Please use this identifier to cite or link to this item: https://doi.org/10.1186/1471-2164-11-S1-S3
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dc.titleComputational approaches for detecting protein complexes from protein interaction networks: A survey
dc.contributor.authorLi, X
dc.contributor.authorWu, M
dc.contributor.authorKwoh, C
dc.contributor.authorNg, S
dc.date.accessioned2020-10-27T11:40:44Z
dc.date.available2020-10-27T11:40:44Z
dc.date.issued2010
dc.identifier.citationLi, X, Wu, M, Kwoh, C, Ng, S (2010). Computational approaches for detecting protein complexes from protein interaction networks: A survey. BMC Genomics 11 (SUPPL. 1) : S3. ScholarBank@NUS Repository. https://doi.org/10.1186/1471-2164-11-S1-S3
dc.identifier.issn14712164
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/181678
dc.description.abstractBackground: Most proteins form macromolecular complexes to perform their biological functions. However, experimentally determined protein complex data, especially of those involving more than two protein partners, are relatively limited in the current state-of-the-art high-throughput experimental techniques. Nevertheless, many techniques (such as yeast-two-hybrid) have enabled systematic screening of pairwise protein-protein interactions en masse. Thus computational approaches for detecting protein complexes from protein interaction data are useful complements to the limited experimental methods. They can be used together with the experimental methods for mapping the interactions of proteins to understand how different proteins are organized into higher-level substructures to perform various cellular functions.Results: Given the abundance of pairwise protein interaction data from high-throughput genome-wide experimental screenings, a protein interaction network can be constructed from protein interaction data by considering individual proteins as the nodes, and the existence of a physical interaction between a pair of proteins as a link. This binary protein interaction graph can then be used for detecting protein complexes using graph clustering techniques. In this paper, we review and evaluate the state-of-the-art techniques for computational detection of protein complexes, and discuss some promising research directions in this field.Conclusions: Experimental results with yeast protein interaction data show that the interaction subgraphs discovered by various computational methods matched well with actual protein complexes. In addition, the computational approaches have also improved in performance over the years. Further improvements could be achieved if the quality of the underlying protein interaction data can be considered adequately to minimize the undesirable effects from the irrelevant and noisy sources, and the various biological evidences can be better incorporated into the detection process to maximize the exploitation of the increasing wealth of biological knowledge available. © 2010 Li et al; licensee BioMed Central Ltd.
dc.rightsAttribution 4.0 International
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.sourceUnpaywall 20201031
dc.subjectaccuracy
dc.subjectarticle
dc.subjectBayesian learning
dc.subjectcluster analysis
dc.subjectdata analysis software
dc.subjectdata mining
dc.subjectdensity
dc.subjectfuzzy system
dc.subjectgene expression
dc.subjectgenome
dc.subjecthidden Markov model
dc.subjecthigh throughput screening
dc.subjectinformation processing
dc.subjectmathematical analysis
dc.subjectnonhuman
dc.subjectprediction
dc.subjectprobability
dc.subjectprotein function
dc.subjectprotein protein interaction
dc.subjectquality control
dc.subjectrecall
dc.subjectreliability
dc.subjectsensitivity and specificity
dc.subjectsimulation
dc.subjectstatistical significance
dc.subjectbiometry
dc.subjectgene expression profiling
dc.subjecthuman
dc.subjectmetabolism
dc.subjectmethodology
dc.subjectprotein analysis
dc.subjectprotein binding
dc.subjectsystems biology
dc.subjectprotein
dc.subjectBiometry
dc.subjectGene Expression Profiling
dc.subjectHumans
dc.subjectProtein Binding
dc.subjectProtein Interaction Mapping
dc.subjectProteins
dc.subjectSystems Biology
dc.typeArticle
dc.contributor.departmentDEPARTMENT OF COMPUTER SCIENCE
dc.description.doi10.1186/1471-2164-11-S1-S3
dc.description.sourcetitleBMC Genomics
dc.description.volume11
dc.description.issueSUPPL. 1
dc.description.pageS3
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