affinity purification coupled with mass spectrometry (AP-MS), there is a wealth of information present in the datasets that often goes unrecorded in public repositories, and as such remains largely unexplored. Further, how this type of data is represented and used by bioinformaticians has not been well established. Here, we point out some common mistakes in how AP-MS data are handled, and describe how protein complex organization and interaction dynamics can be inferred using quantitative AP-MS approaches. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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