Evidence map›Paper›PMID 40016259›Full record

ArticleNature communications2025

Rapid and accurate prediction of protein homo-oligomer symmetry using Seq2Symm.

Meghana Kshirsagar, Artur Meller, Ian R Humphreys, Samuel Sledzieski, Yixi Xu, Rahul Dodhia, Eric Horvitz, Bonnie Berger, Gregory R Bowman, Juan Lavista Ferres and 2 more

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Stoic: fast and accurate protein stoichiometry prediction.Bioinformatics (Oxford, England) · 2026
    Article
  2. Review
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  11. mamp-ml: A deep learning approach to epitope immunogenicity in plants.bioRxiv : the preprint server for biology · 2025
    Article
  12. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors.

Meghana KshirsagarAI for Good Research Lab, Microsoft Corporation, Redmond, WA, USA. meghana.kshirsagar@microsoft.com.ORCID http://orcid.org/0000-0002-4673-614X
Artur Meller *Department of Biochemistry and Molecular Biophysics, Washington University in St. Louis, St. Louis, MO, USA.ORCID http://orcid.org/0000-0002-5504-2684
Ian R Humphreys *Department of Biochemistry, University of Washington, Seattle, WA, USA.
Samuel SledzieskiAI for Good Research Lab, Microsoft Corporation, Redmond, WA, USA.ORCID http://orcid.org/0000-0002-0170-3029
Yixi XuAI for Good Research Lab, Microsoft Corporation, Redmond, WA, USA.
Rahul DodhiaAI for Good Research Lab, Microsoft Corporation, Redmond, WA, USA.
Eric HorvitzMicrosoft Corp, Redmond, WA, USA.
Bonnie BergerComputer Science and Artificial Intelligence Laboratory, Massachusetts Institute of Technology, Cambridge, MA, USA.
Gregory R BowmanDepartment of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, PA, USA.ORCID http://orcid.org/0000-0002-2083-4892
Juan Lavista FerresAI for Good Research Lab, Microsoft Corporation, Redmond, WA, USA.ORCID http://orcid.org/0000-0002-9654-3178
David BakerDepartment of Biochemistry, University of Washington, Seattle, WA, USA.ORCID http://orcid.org/0000-0001-7896-6217
Minkyung BaekDepartment of Biological Sciences, Seoul National University, Seoul, South Korea. minkbaek@snu.ac.kr.ORCID http://orcid.org/0000-0003-3414-9404

Funding

Manifold representations and active learning for 21 st century biologyR35GM141861 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI BERGER, BONNIE · 2021 to 2025
$1.9M
Understanding and controlling protein energy landscapes by combining simulations and experimentsR35GM152085 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI Gregory Bowman · 2024 to 2026
$1.2M
Modeling Hidden Myosin Structural States to Predict Drug Specificity and Disease PhenotypesF30HL162431 · NHLBI · WASHINGTON UNIVERSITY · PI MELLER, ARTUR · 2022 to 2025
$141k
NHLBI NIH HHS F30 HL162431NIGMS NIH HHS R35 GM141861NIGMS NIH HHS R35 GM152085
6 · The paper itself

Abstract

The majority of proteins must form higher-order assemblies to perform their biological functions, yet few machine learning models can accurately and rapidly predict the symmetry of assemblies involving multiple copies of the same protein chain. Here, we address this gap by finetuning several classes of protein foundation models, to predict homo-oligomer symmetry. Our best model named Seq2Symm, which utilizes ESM2, outperforms existing template-based and deep learning methods achieving an average AUC-PR of 0.47, 0.44 and 0.49 across homo-oligomer symmetries on three held-out test sets compared to 0.24, 0.24 and 0.25 with template-based search. Seq2Symm uses a single sequence as input and can predict at the rate of ~80,000 proteins/hour. We apply this method to 5 proteomes and ~3.5 million unlabeled protein sequences, showing its promise to be used in conjunction with downstream computationally intensive all-atom structure generation methods such as RoseTTAFold2 and AlphaFold2-multimer. Code, datasets, model are available at: https://github.com/microsoft/seq2symm .

Indexed as

Computational BiologyProtein MultimerizationProteinsAlgorithmsDeep LearningMachine LearningModels, MolecularProtein ConformationProteomeSoftwareProteinsProteome

Identifiers

PMID40016259
PMCPMC11868566

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.