Evidence map›Paper›PMID 38990514›Full record

ArticleBriefings in bioinformatics2024

GAPS: a geometric attention-based network for peptide binding site identification by the transfer learning approach.

Cheng Zhu, Chengyun Zhang, Tianfeng Shang, Chenhao Zhang, Silong Zhai, Lujing Cao, Zhenyu Xu, Zhihao Su, Ying Song, An Su and 2 more

Abstract read
In one paragraph

Article in Briefings in bioinformatics, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
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

12 authors.

Cheng ZhuCollege of Pharmaceutical Sciences, Zhejiang University of Technology, Chaowang Road, Gongshu District, Hangzhou 310014, China.ORCID 0009-0006-5155-1605
Chengyun ZhangAI Department, Shanghai Highslab Therapeutics. Inc, Zhangheng Road, Pudong New Area, Shanghai 201203, China.
Tianfeng ShangAI Department, Shanghai Highslab Therapeutics. Inc, Zhangheng Road, Pudong New Area, Shanghai 201203, China.
Chenhao ZhangCollege of Pharmaceutical Sciences, Zhejiang University of Technology, Chaowang Road, Gongshu District, Hangzhou 310014, China.ORCID 0009-0009-2816-1416
Silong ZhaiCollege of Pharmaceutical Sciences, Zhejiang University of Technology, Chaowang Road, Gongshu District, Hangzhou 310014, China.
Lujing CaoCollege of Pharmaceutical Sciences, Zhejiang University of Technology, Chaowang Road, Gongshu District, Hangzhou 310014, China.
Zhenyu XuAI Department, Shanghai Highslab Therapeutics. Inc, Zhangheng Road, Pudong New Area, Shanghai 201203, China.
Zhihao SuCollege of Pharmaceutical Sciences, Zhejiang University of Technology, Chaowang Road, Gongshu District, Hangzhou 310014, China.
Ying SongCollege of Pharmaceutical Sciences, Zhejiang University of Technology, Chaowang Road, Gongshu District, Hangzhou 310014, China.
An SuCollege of Chemical Engineering, Zhejiang University of Technology, Chaowang Road, Gongshu District, Hangzhou 310014, China.
Chengxi LiCollege of Chemical and Biological Engineering, Zhejiang University, Yuhangtang Road, Xihu District, Hangzhou 310027, China.
Hongliang DuanFaculty of Applied Sciences, Macao Polytechnic University, R. de Luís Gonzaga Gomes, Macao 999078, China.

Funding

National Natural Science Foundation of China 82174038Natural Science Foundation of Zhejiang Province LD22H300004
6 · The paper itself

Abstract

Protein-peptide interactions (PPepIs) are vital to understanding cellular functions, which can facilitate the design of novel drugs. As an essential component in forming a PPepI, protein-peptide binding sites are the basis for understanding the mechanisms involved in PPepIs. Therefore, accurately identifying protein-peptide binding sites becomes a critical task. The traditional experimental methods for researching these binding sites are labor-intensive and time-consuming, and some computational tools have been invented to supplement it. However, these computational tools have limitations in generality or accuracy due to the need for ligand information, complex feature construction, or their reliance on modeling based on amino acid residues. To deal with the drawbacks of these computational algorithms, we describe a geometric attention-based network for peptide binding site identification (GAPS) in this work. The proposed model utilizes geometric feature engineering to construct atom representations and incorporates multiple attention mechanisms to update relevant biological features. In addition, the transfer learning strategy is implemented for leveraging the protein-protein binding sites information to enhance the protein-peptide binding sites recognition capability, taking into account the common structure and biological bias between proteins and peptides. Consequently, GAPS demonstrates the state-of-the-art performance and excellent robustness in this task. Moreover, our model exhibits exceptional performance across several extended experiments including predicting the apo protein-peptide, protein-cyclic peptide and the AlphaFold-predicted protein-peptide binding sites. These results confirm that the GAPS model is a powerful, versatile, stable method suitable for diverse binding site predictions.

Indexed as

PeptidesAlgorithmsBinding SitesComputational BiologyMachine LearningProtein BindingProteinsPeptidesProteinsattention mechanismbinding sitesgeometric deep learningtransfer learning

Identifiers

PMID38990514
PMCPMC11238429

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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.