Evidence map›Paper›PMID 39436947›Full record

ArticlePLoS computational biology2024

PreMLS: The undersampling technique based on ClusterCentroids to predict multiple lysine sites.

Yun Zuo, Xingze Fang, Jiayong Wan, Wenying He, Xiangrong Liu, Xiangxiang Zeng, Zhaohong Deng

Abstract read
In one paragraph

Article in PLoS computational biology, 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. CLASPP: A unified model for predicting post-translational modifications.bioRxiv : the preprint server for biology · 2026
    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.

Yun ZuoSchool of Artificial Intelligence and Computer Science, Jiangnan University, Wuxi, China.ORCID 0009-0003-4021-3836
Xingze FangSchool of Artificial Intelligence and Computer Science, Jiangnan University, Wuxi, China.
Jiayong WanSchool of Artificial Intelligence and Computer Science, Jiangnan University, Wuxi, China.
Wenying HeSchool of Artificial Intelligence, Hebei University of Technology, Tianjin, China.
Xiangrong LiuDepartment of Computer Science and Technology, National Institute for Data Science in Health and Medicine, Xiamen Key Laboratory of Intelligent Storage and Computing, Xiamen University, Xiamen, China.
Xiangxiang ZengSchool of Information Science and Engineering, Hunan University, Changsha, China.
Zhaohong DengSchool of Artificial Intelligence and Computer Science, Jiangnan University, Wuxi, China.

Funding

Fundamental Research Funds for the Central Universities JUSRP124014National Natural Science Foundation of China 62302198Natural Science Foundation of Jiangsu Province of China BK20231035
6 · The paper itself

Abstract

The translated protein undergoes a specific modification process, which involves the formation of covalent bonds on lysine residues and the attachment of small chemical moieties. The protein's fundamental physicochemical properties undergo a significant alteration. The change significantly alters the proteins' 3D structure and activity, enabling them to modulate key physiological processes. The modulation encompasses inhibiting cancer cell growth, delaying ovarian aging, regulating metabolic diseases, and ameliorating depression. Consequently, the identification and comprehension of post-translational lysine modifications hold substantial value in the realms of biological research and drug development. Post-translational modifications (PTMs) at lysine (K) sites are among the most common protein modifications. However, research on K-PTMs has been largely centered on identifying individual modification types, with a relative scarcity of balanced data analysis techniques. In this study, a classification system is developed for the prediction of concurrent multiple modifications at a single lysine residue. Initially, a well-established multi-label position-specific triad amino acid propensity algorithm is utilized for feature encoding. Subsequently, PreMLS: a novel ClusterCentroids undersampling algorithm based on MiniBatchKmeans was introduced to eliminate redundant or similar major class samples, thereby mitigating the issue of class imbalance. A convolutional neural network architecture was specifically constructed for the analysis of biological sequences to predict multiple lysine modification sites. The model, evaluated through five-fold cross-validation and independent testing, was found to significantly outperform existing models such as iMul-kSite and predML-Site. The results presented here aid in prioritizing potential lysine modification sites, facilitating subsequent biological assays and advancing pharmaceutical research. To enhance accessibility, an open-access predictive script has been crafted for the multi-label predictive model developed in this study.

Indexed as

AlgorithmsComputational BiologyLysineProtein Processing, Post-TranslationalDatabases, ProteinHumansNeural Networks, ComputerProteinsLysineProteins

Identifiers

PMID39436947
PMCPMC11530015

What OpenQuestion holds

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Registered trials

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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.