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An ensemble method approach to investigate kinase-specific phosphorylation sites
Protein phosphorylation is one of the most significant and well-studied post-translational modifications, and it plays an important role in various cellular processes. It has made a considerable impact in understanding the protein functions which are involved in revealing signal transductions and va...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Dove Medical Press
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4026567/ https://www.ncbi.nlm.nih.gov/pubmed/24872686 http://dx.doi.org/10.2147/IJN.S57526 |
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author | Datta, Sutapa Mukhopadhyay, Subhasis |
author_facet | Datta, Sutapa Mukhopadhyay, Subhasis |
author_sort | Datta, Sutapa |
collection | PubMed |
description | Protein phosphorylation is one of the most significant and well-studied post-translational modifications, and it plays an important role in various cellular processes. It has made a considerable impact in understanding the protein functions which are involved in revealing signal transductions and various diseases. The identification of kinase-specific phosphorylation sites has an important role in elucidating the mechanism of phosphorylation; however, experimental techniques for identifying phosphorylation sites are labor intensive and expensive. An exponentially increasing number of protein sequences generated by various laboratories across the globe require computer-aided procedures for reliably and quickly identifying the phosphorylation sites, opening a new horizon for in silico analysis. In this regard, we have introduced a novel ensemble method where we have selected three classifiers (least square support vector machine, multilayer perceptron, and k-Nearest Neighbor) and three different feature encoding parameters (dipeptide composition, physicochemical properties of amino acids, and protein–protein similarity score). Each of these classifiers is trained on each of the three different parameter systems. The final results of the ensemble method are obtained by fusing the results of all the classifiers by a weighted voting algorithm. Extensive experiments reveal that our proposed method can successfully predict phosphorylation sites in a kinase-specific manner and performs significantly better when compared with other existing phosphorylation site prediction methods. |
format | Online Article Text |
id | pubmed-4026567 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Dove Medical Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-40265672014-05-28 An ensemble method approach to investigate kinase-specific phosphorylation sites Datta, Sutapa Mukhopadhyay, Subhasis Int J Nanomedicine Original Research Protein phosphorylation is one of the most significant and well-studied post-translational modifications, and it plays an important role in various cellular processes. It has made a considerable impact in understanding the protein functions which are involved in revealing signal transductions and various diseases. The identification of kinase-specific phosphorylation sites has an important role in elucidating the mechanism of phosphorylation; however, experimental techniques for identifying phosphorylation sites are labor intensive and expensive. An exponentially increasing number of protein sequences generated by various laboratories across the globe require computer-aided procedures for reliably and quickly identifying the phosphorylation sites, opening a new horizon for in silico analysis. In this regard, we have introduced a novel ensemble method where we have selected three classifiers (least square support vector machine, multilayer perceptron, and k-Nearest Neighbor) and three different feature encoding parameters (dipeptide composition, physicochemical properties of amino acids, and protein–protein similarity score). Each of these classifiers is trained on each of the three different parameter systems. The final results of the ensemble method are obtained by fusing the results of all the classifiers by a weighted voting algorithm. Extensive experiments reveal that our proposed method can successfully predict phosphorylation sites in a kinase-specific manner and performs significantly better when compared with other existing phosphorylation site prediction methods. Dove Medical Press 2014-05-10 /pmc/articles/PMC4026567/ /pubmed/24872686 http://dx.doi.org/10.2147/IJN.S57526 Text en © 2014 Datta and Mukhopadhyay. This work is published by Dove Medical Press Limited, and licensed under Creative Commons Attribution – Non Commercial (unported, v3.0) License The full terms of the License are available at http://creativecommons.org/licenses/by-nc/3.0/. Non-commercial uses of the work are permitted without any further permission from Dove Medical Press Limited, provided the work is properly attributed. |
spellingShingle | Original Research Datta, Sutapa Mukhopadhyay, Subhasis An ensemble method approach to investigate kinase-specific phosphorylation sites |
title | An ensemble method approach to investigate kinase-specific phosphorylation sites |
title_full | An ensemble method approach to investigate kinase-specific phosphorylation sites |
title_fullStr | An ensemble method approach to investigate kinase-specific phosphorylation sites |
title_full_unstemmed | An ensemble method approach to investigate kinase-specific phosphorylation sites |
title_short | An ensemble method approach to investigate kinase-specific phosphorylation sites |
title_sort | ensemble method approach to investigate kinase-specific phosphorylation sites |
topic | Original Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4026567/ https://www.ncbi.nlm.nih.gov/pubmed/24872686 http://dx.doi.org/10.2147/IJN.S57526 |
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