Evidence map›Paper›PMID 39097570›Full record

ArticleNature communications2024

Accurate prediction of protein function using statistics-informed graph networks.

Yaan J Jang, Qi-Qi Qin, Si-Yu Huang, Arun T John Peter, Xue-Ming Ding, Benoît Kornmann

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

  1. Gut Microbial Topology and Metabolic Signatures Associated With Colorectal Neoplasia.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
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  3. Artificial Intelligence Powers Protein Functional Annotation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
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  16. Facilitating crRNA Design by Integrating DNA Interaction Features of CRISPR-Cas12a System.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  17. Article
  18. GOBeacon: An ensemble model for protein function prediction enhanced by contrastive learning.Protein science : a publication of the Protein Society · 2025
    Article
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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

6 authors.

Yaan J Jang *Department of Biochemistry, University of Oxford, Oxford, UK. yaan.jang@gmail.com.ORCID 0000-0002-0228-8672
Qi-Qi Qin *AmoAi Technologies, Oxford, UK.
Si-Yu HuangAmoAi Technologies, Oxford, UK.
Arun T John PeterInstitute of Biochemistry, ETH Zürich, Zürich, Switzerland.
Xue-Ming DingSchool of Optical-Electrical and Computer Engineering, University of Shanghai for Science and Technology, Shanghai, China.
Benoît KornmannDepartment of Biochemistry, University of Oxford, Oxford, UK. benoit.kornmann@bioch.ox.ac.uk.ORCID 0000-0002-6030-8555

Funding

Wellcome Trust (Wellcome) 214291/Z/18/Z
6 · The paper itself

Abstract

Understanding protein function is pivotal in comprehending the intricate mechanisms that underlie many crucial biological activities, with far-reaching implications in the fields of medicine, biotechnology, and drug development. However, more than 200 million proteins remain uncharacterized, and computational efforts heavily rely on protein structural information to predict annotations of varying quality. Here, we present a method that utilizes statistics-informed graph networks to predict protein functions solely from its sequence. Our method inherently characterizes evolutionary signatures, allowing for a quantitative assessment of the significance of residues that carry out specific functions. PhiGnet not only demonstrates superior performance compared to alternative approaches but also narrows the sequence-function gap, even in the absence of structural information. Our findings indicate that applying deep learning to evolutionary data can highlight functional sites at the residue level, providing valuable support for interpreting both existing properties and new functionalities of proteins in research and biomedicine.

Indexed as

Computational BiologyProteinsAlgorithmsDatabases, ProteinDeep LearningHumansProteins

Identifiers

PMID39097570
PMCPMC11297950

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.