Evidence map›Paper›PMID 39952928›Full record

ArticleNature communications2025

AlphaFold prediction of structural ensembles of disordered proteins.

Z Faidon Brotzakis, Shengyu Zhang, Mhd Hussein Murtada, Michele Vendruscolo

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 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing 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

52 citing papers in PubMed.

  1. Review
  2. Review
  3. AF-CALVADOS: AlphaFold-guided simulations of multi-domain proteins at the proteome level.Protein science : a publication of the Protein Society · 2026
    Article
  4. AI-Physics-Experiment Trinity for Integrated Protein Dynamics Modeling.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  5. Review
  6. Review
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  16. Review
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  19. Accurate conformational ensembles of intrinsically disordered proteins using reweighting based on NMR chemical shifts.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  20. 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

4 authors.

Z Faidon Brotzakis *Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0001-7024-1430
Shengyu Zhang *Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, UK.
Mhd Hussein Murtada *Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0003-3402-8864
Michele VendruscoloCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, UK. mv245@cam.ac.uk.ORCID http://orcid.org/0000-0002-3616-1610

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Deep learning methods of predicting protein structures have reached an accuracy comparable to that of high-resolution experimental methods. It is thus possible to generate accurate models of the native states of hundreds of millions of proteins. An open question, however, concerns whether these advances can be translated to disordered proteins, which should be represented as structural ensembles because of their heterogeneous and dynamical nature. To address this problem, we introduce the AlphaFold-Metainference method to use AlphaFold-derived distances as structural restraints in molecular dynamics simulations to construct structural ensembles of ordered and disordered proteins. The results obtained using AlphaFold-Metainference illustrate the possibility of making predictions of the conformational properties of disordered proteins using deep learning methods trained on the large structural databases available for folded proteins.

Indexed as

Intrinsically Disordered ProteinsComputational BiologyDatabases, ProteinDeep LearningMolecular Dynamics SimulationProtein ConformationProtein FoldingIntrinsically Disordered Proteins

Identifiers

PMID39952928
PMCPMC11829000

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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.