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PITHIA: Protein Interaction Site Prediction Using Multiple Sequence Alignments and Attention

Cellular functions are governed by proteins, and, while some proteins work independently, most work by interacting with other proteins. As a result it is crucially important to know the interaction sites that facilitate the interactions between the proteins. Since the experimental methods are costly...

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Detalles Bibliográficos
Autores principales: Hosseini, SeyedMohsen, Ilie, Lucian
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9657891/
https://www.ncbi.nlm.nih.gov/pubmed/36361606
http://dx.doi.org/10.3390/ijms232112814
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author Hosseini, SeyedMohsen
Ilie, Lucian
author_facet Hosseini, SeyedMohsen
Ilie, Lucian
author_sort Hosseini, SeyedMohsen
collection PubMed
description Cellular functions are governed by proteins, and, while some proteins work independently, most work by interacting with other proteins. As a result it is crucially important to know the interaction sites that facilitate the interactions between the proteins. Since the experimental methods are costly and time consuming, it is essential to develop effective computational methods. We present PITHIA, a sequence-based deep learning model for protein interaction site prediction that exploits the combination of multiple sequence alignments and learning attention. We demonstrate that our new model clearly outperforms the state-of-the-art models on a wide range of metrics. In order to provide meaningful comparison, we update existing test datasets with new information regarding interaction site, as well as introduce an additional new testing dataset which resolves the shortcomings of the existing ones.
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spelling pubmed-96578912022-11-15 PITHIA: Protein Interaction Site Prediction Using Multiple Sequence Alignments and Attention Hosseini, SeyedMohsen Ilie, Lucian Int J Mol Sci Article Cellular functions are governed by proteins, and, while some proteins work independently, most work by interacting with other proteins. As a result it is crucially important to know the interaction sites that facilitate the interactions between the proteins. Since the experimental methods are costly and time consuming, it is essential to develop effective computational methods. We present PITHIA, a sequence-based deep learning model for protein interaction site prediction that exploits the combination of multiple sequence alignments and learning attention. We demonstrate that our new model clearly outperforms the state-of-the-art models on a wide range of metrics. In order to provide meaningful comparison, we update existing test datasets with new information regarding interaction site, as well as introduce an additional new testing dataset which resolves the shortcomings of the existing ones. MDPI 2022-10-24 /pmc/articles/PMC9657891/ /pubmed/36361606 http://dx.doi.org/10.3390/ijms232112814 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Hosseini, SeyedMohsen
Ilie, Lucian
PITHIA: Protein Interaction Site Prediction Using Multiple Sequence Alignments and Attention
title PITHIA: Protein Interaction Site Prediction Using Multiple Sequence Alignments and Attention
title_full PITHIA: Protein Interaction Site Prediction Using Multiple Sequence Alignments and Attention
title_fullStr PITHIA: Protein Interaction Site Prediction Using Multiple Sequence Alignments and Attention
title_full_unstemmed PITHIA: Protein Interaction Site Prediction Using Multiple Sequence Alignments and Attention
title_short PITHIA: Protein Interaction Site Prediction Using Multiple Sequence Alignments and Attention
title_sort pithia: protein interaction site prediction using multiple sequence alignments and attention
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9657891/
https://www.ncbi.nlm.nih.gov/pubmed/36361606
http://dx.doi.org/10.3390/ijms232112814
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