Evidence map›Paper›PMID 41259418›Full record

ArticleBriefings in bioinformatics2025

PCBert-Kla: an efficient prediction method for lysine lactylation sites based on ProtBert and fusion of physicochemical features.

Hong-Qi Zhang, Yi-Xuan Qi, Huma Fida, Hao-Jiang Zhang, Muhammad Arif, Pei-Yu Zhao, Tanvir Alam, Ye-Chen Qi, Xiao-Long Yu, Ke-Jun Deng

Abstract read
In one paragraph

Article in Briefings in bioinformatics, 2025. 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
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  3. Review
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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

10 authors.

Hong-Qi ZhangSchool of Life Science and Technology and Center for Informational Biology, University of Electronic Science and Technology of China, No. 2006 Xiyuan Avenue, West Hi-Tech Zone, Chengdu 610054, China.ORCID 0009-0000-5214-0855
Yi-Xuan QiSchool of Life Science and Technology and Center for Informational Biology, University of Electronic Science and Technology of China, No. 2006 Xiyuan Avenue, West Hi-Tech Zone, Chengdu 610054, China.
Huma FidaSchool of Life Science and Technology and Center for Informational Biology, University of Electronic Science and Technology of China, No. 2006 Xiyuan Avenue, West Hi-Tech Zone, Chengdu 610054, China.
Hao-Jiang ZhangSchool of Life Science and Technology and Center for Informational Biology, University of Electronic Science and Technology of China, No. 2006 Xiyuan Avenue, West Hi-Tech Zone, Chengdu 610054, China.
Muhammad ArifCollege of Science and Engineering, Hamad Bin Khalifa University, Education City, Doha 34110, Qatar.
Pei-Yu ZhaoSchool of Computer Science and Technology, Hainan University, No. 58 Renmin Avenue, Meilan District, Haikou 570228, China.
Tanvir AlamCollege of Science and Engineering, Hamad Bin Khalifa University, Education City, Doha 34110, Qatar.ORCID 0000-0001-7033-3693
Ye-Chen QiSchool of Life Science and Technology and Center for Informational Biology, University of Electronic Science and Technology of China, No. 2006 Xiyuan Avenue, West Hi-Tech Zone, Chengdu 610054, China.
Xiao-Long YuSchool of Materials Science and Engineering, Hainan University, No. 58 Renmin Avenue, Meilan District, Haikou 570228, China.
Ke-Jun DengSchool of Life Science and Technology and Center for Informational Biology, University of Electronic Science and Technology of China, No. 2006 Xiyuan Avenue, West Hi-Tech Zone, Chengdu 610054, China.ORCID 0000-0003-0411-549X

Funding

General Project of Hainan Provincial Natural Science Foundation 325MS031National Natural Science Foundation of China 62261017National Natural Science Foundation of China 62372090National Natural Science Foundation of China 82130112
6 · The paper itself

Abstract

Protein post-translational modifications (PTMs) play a critical role in regulating protein functionality and structural diversity. Among them, lysine lactylation (Kla), a newly identified PTM, is involved in energy metabolism, cellular reprogramming, and the progression of various diseases. In this study, we propose PCBert-Kla, a feature-fusion deep learning model based on ProtBert. This model leverages ProtBert to extract deep features from protein sequences, effectively capturing global and local contextual information. It integrated various physicochemical properties, including molecular weight, isoelectric point, amino acid composition, secondary structure content, hydrophobicity, and net charge. An attention mechanism in the fully connected layers enabled the model to select features automatically. PCBert-Kla exhibited exceptional accuracy and reliability in Kla site identification and demonstrated excellent generalization capability to outperform the existing models. In addition, we further enhanced the interpretability of the PCBert-Kla model by incorporating average attention maps. This model provided powerful tools for studying the functions of Kla and elucidating the mechanisms of related diseases, which can advance biomedical research and drug development. We also developed a free web service, available at http://pcbert-kla.lin-group.cn/, to provide users with easy access and usage.

Indexed as

Computational BiologyDeep LearningLysineProtein Processing, Post-TranslationalProteinsSoftwareHumansHydrophobic and Hydrophilic InteractionsLysineProteinsdeep learningfeature fusionlysine lactylationpost-translational modificationsProtBert

Identifiers

PMID41259418
PMCPMC12629241

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LicenceCC BY
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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.