Evidence map›Paper›PMID 40332289›Full record

ReviewInternational journal of molecular sciences2025

AlphaFold3: An Overview of Applications and Performance Insights.

Marios G Krokidis, Dimitrios E Koumadorakis, Konstantinos Lazaros, Ouliana Ivantsik, Themis P Exarchos, Aristidis G Vrahatis, Sotiris Kotsiantis, Panagiotis Vlamos

Abstract readReview
In one paragraph

Review in International journal of molecular sciences, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing 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

68 citing papers in PubMed.

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8 more citing papers are in PubMed but not listed here.

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

8 authors.

Marios G KrokidisBioinformatics and Human Electrophysiology Laboratory, Department of Informatics, Ionian University, 49100 Corfu, Greece.
Dimitrios E KoumadorakisBioinformatics and Human Electrophysiology Laboratory, Department of Informatics, Ionian University, 49100 Corfu, Greece.
Konstantinos LazarosBioinformatics and Human Electrophysiology Laboratory, Department of Informatics, Ionian University, 49100 Corfu, Greece.
Ouliana IvantsikBioinformatics and Human Electrophysiology Laboratory, Department of Informatics, Ionian University, 49100 Corfu, Greece.
Themis P ExarchosBioinformatics and Human Electrophysiology Laboratory, Department of Informatics, Ionian University, 49100 Corfu, Greece.
Aristidis G VrahatisBioinformatics and Human Electrophysiology Laboratory, Department of Informatics, Ionian University, 49100 Corfu, Greece.ORCID 0000-0003-1892-0000
Sotiris KotsiantisDepartment of Mathematics, University of Patras, 26504 Rio, Greece.ORCID 0000-0002-2247-3082
Panagiotis VlamosBioinformatics and Human Electrophysiology Laboratory, Department of Informatics, Ionian University, 49100 Corfu, Greece.ORCID 0000-0003-0053-7847

Funding

This work was partially supported by the European Union-Next Generation EU, Greece 2.0 Na-tional Recovery and Resilience Plan Flagship program TAEDR-0535850. TAEDR-0535850
6 · The paper itself

Abstract

AlphaFold3, the latest release of AlphaFold developed by Google DeepMind and Isomorphic Labs, was designed to predict protein structures with remarkable accuracy. AlphaFold3 enhances our ability to model not only single protein structures but also complex biomolecular interactions, including protein-protein interactions, protein-ligand docking, and protein-nucleic acid complexes. Herein, we provide a detailed examination of AlphaFold3's capabilities, emphasizing its applications across diverse biological fields and its effectiveness in complex biological systems. The strengths of the new AI model are also highlighted, including its ability to predict protein structures in dynamic systems, multi-chain assemblies, and complicated biomolecular complexes that were previously challenging to depict. We explore its role in advancing drug discovery, epitope prediction, and the study of disease-related mutations. Despite its significant improvements, the present review also addresses ongoing obstacles, particularly in modeling disordered regions, alternative protein folds, and multi-state conformations. The limitations and future directions of AlphaFold3 are discussed as well, with an emphasis on its potential integration with experimental techniques to further refine predictions. Lastly, the work underscores the transformative contribution of the new model to computational biology, providing new insights into molecular interactions and revolutionizing the fields of accelerated drug design and genomic research.

Indexed as

Computational BiologyProteinsSoftwareHumansModels, MolecularMolecular Docking SimulationProtein BindingProtein ConformationProtein FoldingProteinsAlphaFold3deep learningprediction accuracyprotein–ligand interactionsprotein modelingstructural biology

Identifiers

PMID40332289
PMCPMC12027460

What OpenQuestion holds

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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.