Please use this identifier to cite or link to this item:
|Title:||D-SLIMMER: Domain-SLiM interaction motifs miner for sequence based protein-protein interaction data|
|Authors:||Hugo, W. |
short linear motif
|Citation:||Hugo, W., Ng, S.-K., Sung, W.-K. (2011). D-SLIMMER: Domain-SLiM interaction motifs miner for sequence based protein-protein interaction data. Journal of Proteome Research 10 (12) : 5285-5295. ScholarBank@NUS Repository. https://doi.org/10.1021/pr200312e|
|Abstract:||Many biologically important protein-protein interactions (PPIs) have been found to be mediated by short linear motifs (SLiMs). These interactions are mediated by the binding of a protein domain, often with a nonlinear interaction interface, to a SLiM. We propose a method called D-SLIMMER to mine for SLiMs in PPI data on the basis of the interaction density between a nonlinear motif (i.e., a protein domain) in one protein and a SLiM in the other protein. Our results on a benchmark of 113 experimentally verified reference SLiMs showed that D-SLIMMER outperformed existing methods notably for discovering domain-SLiMs interaction motifs. To illustrate the significance of the SLiMs detected, we highlighted two SLiMs discovered from the PPI data by D-SLIMMER that are variants of the known ELM SLiM, as well as a literature-backed SLiM that is yet to be listed in the reference databases. We also presented a novel SLiM predicted by D-SLIMMER that was strongly supported by existing biological literatures. These examples showed that D-SLIMMER is able to find SLiMs that are biologically relevant. © 2011 American Chemical Society.|
|Source Title:||Journal of Proteome Research|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Dec 6, 2018
WEB OF SCIENCETM
checked on Nov 27, 2018
checked on Dec 8, 2018
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.