Evidence map›Paper›PMID 40520120›Full record

ArticleCurrent research in structural biology2025

Evaluation of the structural models of the human reference proteome: AlphaFold2 versus ESMFold.

Matteo Manfredi, Castrense Savojardo, Pier Luigi Martelli, Rita Casadio

Abstract read
In one paragraph

Article in Current research in structural biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

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3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

4 authors.

Matteo ManfrediBiocomputing Group, Dept. of Pharmacy and Biotechnology, University of Bologna, Italy.
Castrense SavojardoBiocomputing Group, Dept. of Pharmacy and Biotechnology, University of Bologna, Italy.
Pier Luigi MartelliBiocomputing Group, Dept. of Pharmacy and Biotechnology, University of Bologna, Italy.
Rita CasadioBiocomputing Group, AlmaClimate Interdepartmental Center, University of Bologna, Italy.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The human reference proteome is routinely modelled with predictive tools such as AlphaFold2. We recently released a database in which, for each human protein, the AlphaFold2 model is paired with its ESMFold counterpart. The two predictive methods take advantage of different procedures and it is interesting to compare them in relation to their quality, particularly when an experimental protein structure is not available. Here, we select three state-of-the-art quality assessment methods and we adopt them to compare 42,942 pairs of models. This procedure helps to find the most reliable models for human proteins, particularly for the set of proteins for which structure prediction methods give dissimilar results. We obtain that when predicted structures are similar, AlphaFold2 models consistently receive higher scores than the ESMFold counterparts. When predicted structures differ, the ESMFold model is the best choice for 49 % of the proteins according to a consensus of the three QA tools.

Indexed as

AI computed structural modelsAlphaFold2ESMFoldHuman protein structure predictionModel secondary structureModel solvent accessibilityQATENStructural model quality assessment

Identifiers

PMID40520120
PMCPMC12166363

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.