Literature DB >> 22710165

Beyond hairballs: The use of quantitative mass spectrometry data to understand protein-protein interactions.

Anne-Claude Gingras1, Brian Raught.   

Abstract

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.
Copyright © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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Year:  2012        PMID: 22710165      PMCID: PMC3669394          DOI: 10.1016/j.febslet.2012.03.065

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  117 in total

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  18 in total

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5.  Affinity purification-mass spectrometry and network analysis to understand protein-protein interactions.

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Review 7.  Edgotype: a fundamental link between genotype and phenotype.

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8.  The Impact of Mass Spectrometry-Based Proteomics on Fundamental Discoveries in Virology.

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Review 9.  Cross-linking and mass spectrometry methodologies to facilitate structural biology: finding a path through the maze.

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