Evidence map›Paper›PMID 41168475›Full record

ArticleCommunications chemistry2025

Modeling cryo-EM structures in alternative states with AlphaFold2-based models and density-guided simulations.

Tatiana Shugaeva, Rebecca J Howard, Nandan Haloi, Erik Lindahl

Abstract read
In one paragraph

Article in Communications chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. AI-Physics-Experiment Trinity for Integrated Protein Dynamics Modeling.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  5. Article
  6. Review
  7. Lanthanide Nanotheranostics in Radiotherapy.International journal of molecular sciences · 2025
    Review
  8. Generation of protein dynamics by machine learning.Current opinion in structural biology · 2025
    Review
  9. 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.

Tatiana ShugaevaDepartment of Applied Physics, Science for Life Laboratory, KTH Royal Institute of Technology, Tomtebodavägen 23, Solna, SE-17165, Sweden.ORCID http://orcid.org/0009-0001-8147-0762
Rebecca J HowardDepartment of Applied Physics, Science for Life Laboratory, KTH Royal Institute of Technology, Tomtebodavägen 23, Solna, SE-17165, Sweden.ORCID http://orcid.org/0000-0003-2049-3378
Nandan HaloiDepartment of Applied Physics, Science for Life Laboratory, KTH Royal Institute of Technology, Tomtebodavägen 23, Solna, SE-17165, Sweden. nandan.haloi@scilifelab.se.ORCID http://orcid.org/0000-0003-3542-333X
Erik LindahlDepartment of Applied Physics, Science for Life Laboratory, KTH Royal Institute of Technology, Tomtebodavägen 23, Solna, SE-17165, Sweden. erik.lindahl@scilifelab.se.ORCID http://orcid.org/0000-0002-2734-2794

Funding

EC | EU Framework Programme for Research and Innovation H2020 | H2020 Priority Excellent Science | H2020 Marie Skłodowska-Curie Actions (H2020 Excellent Science - Marie Skłodowska-Curie Actions) 101107036
6 · The paper itself

Abstract

Modeling atomic coordinates into a target cryo-electron microscopy map is a crucial step in structure determination. Despite recent advances, proteins with multiple functional states remain a challenge - particularly when suitable molecular templates are unavailable for certain states, and the map resolution is not high enough to build de novo models. This is a common scenario, for example, among pharmacologically relevant membrane-bound receptors and transporters. Here, we introduce a refinement approach in which (i) several initial models are generated by stochastic subsampling of the multiple sequence alignment (MSA) space in AlphaFold2, (ii) the resulting models are subjected to structure-based k-means clustering, iii) density-guided molecular dynamics simulations are performed from the cluster representatives, and (iv) a final model is selected on the basis of both map fit and model quality. This results in improved fitting accuracy compared to single starting point scenarios for three membrane proteins (the calcitonin receptor-like receptor, L-type amino acid transporter and alanine-serine-cysteine transporter) which undergo substantial conformational transitions between functional states. Our results indicate that ensemble construction using generative AI combined with simulation-based refinement facilitates building of alternative states in several families of membrane proteins.

Identifiers

PMID41168475
PMCPMC12575730

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Registered trials

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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.