Molecular function is the result of proteins working together, mediated by highly specific interactions. Maintenance and change of protein interactions can thus be considered one of the main links between molecular function and mutation. As a consequence, protein interaction datasets can be used to study functional evolution directly. In terms of constraining change, the co-evolution of interacting molecules is a very subtle process. This has implications for the signal being used to predict protein–protein interactions. In terms of functional change, the ‘rewiring’ of interaction networks, gene duplication is critically important. Interestingly, once duplication has occurred, the genes involved have different probabilities of being retained related to how they were generated. In the present paper, we discuss some of our recent work in this area.
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August 2009
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Conference Article|
July 22 2009
Evolution in protein interaction networks: co-evolution, rewiring and the role of duplication
David L. Robertson;
David L. Robertson
1
1Faculty of Life Sciences, University of Manchester, Oxford Road, Manchester M13 9PT, U.K.
1To whom correspondence should be addressed (email david.robertson@manchester.ac.uk).
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Simon C. Lovell
Simon C. Lovell
1Faculty of Life Sciences, University of Manchester, Oxford Road, Manchester M13 9PT, U.K.
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Publisher: Portland Press Ltd
Received:
May 12 2009
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2009 Biochemical Society
2009
Biochem Soc Trans (2009) 37 (4): 768–771.
Article history
Received:
May 12 2009
Citation
David L. Robertson, Simon C. Lovell; Evolution in protein interaction networks: co-evolution, rewiring and the role of duplication. Biochem Soc Trans 1 August 2009; 37 (4): 768–771. doi: https://doi.org/10.1042/BST0370768
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