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ENTAIL: yEt aNoTher amyloid fIbrils cLassifier
BACKGROUND: This research aims to increase our knowledge of amyloidoses. These disorders cause incorrect protein folding, affecting protein functionality (on structure). Fibrillar deposits are the basis of some wellknown diseases, such as Alzheimer, Creutzfeldt–Jakob diseases and type II diabetes. F...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9714056/ https://www.ncbi.nlm.nih.gov/pubmed/36456900 http://dx.doi.org/10.1186/s12859-022-05070-6 |
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author | Auriemma Citarella, Alessia Di Biasi, Luigi De Marco, Fabiola Tortora, Genoveffa |
author_facet | Auriemma Citarella, Alessia Di Biasi, Luigi De Marco, Fabiola Tortora, Genoveffa |
author_sort | Auriemma Citarella, Alessia |
collection | PubMed |
description | BACKGROUND: This research aims to increase our knowledge of amyloidoses. These disorders cause incorrect protein folding, affecting protein functionality (on structure). Fibrillar deposits are the basis of some wellknown diseases, such as Alzheimer, Creutzfeldt–Jakob diseases and type II diabetes. For many of these amyloid proteins, the relative precursors are known. Discovering new protein precursors involved in forming amyloid fibril deposits would improve understanding the pathological processes of amyloidoses. RESULTS: A new classifier, called ENTAIL, was developed using over than 4000 molecular descriptors. ENTAIL was based on the Naive Bayes Classifier with Unbounded Support and Gaussian Kernel Type, with an accuracy on the test set of 81.80%, SN of 100%, SP of 63.63% and an MCC of 0.683 on a balanced dataset. CONCLUSIONS: The analysis carried out has demonstrated how, despite the various configurations of the tests, performances are superior in terms of performance on a balanced dataset. |
format | Online Article Text |
id | pubmed-9714056 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-97140562022-12-02 ENTAIL: yEt aNoTher amyloid fIbrils cLassifier Auriemma Citarella, Alessia Di Biasi, Luigi De Marco, Fabiola Tortora, Genoveffa BMC Bioinformatics Research BACKGROUND: This research aims to increase our knowledge of amyloidoses. These disorders cause incorrect protein folding, affecting protein functionality (on structure). Fibrillar deposits are the basis of some wellknown diseases, such as Alzheimer, Creutzfeldt–Jakob diseases and type II diabetes. For many of these amyloid proteins, the relative precursors are known. Discovering new protein precursors involved in forming amyloid fibril deposits would improve understanding the pathological processes of amyloidoses. RESULTS: A new classifier, called ENTAIL, was developed using over than 4000 molecular descriptors. ENTAIL was based on the Naive Bayes Classifier with Unbounded Support and Gaussian Kernel Type, with an accuracy on the test set of 81.80%, SN of 100%, SP of 63.63% and an MCC of 0.683 on a balanced dataset. CONCLUSIONS: The analysis carried out has demonstrated how, despite the various configurations of the tests, performances are superior in terms of performance on a balanced dataset. BioMed Central 2022-12-01 /pmc/articles/PMC9714056/ /pubmed/36456900 http://dx.doi.org/10.1186/s12859-022-05070-6 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/ (https://creativecommons.org/publicdomain/zero/1.0/) ) applies to the data made available in this article, unless otherwise stated in a credit line to the data. |
spellingShingle | Research Auriemma Citarella, Alessia Di Biasi, Luigi De Marco, Fabiola Tortora, Genoveffa ENTAIL: yEt aNoTher amyloid fIbrils cLassifier |
title | ENTAIL: yEt aNoTher amyloid fIbrils cLassifier |
title_full | ENTAIL: yEt aNoTher amyloid fIbrils cLassifier |
title_fullStr | ENTAIL: yEt aNoTher amyloid fIbrils cLassifier |
title_full_unstemmed | ENTAIL: yEt aNoTher amyloid fIbrils cLassifier |
title_short | ENTAIL: yEt aNoTher amyloid fIbrils cLassifier |
title_sort | entail: yet another amyloid fibrils classifier |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9714056/ https://www.ncbi.nlm.nih.gov/pubmed/36456900 http://dx.doi.org/10.1186/s12859-022-05070-6 |
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