Evidence map›Paper›PMID 38175759›Full record

ArticleBioinformatics (Oxford, England)2024

RPEMHC: improved prediction of MHC-peptide binding affinity by a deep learning approach based on residue-residue pair encoding.

Xuejiao Wang, Tingfang Wu, Yelu Jiang, Taoning Chen, Deng Pan, Zhi Jin, Jingxin Xie, Lijun Quan, Qiang Lyu

Open access · goldAbstract read
In one paragraph

Article in Bioinformatics (Oxford, England), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
3.3field-weighted citation impact, top 8% of its field
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

13 citing papers in PubMed, 14 citations in OpenAlex.

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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

9 authors at 1 institution in 1 country.

Xuejiao WangSchool of Computer Science and Technology, Soochow University, Suzhou, Jiangsu 215006, China.
Tingfang WuSchool of Computer Science and Technology, Soochow University, Suzhou, Jiangsu 215006, China.ORCID 0000-0001-8137-2436
Yelu JiangSchool of Computer Science and Technology, Soochow University, Suzhou, Jiangsu 215006, China.
Taoning ChenSchool of Computer Science and Technology, Soochow University, Suzhou, Jiangsu 215006, China.
Deng PanSchool of Computer Science and Technology, Soochow University, Suzhou, Jiangsu 215006, China.
Zhi JinSchool of Computer Science and Technology, Soochow University, Suzhou, Jiangsu 215006, China.
Jingxin XieSchool of Computer Science and Technology, Soochow University, Suzhou, Jiangsu 215006, China.
Lijun QuanSchool of Computer Science and Technology, Soochow University, Suzhou, Jiangsu 215006, China.ORCID 0000-0002-8103-555X
Qiang LyuSchool of Computer Science and Technology, Soochow University, Suzhou, Jiangsu 215006, China.
Soochow University · CN

Funding

Collaborative Innovation Center of Novel Software Technology and IndustrializationNational Natural Science Foundation of China 62002251Natural Science Foundation of Jiangsu Province Youth Fund BK20200856Priority Academic Program Development of Jiangsu Higher Education Institutions
6 · The paper itself

Abstract

motivationBinding of peptides to major histocompatibility complex (MHC) molecules plays a crucial role in triggering T cell recognition mechanisms essential for immune response. Accurate prediction of MHC-peptide binding is vital for the development of cancer therapeutic vaccines. While recent deep learning-based methods have achieved significant performance in predicting MHC-peptide binding affinity, most of them separately encode MHC molecules and peptides as inputs, potentially overlooking critical interaction information between the two.

resultsIn this work, we propose RPEMHC, a new deep learning approach based on residue-residue pair encoding to predict the binding affinity between peptides and MHC, which encode an MHC molecule and a peptide as a residue-residue pair map. We evaluate the performance of RPEMHC on various MHC-II-related datasets for MHC-peptide binding prediction, demonstrating that RPEMHC achieves better or comparable performance against other state-of-the-art baselines. Moreover, we further construct experiments on MHC-I-related datasets, and experimental results demonstrate that our method can work on both two MHC classes. These extensive validations have manifested that RPEMHC is an effective tool for studying MHC-peptide interactions and can potentially facilitate the vaccine development. AVAILABILITY: The source code of the method along with trained models is freely available at https://github.com/lennylv/RPEMHC.

Indexed as

Deep LearningHistocompatibility Antigens Class IMajor Histocompatibility ComplexPeptidesProtein BindingHistocompatibility Antigens Class IPeptides

Identifiers

PMID38175759
PMCPMC10796178
OpenAlexW4390578258

What OpenQuestion holds

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LicenceCC BY
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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.