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Protein complex analysis: From raw protein lists to protein interaction networks.
- Source :
-
Mass Spectrometry Reviews . Sep/Oct2017, Vol. 36 Issue 5, p600-614. 15p. - Publication Year :
- 2017
-
Abstract
- The elucidation of molecular interaction networks is one of the pivotal challenges in the study of biology. Affinity purification-mass spectrometry and other co-complex methods have become widely employed experimental techniques to identify protein complexes. These techniques typically suffer from a high number of false negatives and false positive contaminants due to technical shortcomings and purification biases. To support a diverse range of experimental designs and approaches, a large number of computational methods have been proposed to filter, infer and validate protein interaction networks from experimental pull-down MS data. Nevertheless, this expansion of available methods complicates the selection of the most optimal ones to support systems biology-driven knowledge extraction. In this review, we give an overview of the most commonly used computational methods to process and interpret co-complex results, and we discuss the issues and unsolved problems that still exist within the field. © 2015 Wiley Periodicals, Inc. Mass Spec Rev 36:600-614, 2017 [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 02777037
- Volume :
- 36
- Issue :
- 5
- Database :
- Academic Search Index
- Journal :
- Mass Spectrometry Reviews
- Publication Type :
- Academic Journal
- Accession number :
- 124720307
- Full Text :
- https://doi.org/10.1002/mas.21485