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Protein functional annotation of simultaneously improved stability, accuracy and false discovery rate achieved by a sequence-based deep learning
Functional annotation of protein sequence with high accuracy has become one of the most important issues in modern biomedical studies, and computational approaches of significantly accelerated analysis process and enhanced accuracy are greatly desired. Although a variety of methods have been develop...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7412958/ https://www.ncbi.nlm.nih.gov/pubmed/31504150 http://dx.doi.org/10.1093/bib/bbz081 |
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author | Hong, Jiajun Luo, Yongchao Zhang, Yang Ying, Junbiao Xue, Weiwei Xie, Tian Tao, Lin Zhu, Feng |
author_facet | Hong, Jiajun Luo, Yongchao Zhang, Yang Ying, Junbiao Xue, Weiwei Xie, Tian Tao, Lin Zhu, Feng |
author_sort | Hong, Jiajun |
collection | PubMed |
description | Functional annotation of protein sequence with high accuracy has become one of the most important issues in modern biomedical studies, and computational approaches of significantly accelerated analysis process and enhanced accuracy are greatly desired. Although a variety of methods have been developed to elevate protein annotation accuracy, their ability in controlling false annotation rates remains either limited or not systematically evaluated. In this study, a protein encoding strategy, together with a deep learning algorithm, was proposed to control the false discovery rate in protein function annotation, and its performances were systematically compared with that of the traditional similarity-based and de novo approaches. Based on a comprehensive assessment from multiple perspectives, the proposed strategy and algorithm were found to perform better in both prediction stability and annotation accuracy compared with other de novo methods. Moreover, an in-depth assessment revealed that it possessed an improved capacity of controlling the false discovery rate compared with traditional methods. All in all, this study not only provided a comprehensive analysis on the performances of the newly proposed strategy but also provided a tool for the researcher in the fields of protein function annotation. |
format | Online Article Text |
id | pubmed-7412958 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-74129582020-08-12 Protein functional annotation of simultaneously improved stability, accuracy and false discovery rate achieved by a sequence-based deep learning Hong, Jiajun Luo, Yongchao Zhang, Yang Ying, Junbiao Xue, Weiwei Xie, Tian Tao, Lin Zhu, Feng Brief Bioinform Problem Solving Protocol Functional annotation of protein sequence with high accuracy has become one of the most important issues in modern biomedical studies, and computational approaches of significantly accelerated analysis process and enhanced accuracy are greatly desired. Although a variety of methods have been developed to elevate protein annotation accuracy, their ability in controlling false annotation rates remains either limited or not systematically evaluated. In this study, a protein encoding strategy, together with a deep learning algorithm, was proposed to control the false discovery rate in protein function annotation, and its performances were systematically compared with that of the traditional similarity-based and de novo approaches. Based on a comprehensive assessment from multiple perspectives, the proposed strategy and algorithm were found to perform better in both prediction stability and annotation accuracy compared with other de novo methods. Moreover, an in-depth assessment revealed that it possessed an improved capacity of controlling the false discovery rate compared with traditional methods. All in all, this study not only provided a comprehensive analysis on the performances of the newly proposed strategy but also provided a tool for the researcher in the fields of protein function annotation. Oxford University Press 2019-08-02 /pmc/articles/PMC7412958/ /pubmed/31504150 http://dx.doi.org/10.1093/bib/bbz081 Text en © The Author(s) 2019. Published by Oxford University Press. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
spellingShingle | Problem Solving Protocol Hong, Jiajun Luo, Yongchao Zhang, Yang Ying, Junbiao Xue, Weiwei Xie, Tian Tao, Lin Zhu, Feng Protein functional annotation of simultaneously improved stability, accuracy and false discovery rate achieved by a sequence-based deep learning |
title | Protein functional annotation of simultaneously improved stability, accuracy and false discovery rate achieved by a sequence-based deep learning |
title_full | Protein functional annotation of simultaneously improved stability, accuracy and false discovery rate achieved by a sequence-based deep learning |
title_fullStr | Protein functional annotation of simultaneously improved stability, accuracy and false discovery rate achieved by a sequence-based deep learning |
title_full_unstemmed | Protein functional annotation of simultaneously improved stability, accuracy and false discovery rate achieved by a sequence-based deep learning |
title_short | Protein functional annotation of simultaneously improved stability, accuracy and false discovery rate achieved by a sequence-based deep learning |
title_sort | protein functional annotation of simultaneously improved stability, accuracy and false discovery rate achieved by a sequence-based deep learning |
topic | Problem Solving Protocol |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7412958/ https://www.ncbi.nlm.nih.gov/pubmed/31504150 http://dx.doi.org/10.1093/bib/bbz081 |
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