Evidence map›Paper›PMID 30646505›Full record

ArticleInternational journal of molecular sciences2019

KSIMC: Predicting Kinase⁻Substrate Interactions Based on Matrix Completion.

Jingzhong Gan, Jie Qiu, Canshang Deng, Wei Lan, Qingfeng Chen, Yanling Hu

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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

The trial behind it

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3 · Its place in the literature

Who cites it

3 citing papers in PubMed.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Jingzhong GanSchool of Computer Science and Engineering, Yulin Normal University, Yulin 537000, China. jgxygjz@126.com.
Jie QiuSchool of Computer Science and Engineering, Yulin Normal University, Yulin 537000, China. jgxyqj@126.com.
Canshang DengSchool of Computer, Electronics and Information, Guangxi University, Nanning 530004, China. dcs288@mail.gxu.cn.
Wei LanSchool of Computer, Electronics and Information, Guangxi University, Nanning 530004, China. lanwei@gxu.edu.cn.
Qingfeng ChenSchool of Computer, Electronics and Information, Guangxi University, Nanning 530004, China. qingfeng@gxu.edu.cn.
Yanling HuCenter for Genomic and Personalized Medicine, Guangxi Medical University, Nanning 530021, China. ylhupost@163.com.

Funding

National Natural Science Foundation of China 61702122, 61751314Natural Science Foundation of Guangxi 2017GXNSFDA198033
6 · The paper itself

Abstract

Protein phosphorylation is an important chemical modification catalyzed by kinases. It plays important roles in many cellular processes. Predicting kinase⁻substrate interactions is vital to understanding the mechanism of many diseases. Many computational methods have been proposed to identify kinase⁻substrate interactions. However, the prediction accuracy still needs to be improved. Therefore, it is necessary to develop an efficient computational method to predict kinase⁻substrate interactions. In this paper, we propose a novel computational approach, KSIMC, to identify kinase⁻substrate interactions based on matrix completion. Firstly, the kinase similarity and substrate similarity are calculated by aligning sequence of kinase⁻kinase and substrate⁻substrate, respectively. Then, the original association network is adjusted based on the similarities. Finally, the matrix completion is used to predict potential kinase⁻substrate interactions. The experiment results show that our method outperforms other state-of-the-art algorithms in performance. Furthermore, the relevant databases and scientific literature verify the effectiveness of our algorithm for new kinase⁻substrate interaction identification.

Indexed as

Computational BiologyProtein Interaction MappingAlgorithmsBiophysical PhenomenaDatabases, FactualHumansModels, TheoreticalPhosphorylationPhosphotransferasesSequence AlignmentSubstrate SpecificityPhosphotransferasesheterogeneous networkkinase-substrate interactionmatrix completionprotein phosphorylation

Identifiers

PMID30646505
PMCPMC6358935

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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.