Evidence map›Paper›PMID 40804041›Full record

ArticleNature communications2025

The topological properties of the protein universe.

Christian D Madsen, Agnese Barbensi, Stephen Y Zhang, Lucy Ham, Alessia David, Douglas E V Pires, Michael P H Stumpf

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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

7 authors.

Christian D MadsenSchool of Mathematics and Statistics, University of Melbourne, Parkville, Australia.ORCID http://orcid.org/0000-0001-8218-7160
Agnese BarbensiSchool of Mathematics and Statistics, University of Melbourne, Parkville, Australia.
Stephen Y ZhangSchool of Mathematics and Statistics, University of Melbourne, Parkville, Australia.
Lucy HamSchool of Mathematics and Statistics, University of Melbourne, Parkville, Australia.
Alessia DavidDepartment of Life Sciences, Imperial College, London, United Kingdom.ORCID http://orcid.org/0000-0001-8687-024X
Douglas E V PiresSchool of Computing and Information Systems, University of Melbourne, Parkville, Australia. douglas.pires@unimelb.edu.au.ORCID http://orcid.org/0000-0002-3004-2119
Michael P H StumpfSchool of Mathematics and Statistics, University of Melbourne, Parkville, Australia. mstumpf@theosysbio.org.ORCID http://orcid.org/0000-0002-3577-1222

Funding

University of Melbourne (Melbourne University) DRMWellcome Trust
6 · The paper itself

Abstract

Deep learning methods have revolutionised our ability to predict protein structures, allowing us a glimpse into the entire protein universe. As a result, our understanding of how protein structure drives function is now lagging behind our ability to determine and predict protein structure. Here, we describe how topology, the branch of mathematics concerned with qualitative properties of spatial structures, provides a lens through which we can identify fundamental organising features across the known protein universe. We identify topological determinants that capture global features of the protein universe, such as domain architecture and binding sites. Additionally, our analysis identifies highly specific properties, so-called topological generators, that can be used to provide deeper insights into protein structure-function and evolutionary relationships. We present a practical methodology for mapping the topology of the known protein universe at scale. We then use our approach to determine structural, functional and disease consequences of mutations. Our approach reveals and helps to explain differences in properties of proteins in mesophiles and thermophiles, and the likely structural and functional consequences of polymorphisms in a protein. For eukaryotes we find striking differences between protein topologies in multi-cellular and single-celled organisms.

Indexed as

ProteinsBinding SitesDeep LearningHumansModels, MolecularMutationProtein ConformationProtein DomainsProteins

Identifiers

PMID40804041
PMCPMC12350623

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.