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A systematic identification of species-specific protein succinylation sites using joint element features information
Lysine succinylation, an important type of protein posttranslational modification, plays significant roles in many cellular processes. Accurate identification of succinylation sites can facilitate our understanding about the molecular mechanism and potential roles of lysine succinylation. However, e...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Dove Medical Press
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5584904/ https://www.ncbi.nlm.nih.gov/pubmed/28894368 http://dx.doi.org/10.2147/IJN.S140875 |
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author | Hasan, Md Mehedi Khatun, Mst Shamima Mollah, Md Nurul Haque Yong, Cao Guo, Dianjing |
author_facet | Hasan, Md Mehedi Khatun, Mst Shamima Mollah, Md Nurul Haque Yong, Cao Guo, Dianjing |
author_sort | Hasan, Md Mehedi |
collection | PubMed |
description | Lysine succinylation, an important type of protein posttranslational modification, plays significant roles in many cellular processes. Accurate identification of succinylation sites can facilitate our understanding about the molecular mechanism and potential roles of lysine succinylation. However, even in well-studied systems, a majority of the succinylation sites remain undetected because the traditional experimental approaches to succinylation site identification are often costly, time-consuming, and laborious. In silico approach, on the other hand, is potentially an alternative strategy to predict succinylation substrates. In this paper, a novel computational predictor SuccinSite2.0 was developed for predicting generic and species-specific protein succinylation sites. This predictor takes the composition of profile-based amino acid and orthogonal binary features, which were used to train a random forest classifier. We demonstrated that the proposed SuccinSite2.0 predictor outperformed other currently existing implementations on a complementarily independent dataset. Furthermore, the important features that make visible contributions to species-specific and cross-species-specific prediction of protein succinylation site were analyzed. The proposed predictor is anticipated to be a useful computational resource for lysine succinylation site prediction. The integrated species-specific online tool of SuccinSite2.0 is publicly accessible. |
format | Online Article Text |
id | pubmed-5584904 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Dove Medical Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-55849042017-09-11 A systematic identification of species-specific protein succinylation sites using joint element features information Hasan, Md Mehedi Khatun, Mst Shamima Mollah, Md Nurul Haque Yong, Cao Guo, Dianjing Int J Nanomedicine Original Research Lysine succinylation, an important type of protein posttranslational modification, plays significant roles in many cellular processes. Accurate identification of succinylation sites can facilitate our understanding about the molecular mechanism and potential roles of lysine succinylation. However, even in well-studied systems, a majority of the succinylation sites remain undetected because the traditional experimental approaches to succinylation site identification are often costly, time-consuming, and laborious. In silico approach, on the other hand, is potentially an alternative strategy to predict succinylation substrates. In this paper, a novel computational predictor SuccinSite2.0 was developed for predicting generic and species-specific protein succinylation sites. This predictor takes the composition of profile-based amino acid and orthogonal binary features, which were used to train a random forest classifier. We demonstrated that the proposed SuccinSite2.0 predictor outperformed other currently existing implementations on a complementarily independent dataset. Furthermore, the important features that make visible contributions to species-specific and cross-species-specific prediction of protein succinylation site were analyzed. The proposed predictor is anticipated to be a useful computational resource for lysine succinylation site prediction. The integrated species-specific online tool of SuccinSite2.0 is publicly accessible. Dove Medical Press 2017-08-28 /pmc/articles/PMC5584904/ /pubmed/28894368 http://dx.doi.org/10.2147/IJN.S140875 Text en © 2017 Hasan et al. This work is published and licensed by Dove Medical Press Limited The full terms of this license are available at https://www.dovepress.com/terms.php and incorporate the Creative Commons Attribution – Non Commercial (unported, v3.0) License (http://creativecommons.org/licenses/by-nc/3.0/). By accessing the work you hereby accept the Terms. 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 Hasan, Md Mehedi Khatun, Mst Shamima Mollah, Md Nurul Haque Yong, Cao Guo, Dianjing A systematic identification of species-specific protein succinylation sites using joint element features information |
title | A systematic identification of species-specific protein succinylation sites using joint element features information |
title_full | A systematic identification of species-specific protein succinylation sites using joint element features information |
title_fullStr | A systematic identification of species-specific protein succinylation sites using joint element features information |
title_full_unstemmed | A systematic identification of species-specific protein succinylation sites using joint element features information |
title_short | A systematic identification of species-specific protein succinylation sites using joint element features information |
title_sort | systematic identification of species-specific protein succinylation sites using joint element features information |
topic | Original Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5584904/ https://www.ncbi.nlm.nih.gov/pubmed/28894368 http://dx.doi.org/10.2147/IJN.S140875 |
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