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Prediction of protein-protein interaction types using association rule based classification
BACKGROUND: Protein-protein interactions (PPI) can be classified according to their characteristics into, for example obligate or transient interactions. The identification and characterization of these PPI types may help in the functional annotation of new protein complexes and in the prediction of...
Autores principales: | , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2009
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2667511/ https://www.ncbi.nlm.nih.gov/pubmed/19173748 http://dx.doi.org/10.1186/1471-2105-10-36 |
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author | Park, Sung Hee Reyes, José A Gilbert, David R Kim, Ji Woong Kim, Sangsoo |
author_facet | Park, Sung Hee Reyes, José A Gilbert, David R Kim, Ji Woong Kim, Sangsoo |
author_sort | Park, Sung Hee |
collection | PubMed |
description | BACKGROUND: Protein-protein interactions (PPI) can be classified according to their characteristics into, for example obligate or transient interactions. The identification and characterization of these PPI types may help in the functional annotation of new protein complexes and in the prediction of protein interaction partners by knowledge driven approaches. RESULTS: This work addresses pattern discovery of the interaction sites for four different interaction types to characterize and uses them for the prediction of PPI types employing Association Rule Based Classification (ARBC) which includes association rule generation and posterior classification. We incorporated domain information from protein complexes in SCOP proteins and identified 354 domain-interaction sites. 14 interface properties were calculated from amino acid and secondary structure composition and then used to generate a set of association rules characterizing these domain-interaction sites employing the APRIORI algorithm. Our results regarding the classification of PPI types based on a set of discovered association rules shows that the discriminative ability of association rules can significantly impact on the prediction power of classification models. We also showed that the accuracy of the classification can be improved through the use of structural domain information and also the use of secondary structure content. CONCLUSION: The advantage of our approach is that we can extract biologically significant information from the interpretation of the discovered association rules in terms of understandability and interpretability of rules. A web application based on our method can be found at |
format | Text |
id | pubmed-2667511 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-26675112009-04-10 Prediction of protein-protein interaction types using association rule based classification Park, Sung Hee Reyes, José A Gilbert, David R Kim, Ji Woong Kim, Sangsoo BMC Bioinformatics Research Article BACKGROUND: Protein-protein interactions (PPI) can be classified according to their characteristics into, for example obligate or transient interactions. The identification and characterization of these PPI types may help in the functional annotation of new protein complexes and in the prediction of protein interaction partners by knowledge driven approaches. RESULTS: This work addresses pattern discovery of the interaction sites for four different interaction types to characterize and uses them for the prediction of PPI types employing Association Rule Based Classification (ARBC) which includes association rule generation and posterior classification. We incorporated domain information from protein complexes in SCOP proteins and identified 354 domain-interaction sites. 14 interface properties were calculated from amino acid and secondary structure composition and then used to generate a set of association rules characterizing these domain-interaction sites employing the APRIORI algorithm. Our results regarding the classification of PPI types based on a set of discovered association rules shows that the discriminative ability of association rules can significantly impact on the prediction power of classification models. We also showed that the accuracy of the classification can be improved through the use of structural domain information and also the use of secondary structure content. CONCLUSION: The advantage of our approach is that we can extract biologically significant information from the interpretation of the discovered association rules in terms of understandability and interpretability of rules. A web application based on our method can be found at BioMed Central 2009-01-28 /pmc/articles/PMC2667511/ /pubmed/19173748 http://dx.doi.org/10.1186/1471-2105-10-36 Text en Copyright © 2009 Park et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Park, Sung Hee Reyes, José A Gilbert, David R Kim, Ji Woong Kim, Sangsoo Prediction of protein-protein interaction types using association rule based classification |
title | Prediction of protein-protein interaction types using association rule based classification |
title_full | Prediction of protein-protein interaction types using association rule based classification |
title_fullStr | Prediction of protein-protein interaction types using association rule based classification |
title_full_unstemmed | Prediction of protein-protein interaction types using association rule based classification |
title_short | Prediction of protein-protein interaction types using association rule based classification |
title_sort | prediction of protein-protein interaction types using association rule based classification |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2667511/ https://www.ncbi.nlm.nih.gov/pubmed/19173748 http://dx.doi.org/10.1186/1471-2105-10-36 |
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