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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...

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Autores principales: Datta, Sutapa, Mukhopadhyay, Subhasis
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Dove Medical Press 2014
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.
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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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