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Protein complex analysis: From raw protein lists to protein interaction networks.
- Source :
-
Mass spectrometry reviews [Mass Spectrom Rev] 2017 Sep; Vol. 36 (5), pp. 600-614. Date of Electronic Publication: 2015 Dec 28. - 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.<br /> (© 2015 Wiley Periodicals, Inc.)
- Subjects :
- Cluster Analysis
Databases, Protein
Multiprotein Complexes analysis
Multiprotein Complexes chemistry
Multiprotein Complexes metabolism
Protein Interaction Mapping standards
Proteins chemistry
Proteins metabolism
Quality Control
Reproducibility of Results
Workflow
Computational Biology methods
Protein Interaction Mapping methods
Protein Interaction Maps
Proteins analysis
Subjects
Details
- Language :
- English
- ISSN :
- 1098-2787
- Volume :
- 36
- Issue :
- 5
- Database :
- MEDLINE
- Journal :
- Mass spectrometry reviews
- Publication Type :
- Academic Journal
- Accession number :
- 26709718
- Full Text :
- https://doi.org/10.1002/mas.21485