Evidence map›Paper›PMID 41628239›Full record

ArticlePloS one2026

Large-scale multi-omic biosequence transformers for modeling protein-nucleic acid interactions.

Sully F Chen, Robert J Steele, Glen M Hocky, Beakal Lemeneh, Shivanand P Lad, Eric K Oermann

Abstract read
In one paragraph

Article in PloS one, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed, 1 pooled it
–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

3 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Sully F ChenDuke University School of Medicine, Department of Neurosurgery, Durham, North Carolina, United States of America.ORCID https://orcid.org/0000-0001-7719-469X
Robert J SteeleNYU Langone Health, Department of Neurological Surgery, New York, New York, United States of America.
Glen M HockyDepartment of Chemistry and Simons Center for Computational Physical Chemistry, New York University, New York, New York, United States of America.ORCID https://orcid.org/0000-0002-5637-0698
Beakal LemenehNYU Langone Health, Department of Neurological Surgery, New York, New York, United States of America.
Shivanand P LadDuke University School of Medicine, Department of Neurosurgery, Durham, North Carolina, United States of America.
Eric K OermannNYU Langone Health, Department of Neurological Surgery, New York, New York, United States of America.ORCID https://orcid.org/0000-0002-1876-5963

Funding

Harnessing simulations to uncover molecular mechanisms of mechanosensingR35GM138312 · NIGMS · NEW YORK UNIVERSITY · PI Glen Hocky · 2020 to 2026
$3.0M
NIGMS NIH HHS R35 GM138312
6 · The paper itself

Abstract

The transformer architecture has revolutionized bioinformatics and driven progress in the understanding and prediction of the properties of biomolecules. To date, most biosequence transformers have been trained on single-omic data-either proteins or nucleic acids-and have seen incredible success in downstream tasks in each domain, with particularly noteworthy breakthroughs in protein structural modeling. However, single-omic pretraining limits the ability of these models to capture cross-modal interactions. Here we present OmniBioTE, the largest open-source multi-omic model trained on over 250 billion tokens of mixed protein and nucleic acid data. We show that despite only being trained on unlabeled sequence data, OmniBioTE learns joint representations mapping genes to their corresponding protein sequences. We further demonstrate that OmniBioTE achieves state-of-the-art results predicting the change in Gibbs free energy ([Formula: see text]) of the binding interaction between a given nucleic acid and protein. Remarkably, we show that multi-omic biosequence transformers emergently learn useful structural information without any a priori structural training, allowing us to predict which protein residues are most involved in the protein-nucleic acid binding interaction. Compared to single-omic controls trained with identical compute, OmniBioTE also demonstrates superior performance-per-FLOP across both multi-omic and single-omic benchmarks. Together, these results highlight the power of a unified modeling approach for biological sequences and establish OmniBioTE as a foundation model for multi-omic discovery.

Indexed as

Computational BiologyNucleic AcidsProteinsModels, MolecularMultiomicsProtein BindingNucleic AcidsProteins

Identifiers

PMID41628239
PMCPMC12863687

What Socratic holds

Textmetadata
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 Socratic graph.