Evidence map›Paper›PMID 37874953›Full record

ArticleBioinformatics (Oxford, England)2023

THPLM: a sequence-based deep learning framework for protein stability changes prediction upon point variations using pretrained protein language model.

Jianting Gong, Lili Jiang, Yongbing Chen, Yixiang Zhang, Xue Li, Zhiqiang Ma, Zhiguo Fu, Fei He, Pingping Sun, Zilin Ren and 1 more

Abstract read
In one paragraph

Article in Bioinformatics (Oxford, England), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed, 1 pooled it
–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

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3 · Its place in the literature

Who cites it

13 citing papers in PubMed, 1 synthesis or guideline pooled it.

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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

11 authors.

Jianting GongSchool of Information Science and Technology, Institution of Computational Biology, Northeast Normal University, Changchun 130117, China.
Lili JiangSchool of Information Science and Technology, Institution of Computational Biology, Northeast Normal University, Changchun 130117, China.
Yongbing ChenSchool of Information Science and Technology, Institution of Computational Biology, Northeast Normal University, Changchun 130117, China.
Yixiang ZhangSchool of Information Science and Technology, Institution of Computational Biology, Northeast Normal University, Changchun 130117, China.
Xue LiChangchun Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Changchun 130122, China.
Zhiqiang MaSchool of Information Science and Technology, Institution of Computational Biology, Northeast Normal University, Changchun 130117, China.
Zhiguo FuSchool of Information Science and Technology, Institution of Computational Biology, Northeast Normal University, Changchun 130117, China.
Fei HeSchool of Information Science and Technology, Institution of Computational Biology, Northeast Normal University, Changchun 130117, China.
Pingping SunSchool of Information Science and Technology, Institution of Computational Biology, Northeast Normal University, Changchun 130117, China.
Zilin RenSchool of Information Science and Technology, Institution of Computational Biology, Northeast Normal University, Changchun 130117, China.ORCID 0000-0002-3621-1024
Mingyao TianChangchun Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Changchun 130122, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

motivationQuantitative determination of protein thermodynamic stability is a critical step in protein and drug design. Reliable prediction of protein stability changes caused by point variations contributes to developing-related fields. Over the past decades, dozens of structure-based and sequence-based methods have been proposed, showing good prediction performance. Despite the impressive progress, it is necessary to explore wild-type and variant protein representations to address the problem of how to represent the protein stability change in view of global sequence. With the development of structure prediction using learning-based methods, protein language models (PLMs) have shown accurate and high-quality predictions of protein structure. Because PLM captures the atomic-level structural information, it can help to understand how single-point variations cause functional changes.

resultsHere, we proposed THPLM, a sequence-based deep learning model for stability change prediction using Meta's ESM-2. With ESM-2 and a simple convolutional neural network, THPLM achieved comparable or even better performance than most methods, including sequence-based and structure-based methods. Furthermore, the experimental results indicate that the PLM's ability to generate representations of sequence can effectively improve the ability of protein function prediction. AVAILABILITY AND IMPLEMENTATION: The source code of THPLM and the testing data can be accessible through the following links: https://github.com/FPPGroup/THPLM.

Indexed as

Deep LearningNeural Networks, ComputerProtein Processing, Post-TranslationalProteinsSoftwareProteins

Identifiers

PMID37874953
PMCPMC10627365

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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.