Evidence map›Paper›PMID 40233800›Full record

ReviewJournal of the Royal Society, Interface2025

Emerging frontiers in protein structure prediction following the AlphaFold revolution.

Martin Luke Rennie, Michael R Oliver

Abstract readReview
In one paragraph

Review in Journal of the Royal Society, Interface, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Biophysical and enzymatic comparison ofbioRxiv : the preprint server for biology · 2026
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. 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

2 authors.

Martin Luke RennieSchool of Molecular Biosciences, University of Glasgow, Glasgow, UK.ORCID 0000-0002-0799-3450
Michael R OliverMRC-University of Glasgow Centre for Virus Research, Glasgow, UK.

Funding

Medical Research CouncilRoyal Society
6 · The paper itself

Abstract

Models of protein structures enable molecular understanding of biological processes. Current protein structure prediction tools lie at the interface of biology, chemistry and computer science. Millions of protein structure models have been generated in a very short space of time through a revolution in protein structure prediction driven by deep learning, led by AlphaFold. This has provided a wealth of new structural information. Interpreting these predictions is critical to determining where and when this information is useful. But proteins are not static nor do they act alone, and structures of proteins interacting with other proteins and other biomolecules are critical to a complete understanding of their biological function at the molecular level. This review focuses on the application of state-of-the-art protein structure prediction to these advanced applications. We also suggest a set of guidelines for reporting AlphaFold predictions.

Indexed as

Deep LearningModels, MolecularProtein FoldingProteinsComputational BiologyProtein ConformationProteinsAlphaFoldbiomolecular interactionsco-evolutionconformational changesprotein–protein interactionsprotein structure prediction

Identifiers

PMID40233800
PMCPMC11999738

What OpenQuestion holds

Textmetadata
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.