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An Ensemble Method with Hybrid Features to Identify Extracellular Matrix Proteins
The extracellular matrix (ECM) is a dynamic composite of secreted proteins that play important roles in numerous biological processes such as tissue morphogenesis, differentiation and homeostasis. Furthermore, various diseases are caused by the dysfunction of ECM proteins. Therefore, identifying the...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4334504/ https://www.ncbi.nlm.nih.gov/pubmed/25680094 http://dx.doi.org/10.1371/journal.pone.0117804 |
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author | Yang, Runtao Zhang, Chengjin Gao, Rui Zhang, Lina |
author_facet | Yang, Runtao Zhang, Chengjin Gao, Rui Zhang, Lina |
author_sort | Yang, Runtao |
collection | PubMed |
description | The extracellular matrix (ECM) is a dynamic composite of secreted proteins that play important roles in numerous biological processes such as tissue morphogenesis, differentiation and homeostasis. Furthermore, various diseases are caused by the dysfunction of ECM proteins. Therefore, identifying these important ECM proteins may assist in understanding related biological processes and drug development. In view of the serious imbalance in the training dataset, a Random Forest-based ensemble method with hybrid features is developed in this paper to identify ECM proteins. Hybrid features are employed by incorporating sequence composition, physicochemical properties, evolutionary and structural information. The Information Gain Ratio and Incremental Feature Selection (IGR-IFS) methods are adopted to select the optimal features. Finally, the resulting predictor termed IECMP (Identify ECM Proteins) achieves an balanced accuracy of 86.4% using the 10-fold cross-validation on the training dataset, which is much higher than results obtained by other methods (ECMPRED: 71.0%, ECMPP: 77.8%). Moreover, when tested on a common independent dataset, our method also achieves significantly improved performance over ECMPP and ECMPRED. These results indicate that IECMP is an effective method for ECM protein prediction, which has a more balanced prediction capability for positive and negative samples. It is anticipated that the proposed method will provide significant information to fully decipher the molecular mechanisms of ECM-related biological processes and discover candidate drug targets. For public access, we develop a user-friendly web server for ECM protein identification that is freely accessible at http://iecmp.weka.cc. |
format | Online Article Text |
id | pubmed-4334504 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-43345042015-02-24 An Ensemble Method with Hybrid Features to Identify Extracellular Matrix Proteins Yang, Runtao Zhang, Chengjin Gao, Rui Zhang, Lina PLoS One Research Article The extracellular matrix (ECM) is a dynamic composite of secreted proteins that play important roles in numerous biological processes such as tissue morphogenesis, differentiation and homeostasis. Furthermore, various diseases are caused by the dysfunction of ECM proteins. Therefore, identifying these important ECM proteins may assist in understanding related biological processes and drug development. In view of the serious imbalance in the training dataset, a Random Forest-based ensemble method with hybrid features is developed in this paper to identify ECM proteins. Hybrid features are employed by incorporating sequence composition, physicochemical properties, evolutionary and structural information. The Information Gain Ratio and Incremental Feature Selection (IGR-IFS) methods are adopted to select the optimal features. Finally, the resulting predictor termed IECMP (Identify ECM Proteins) achieves an balanced accuracy of 86.4% using the 10-fold cross-validation on the training dataset, which is much higher than results obtained by other methods (ECMPRED: 71.0%, ECMPP: 77.8%). Moreover, when tested on a common independent dataset, our method also achieves significantly improved performance over ECMPP and ECMPRED. These results indicate that IECMP is an effective method for ECM protein prediction, which has a more balanced prediction capability for positive and negative samples. It is anticipated that the proposed method will provide significant information to fully decipher the molecular mechanisms of ECM-related biological processes and discover candidate drug targets. For public access, we develop a user-friendly web server for ECM protein identification that is freely accessible at http://iecmp.weka.cc. Public Library of Science 2015-02-13 /pmc/articles/PMC4334504/ /pubmed/25680094 http://dx.doi.org/10.1371/journal.pone.0117804 Text en © 2015 Yang et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Yang, Runtao Zhang, Chengjin Gao, Rui Zhang, Lina An Ensemble Method with Hybrid Features to Identify Extracellular Matrix Proteins |
title | An Ensemble Method with Hybrid Features to Identify Extracellular Matrix Proteins |
title_full | An Ensemble Method with Hybrid Features to Identify Extracellular Matrix Proteins |
title_fullStr | An Ensemble Method with Hybrid Features to Identify Extracellular Matrix Proteins |
title_full_unstemmed | An Ensemble Method with Hybrid Features to Identify Extracellular Matrix Proteins |
title_short | An Ensemble Method with Hybrid Features to Identify Extracellular Matrix Proteins |
title_sort | ensemble method with hybrid features to identify extracellular matrix proteins |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4334504/ https://www.ncbi.nlm.nih.gov/pubmed/25680094 http://dx.doi.org/10.1371/journal.pone.0117804 |
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