Evidence map›Paper›PMID 27669239›Full record

ArticleInternational journal of molecular sciences2016

Identification of Protein-Protein Interactions via a Novel Matrix-Based Sequence Representation Model with Amino Acid Contact Information.

Yijie Ding, Jijun Tang, Fei Guo

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Article in International journal of molecular sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

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38citing papers in PubMed
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1 · What the graph read from it

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3 · Its place in the literature

Who cites it

38 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

3 authors.

Yijie DingSchool of Computer Science and Technology, Tianjin University, Tianjin 300350, China. wuxi_dyj@tju.edu.cn.
Jijun TangSchool of Computer Science and Technology, Tianjin University, Tianjin 300350, China. tangjijun@tju.edu.cn.
Fei GuoSchool of Computer Science and Technology, Tianjin University, Tianjin 300350, China. fguo@tju.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Identification of protein-protein interactions (PPIs) is a difficult and important problem in biology. Since experimental methods for predicting PPIs are both expensive and time-consuming, many computational methods have been developed to predict PPIs and interaction networks, which can be used to complement experimental approaches. However, these methods have limitations to overcome. They need a large number of homology proteins or literature to be applied in their method. In this paper, we propose a novel matrix-based protein sequence representation approach to predict PPIs, using an ensemble learning method for classification. We construct the matrix of Amino Acid Contact (AAC), based on the statistical analysis of residue-pairing frequencies in a database of 6323 protein-protein complexes. We first represent the protein sequence as a Substitution Matrix Representation (SMR) matrix. Then, the feature vector is extracted by applying algorithms of Histogram of Oriented Gradient (HOG) and Singular Value Decomposition (SVD) on the SMR matrix. Finally, we feed the feature vector into a Random Forest (RF) for judging interaction pairs and non-interaction pairs. Our method is applied to several PPI datasets to evaluate its performance. On the S . c e r e v i s i a e dataset, our method achieves 94 . 83 % accuracy and 92 . 40 % sensitivity. Compared with existing methods, and the accuracy of our method is increased by 0 . 11 percentage points. On the H . p y l o r i dataset, our method achieves 89 . 06 % accuracy and 88 . 15 % sensitivity, the accuracy of our method is increased by 0 . 76 % . On the H u m a n PPI dataset, our method achieves 97 . 60 % accuracy and 96 . 37 % sensitivity, and the accuracy of our method is increased by 1 . 30 % . In addition, we test our method on a very important PPI network, and it achieves 92 . 71 % accuracy. In the Wnt-related network, the accuracy of our method is increased by 16 . 67 % . The source code and all datasets are available at https://figshare.com/s/580c11dce13e63cb9a53.

Indexed as

AlgorithmsAmino AcidsAnimalsDatabases, ProteinHumansProtein Interaction MapsProteinsSaccharomyces cerevisiaeAmino AcidsProteinsamino acid contactfeature extractionprotein–protein interactionsprotein sequencesubstitution matrix representation

Identifiers

PMID27669239
PMCPMC5085656

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.