Evidence map›Paper›PMID 37771850›Full record

ArticleResearch (Washington, D.C.)2023

A Transformer-Based Ensemble Framework for the Prediction of Protein-Protein Interaction Sites.

Minjie Mou, Ziqi Pan, Zhimeng Zhou, Lingyan Zheng, Hanyu Zhang, Shuiyang Shi, Fengcheng Li, Xiuna Sun, Feng Zhu

Abstract read
In one paragraph

Article in Research (Washington, D.C.), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
45citing 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

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

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

  1. Pooled it
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  7. Accurate Identification of Protein Binding Sites for All Drug Modalities Using ALLSites.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  8. Review
  9. Article
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  11. Predicting Protein-Protein Interactions from Machine-Learned Representations.Advances in experimental medicine and biology · 2026
    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

9 authors.

Minjie MouCollege of Pharmaceutical Sciences, The Second Affiliated Hospital, Zhejiang UniversitySchool of Medicine, National Key Laboratory of Advanced Drug Delivery and Release Systems, Zhejiang University, Hangzhou 310058, China.ORCID https://orcid.org/0000-0001-7619-2975
Ziqi PanCollege of Pharmaceutical Sciences, The Second Affiliated Hospital, Zhejiang UniversitySchool of Medicine, National Key Laboratory of Advanced Drug Delivery and Release Systems, Zhejiang University, Hangzhou 310058, China.ORCID https://orcid.org/0000-0002-3883-4161
Zhimeng ZhouCollege of Pharmaceutical Sciences, The Second Affiliated Hospital, Zhejiang UniversitySchool of Medicine, National Key Laboratory of Advanced Drug Delivery and Release Systems, Zhejiang University, Hangzhou 310058, China.ORCID https://orcid.org/0009-0007-7980-7577
Lingyan ZhengCollege of Pharmaceutical Sciences, The Second Affiliated Hospital, Zhejiang UniversitySchool of Medicine, National Key Laboratory of Advanced Drug Delivery and Release Systems, Zhejiang University, Hangzhou 310058, China.ORCID https://orcid.org/0000-0001-7533-2649
Hanyu ZhangCollege of Pharmaceutical Sciences, The Second Affiliated Hospital, Zhejiang UniversitySchool of Medicine, National Key Laboratory of Advanced Drug Delivery and Release Systems, Zhejiang University, Hangzhou 310058, China.ORCID https://orcid.org/0000-0002-4728-7702
Shuiyang ShiCollege of Pharmaceutical Sciences, The Second Affiliated Hospital, Zhejiang UniversitySchool of Medicine, National Key Laboratory of Advanced Drug Delivery and Release Systems, Zhejiang University, Hangzhou 310058, China.ORCID https://orcid.org/0009-0007-9638-5089
Fengcheng LiCollege of Pharmaceutical Sciences, The Second Affiliated Hospital, Zhejiang UniversitySchool of Medicine, National Key Laboratory of Advanced Drug Delivery and Release Systems, Zhejiang University, Hangzhou 310058, China.ORCID https://orcid.org/0000-0002-1846-639X
Xiuna SunCollege of Pharmaceutical Sciences, The Second Affiliated Hospital, Zhejiang UniversitySchool of Medicine, National Key Laboratory of Advanced Drug Delivery and Release Systems, Zhejiang University, Hangzhou 310058, China.ORCID https://orcid.org/0000-0001-7991-5825
Feng ZhuCollege of Pharmaceutical Sciences, The Second Affiliated Hospital, Zhejiang UniversitySchool of Medicine, National Key Laboratory of Advanced Drug Delivery and Release Systems, Zhejiang University, Hangzhou 310058, China.ORCID https://orcid.org/0000-0001-8069-0053

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The identification of protein-protein interaction (PPI) sites is essential in the research of protein function and the discovery of new drugs. So far, a variety of computational tools based on machine learning have been developed to accelerate the identification of PPI sites. However, existing methods suffer from the low predictive accuracy or the limited scope of application. Specifically, some methods learned only global or local sequential features, leading to low predictive accuracy, while others achieved improved performance by extracting residue interactions from structures but were limited in their application scope for the serious dependence on precise structure information. There is an urgent need to develop a method that integrates comprehensive information to realize proteome-wide accurate profiling of PPI sites. Herein, a novel ensemble framework for PPI sites prediction, EnsemPPIS, was therefore proposed based on transformer and gated convolutional networks. EnsemPPIS can effectively capture not only global and local patterns but also residue interactions. Specifically, EnsemPPIS was unique in (a) extracting residue interactions from protein sequences with transformer and (b) further integrating global and local sequential features with the ensemble learning strategy. Compared with various existing methods, EnsemPPIS exhibited either superior performance or broader applicability on multiple PPI sites prediction tasks. Moreover, pattern analysis based on the interpretability of EnsemPPIS demonstrated that EnsemPPIS was fully capable of learning residue interactions within the local structure of PPI sites using only sequence information. The web server of EnsemPPIS is freely available at http://idrblab.org/ensemppis.

Identifiers

PMID37771850
PMCPMC10528219

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.