Evidence map›Paper›PMID 34413375›Full record

ArticleScientific reports2021

Robust and accurate prediction of protein-protein interactions by exploiting evolutionary information.

Yang Li, Zheng Wang, Li-Ping Li, Zhu-Hong You, Wen-Zhun Huang, Xin-Ke Zhan, Yan-Bin Wang

Abstract read
In one paragraph

Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

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0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

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3 · Its place in the literature

Who cites it

15 citing papers in PubMed.

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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

7 authors.

Yang LiSchool of Information Engineering, Xijing University, Xi'an, 710123, China.
Zheng WangSchool of Information Engineering, Xijing University, Xi'an, 710123, China. xywangzheng0971@163.com.
Li-Ping LiSchool of Information Engineering, Xijing University, Xi'an, 710123, China. Lipingli@gmail.com.
Zhu-Hong YouSchool of Information Engineering, Xijing University, Xi'an, 710123, China.
Wen-Zhun HuangSchool of Information Engineering, Xijing University, Xi'an, 710123, China.
Xin-Ke ZhanSchool of Information Engineering, Xijing University, Xi'an, 710123, China.
Yan-Bin WangSchool of Cyber Science and Technology, Zhejiang University, Hangzhou, 310027, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Various biochemical functions of organisms are performed by protein-protein interactions (PPIs). Therefore, recognition of protein-protein interactions is very important for understanding most life activities, such as DNA replication and transcription, protein synthesis and secretion, signal transduction and metabolism. Although high-throughput technology makes it possible to generate large-scale PPIs data, it requires expensive cost of both time and labor, and leave a risk of high false positive rate. In order to formulate a more ingenious solution, biology community is looking for computational methods to quickly and efficiently discover massive protein interaction data. In this paper, we propose a computational method for predicting PPIs based on a fresh idea of combining orthogonal locality preserving projections (OLPP) and rotation forest (RoF) models, using protein sequence information. Specifically, the protein sequence is first converted into position-specific scoring matrices (PSSMs) containing protein evolutionary information by using the Position-Specific Iterated Basic Local Alignment Search Tool (PSI-BLAST). Then we characterize a protein as a fixed length feature vector by applying OLPP to PSSMs. Finally, we train an RoF classifier for the purpose of identifying non-interacting and interacting protein pairs. The proposed method yielded a significantly better results than existing methods, with 90.07% and 96.09% prediction accuracy on Yeast and Human datasets. Our experiment show the proposed method can serve as a useful tool to accelerate the process of solving key problems in proteomics.

Indexed as

Evolution, MolecularProtein Interaction MappingDatabases, ProteinHumansReproducibility of ResultsROC CurveSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSupport Vector MachineSaccharomyces cerevisiae Proteins

Identifiers

PMID34413375
PMCPMC8376940

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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.