Evidence map›Paper›PMID 38457108›Full record

ArticleInterdisciplinary sciences, computational life sciences2024

Identifying Protein Phosphorylation Site-Disease Associations Based on Multi-Similarity Fusion and Negative Sample Selection by Convolutional Neural Network.

Qian Deng, Jing Zhang, Jie Liu, Yuqi Liu, Zong Dai, Xiaoyong Zou, Zhanchao Li

Abstract read
PubMed Publisher
In one paragraph

Article in Interdisciplinary sciences, computational life sciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
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

7 authors.

Qian DengSchool of Chemistry and Chemical Engineering, Guangdong Pharmaceutical University, Guangzhou, 510006, China.
Jing ZhangSchool of Chemistry and Chemical Engineering, Guangdong Pharmaceutical University, Guangzhou, 510006, China.
Jie LiuSchool of Chemistry and Chemical Engineering, Guangdong Pharmaceutical University, Guangzhou, 510006, China.
Yuqi LiuSchool of Chemistry and Chemical Engineering, Guangdong Pharmaceutical University, Guangzhou, 510006, China.
Zong DaiSchool of Biomedical Engineering, Sun Yat-Sen University, Guangzhou, 510275, China.
Xiaoyong ZouSchool of Chemistry, Sun Yat-Sen University, Guangzhou, 510275, China. ceszxy@mail.sysu.edu.cn.
Zhanchao LiSchool of Chemistry and Chemical Engineering, Guangdong Pharmaceutical University, Guangzhou, 510006, China. zhanchao8052@gdpu.edu.cn.ORCID http://orcid.org/0000-0003-1760-5893

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

As one of the most important post-translational modifications (PTMs), protein phosphorylation plays a key role in a variety of biological processes. Many studies have shown that protein phosphorylation is associated with various human diseases. Therefore, identifying protein phosphorylation site-disease associations can help to elucidate the pathogenesis of disease and discover new drug targets. Networks of sequence similarity and Gaussian interaction profile kernel similarity were constructed for phosphorylation sites, as well as networks of disease semantic similarity, disease symptom similarity and Gaussian interaction profile kernel similarity were constructed for diseases. To effectively combine different phosphorylation sites and disease similarity information, random walk with restart algorithm was used to obtain the topology information of the network. Then, the diffusion component analysis method was utilized to obtain the comprehensive phosphorylation site similarity and disease similarity. Meanwhile, the reliable negative samples were screened based on the Euclidean distance method. Finally, a convolutional neural network (CNN) model was constructed to identify potential associations between phosphorylation sites and diseases. Based on tenfold cross-validation, the evaluation indicators were obtained including accuracy of 93.48%, specificity of 96.82%, sensitivity of 90.15%, precision of 96.62%, Matthew's correlation coefficient of 0.8719, area under the receiver operating characteristic curve of 0.9786 and area under the precision-recall curve of 0.9836. Additionally, most of the top 20 predicted disease-related phosphorylation sites (19/20 for Alzheimer's disease; 20/16 for neuroblastoma) were verified by literatures and databases. These results show that the proposed method has an outstanding prediction performance and a high practical value.

Indexed as

AlgorithmsNeural Networks, ComputerAlzheimer DiseaseComputational BiologyHumansPhosphorylationProtein Processing, Post-TranslationalProteinsROC CurveProteinsConvolutional neural networkDiseasesProtein phosphorylation siteThe Euclidean distance

Identifiers

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.