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Using Random Forest Model Combined With Gabor Feature to Predict Protein-Protein Interaction From Protein Sequence

Protein-protein interactions (PPIs) play a crucial role in the life cycles of living cells. Thus, it is important to understand the underlying mechanisms of PPIs. Although many high-throughput technologies have generated large amounts of PPI data in different organisms, the experiments for detecting...

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Autores principales: Zhan, Xin-Ke, You, Zhu-Hong, Li, Li-Ping, Li, Yang, Wang, Zheng, Pan, Jie
Formato: Online Artículo Texto
Lenguaje:English
Publicado: SAGE Publications 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7328357/
https://www.ncbi.nlm.nih.gov/pubmed/32655275
http://dx.doi.org/10.1177/1176934320934498
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author Zhan, Xin-Ke
You, Zhu-Hong
Li, Li-Ping
Li, Yang
Wang, Zheng
Pan, Jie
author_facet Zhan, Xin-Ke
You, Zhu-Hong
Li, Li-Ping
Li, Yang
Wang, Zheng
Pan, Jie
author_sort Zhan, Xin-Ke
collection PubMed
description Protein-protein interactions (PPIs) play a crucial role in the life cycles of living cells. Thus, it is important to understand the underlying mechanisms of PPIs. Although many high-throughput technologies have generated large amounts of PPI data in different organisms, the experiments for detecting PPIs are still costly and time-consuming. Therefore, novel computational methods are urgently needed for predicting PPIs. For this reason, developing a new computational method for predicting PPIs is drawing more and more attention. In this study, we proposed a novel computational method based on texture feature of protein sequence for predicting PPIs. Especially, the Gabor feature is used to extract texture feature and protein evolutionary information from Position-Specific Scoring Matrix, which is generated by Position-Specific Iterated Basic Local Alignment Search Tool. Then, random forest–based classifiers are used to infer the protein interactions. When performed on PPI data sets of yeast, human, and Helicobacter pylori, we obtained good results with average accuracies of 92.10%, 97.03%, and 86.45%, respectively. To better evaluate the proposed method, we compared Gabor feature, Discrete Cosine Transform, and Local Phase Quantization. Our results show that the proposed method is both feasible and stable and the Gabor feature descriptor is reliable in extracting protein sequence information. Furthermore, additional experiments have been conducted to predict PPIs of other 4 species data sets. The promising results indicate that our proposed method is both powerful and robust.
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spelling pubmed-73283572020-07-09 Using Random Forest Model Combined With Gabor Feature to Predict Protein-Protein Interaction From Protein Sequence Zhan, Xin-Ke You, Zhu-Hong Li, Li-Ping Li, Yang Wang, Zheng Pan, Jie Evol Bioinform Online Methods and Protocols Protein-protein interactions (PPIs) play a crucial role in the life cycles of living cells. Thus, it is important to understand the underlying mechanisms of PPIs. Although many high-throughput technologies have generated large amounts of PPI data in different organisms, the experiments for detecting PPIs are still costly and time-consuming. Therefore, novel computational methods are urgently needed for predicting PPIs. For this reason, developing a new computational method for predicting PPIs is drawing more and more attention. In this study, we proposed a novel computational method based on texture feature of protein sequence for predicting PPIs. Especially, the Gabor feature is used to extract texture feature and protein evolutionary information from Position-Specific Scoring Matrix, which is generated by Position-Specific Iterated Basic Local Alignment Search Tool. Then, random forest–based classifiers are used to infer the protein interactions. When performed on PPI data sets of yeast, human, and Helicobacter pylori, we obtained good results with average accuracies of 92.10%, 97.03%, and 86.45%, respectively. To better evaluate the proposed method, we compared Gabor feature, Discrete Cosine Transform, and Local Phase Quantization. Our results show that the proposed method is both feasible and stable and the Gabor feature descriptor is reliable in extracting protein sequence information. Furthermore, additional experiments have been conducted to predict PPIs of other 4 species data sets. The promising results indicate that our proposed method is both powerful and robust. SAGE Publications 2020-06-30 /pmc/articles/PMC7328357/ /pubmed/32655275 http://dx.doi.org/10.1177/1176934320934498 Text en © The Author(s) 2020 https://creativecommons.org/licenses/by-nc/4.0/ This article is distributed under the terms of the Creative Commons Attribution-NonCommercial 4.0 License (https://creativecommons.org/licenses/by-nc/4.0/) which permits non-commercial use, reproduction and distribution of the work without further permission provided the original work is attributed as specified on the SAGE and Open Access page (https://us.sagepub.com/en-us/nam/open-access-at-sage).
spellingShingle Methods and Protocols
Zhan, Xin-Ke
You, Zhu-Hong
Li, Li-Ping
Li, Yang
Wang, Zheng
Pan, Jie
Using Random Forest Model Combined With Gabor Feature to Predict Protein-Protein Interaction From Protein Sequence
title Using Random Forest Model Combined With Gabor Feature to Predict Protein-Protein Interaction From Protein Sequence
title_full Using Random Forest Model Combined With Gabor Feature to Predict Protein-Protein Interaction From Protein Sequence
title_fullStr Using Random Forest Model Combined With Gabor Feature to Predict Protein-Protein Interaction From Protein Sequence
title_full_unstemmed Using Random Forest Model Combined With Gabor Feature to Predict Protein-Protein Interaction From Protein Sequence
title_short Using Random Forest Model Combined With Gabor Feature to Predict Protein-Protein Interaction From Protein Sequence
title_sort using random forest model combined with gabor feature to predict protein-protein interaction from protein sequence
topic Methods and Protocols
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7328357/
https://www.ncbi.nlm.nih.gov/pubmed/32655275
http://dx.doi.org/10.1177/1176934320934498
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