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Quantitative proteomics: A strategic ally to map protein interaction networks.
MedLine Citation:
PMID:  23281033     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
Many physiological processes are regulated by dynamic protein interaction networks whose characterization provides valuable information on cell biology. Several strategies can be used to analyze protein-protein interactions. Among them, affinity purification combined with mass spectrometry (AP-MS) is arguably the most widely employed technique, not only owing to its high throughput and sensitivity but also because it can answer critical questions such as where, when, and how protein-protein interactions occur. In AP-MS workflows, both the target protein and its interacting partners are isolated before being identified by MS. The main challenge of this approach is to distinguish bona fide binders from background contaminants. This review focuses on the different strategies designed to circumvent this limitation. In this regard, the combination of quantitative proteomics and affinity purification emerges as one of the most powerful, yet relatively simple, strategies to characterize protein-protein interactions. © IUBMB Life, 65(1):9-16, 2013.
Authors:
Miguel Marcilla; Juan Pablo Albar
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  IUBMB life     Volume:  65     ISSN:  1521-6551     ISO Abbreviation:  IUBMB Life     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-01-02     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  100888706     Medline TA:  IUBMB Life     Country:  England    
Other Details:
Languages:  eng     Pagination:  9-16     Citation Subset:  IM    
Copyright Information:
Copyright © 2012 International Union of Biochemistry and Molecular Biology, Inc.
Affiliation:
Proteomics Unit, Centro Nacional de Biotecnología, CSIC, Madrid, Spain. mmarcilla@cnb.csic.es.
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