Evidence map›Paper›PMID 40785361›Full record

ArticleJournal of chemical information and modeling2025

Structure Prediction of Alternate Frame Folding Systems with AlphaFold3.

Gonzalo Jiménez-Osés, Francesca Peccati

Abstract read
In one paragraph

Article in Journal of chemical information and modeling, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. 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

2 authors.

Gonzalo Jiménez-OsésCenter for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA) Bizkaia Technology Park, Derio 48160, Spain.ORCID 0000-0003-0105-4337
Francesca PeccatiCenter for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA) Bizkaia Technology Park, Derio 48160, Spain.ORCID 0000-0002-7813-8216

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

AlphaFold has proven to be a valuable tool for predicting protein structures with unprecedented speed and accuracy. Extensive research from multiple groups has demonstrated that manipulating the multiple sequence alignment used for structure prediction can enhance AlphaFold2's ability to explore protein conformational landscapes, yielding reliable models of proteins capable of switching between alternative conformations. The release of the thoroughly reengineered AlphaFold3, which promises even greater prediction accuracy and efficiency, raises the question of whether such alternative conformational states can be modeled-either natively or by tuning the multiple sequence alignment used for prediction. In this work, we use a family of green fluorescent proteins engineered through alternate frame folding to assess AlphaFold3's prediction accuracy and uncover an unexpected role of disordered regions in driving the conformational preferences of the models.

Indexed as

Computational BiologyProtein FoldingGreen Fluorescent ProteinsModels, MolecularProtein ConformationGreen Fluorescent Proteins

Identifiers

PMID40785361
PMCPMC12344692

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.