Evidence map›Paper›PMID 42024027›Full record

ArticleActa crystallographica. Section D, Structural biology2026

Alphafuser: a parsimonious approach to predicting higher-order protein complexes.

Audrey Guillotin, Stephanie Hutin, Lorelei Masselot-Joubert, Kamel Hammani, Chloe Zubieta, Max Nanao

Abstract read
In one paragraph

Article in Acta crystallographica. Section D, Structural biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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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

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3 · Its place in the literature

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4 · The record

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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

6 authors.

Audrey GuillotinLaboratoire de Physiologie Cellulaire et Végétale, Université Grenoble-Alpes, CNRS, CEA, INRAE, IRIG-DBSCI, 17 Rue des Martyrs, 38000 Grenoble, France.
Stephanie HutinLaboratoire de Physiologie Cellulaire et Végétale, Université Grenoble-Alpes, CNRS, CEA, INRAE, IRIG-DBSCI, 17 Rue des Martyrs, 38000 Grenoble, France.ORCID 0000-0002-2168-5841
Lorelei Masselot-JoubertLaboratoire de Physiologie Cellulaire et Végétale, Université Grenoble-Alpes, CNRS, CEA, INRAE, IRIG-DBSCI, 17 Rue des Martyrs, 38000 Grenoble, France.
Kamel HammaniInstitut de Biologie Moléculaire des Plantes, Centre National de la Recherche Scientifique (CNRS), Université de Strasbourg, 12 Rue du Général Zimmer, 67084 Strasbourg, France.
Chloe ZubietaLaboratoire de Physiologie Cellulaire et Végétale, Université Grenoble-Alpes, CNRS, CEA, INRAE, IRIG-DBSCI, 17 Rue des Martyrs, 38000 Grenoble, France.ORCID 0000-0003-4558-9333
Max NanaoStructural Biology Group, European Synchrotron Radiation Facility, 71 Avenue des Martyrs, 38000 Grenoble, France.

Funding

Agence Nationale de la Recherche ANR-23-CE20-0019
6 · The paper itself

Abstract

Many biological processes rely on the activity of multiple proteins acting in concert as part of higher-order oligomeric complexes. However, the majority of structural studies have routinely simplified these systems to examine only one or a few protein partners of a multi-component system. Artificial intelligence (AI) methods implemented in AlphaFold, RoseTTAFold, ESMFold and others have revolutionized our ability to not only predict the fold of individual proteins, but also to predict that of complex assemblies. A major bottleneck in exploiting AI-based protein fold prediction for multiprotein complexes, however, is identifying likely interacting partners from a given interactome. Here, we present a protein complex prediction pipeline based on AlphaFold, called Alphafuser, that combines experimental interaction data with systematic querying of possible combinations of protein partners in a computationally parsimonious manner. This versatile protein complex prediction pipeline creates a queue of all potential complexes, up to a user defined number of partners. Because a complete search of all permutations is not typically practical, we implemented a simple dead-end trimming algorithm from the dimer step onwards based on the interface probability template modeling (ipTM) score to remove low-probability subcomplexes from the queue of higher-order complexes. Experimentally structurally characterized multiprotein complexes in the Protein Data Bank, PP2A-B56γ1 holoenzyme-PME-1 complex, the human γ-secretase complex, the TFIIIC complex and the TRAPP I complex, were used to obtain a general ipTM cutoff parameter for the pipeline and to confirm that complexes without extensive direct contacts between all subunits could be identified. We applied Alphafuser to two test cases starting from yeast two-hybrid and co-immunoprecipitation/mass spectrometry (co-IP/MS) interaction data. These predictions were tested experimentally using pull-down assays, confirming direct interactions of the proteins identified computationally by the Alphafuser pipeline.

Indexed as

Multiprotein ComplexesProteinsSoftwareAlgorithmsArtificial IntelligenceHumansModels, MolecularPrediction AlgorithmsProtein ConformationProtein FoldingMultiprotein ComplexesProteinsAlphaFoldcomplexesinteractomemultimers

Identifiers

PMID42024027
PMCPMC13133988

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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.