Evidence map›Paper›PMID 41748587›Full record

ArticleNature communications2026

Identification and engineering of highly functional potyviral proteases in cells using co-evolutionary models.

Medel B Lim Suan, Cheyenne Ziegler, Zain Syed, Arjun Sai Yedavalli, Jaimahesh Nagineni, Rodrigo Raposo, Ajay Tunikipati, Jaideep Kaur, Faruck Morcos, P C Dave P Dingal

Abstract read
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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

10 authors.

Medel B Lim Suan *Department of Bioengineering, The University of Texas at Dallas, Richardson, TX, USA.
Cheyenne Ziegler *Department of Biological Sciences, The University of Texas at Dallas, Richardson, TX, USA.ORCID http://orcid.org/0000-0002-6379-3162
Zain SyedDepartment of Biological Sciences, The University of Texas at Dallas, Richardson, TX, USA.ORCID http://orcid.org/0009-0006-4450-3306
Arjun Sai YedavalliDepartment of Biological Sciences, The University of Texas at Dallas, Richardson, TX, USA.
Jaimahesh NagineniDepartment of Biological Sciences, The University of Texas at Dallas, Richardson, TX, USA.ORCID http://orcid.org/0009-0003-2518-1637
Rodrigo RaposoDepartment of Biological Sciences, The University of Texas at Dallas, Richardson, TX, USA.
Ajay TunikipatiDepartment of Biological Sciences, The University of Texas at Dallas, Richardson, TX, USA.
Jaideep KaurDepartment of Bioengineering, The University of Texas at Dallas, Richardson, TX, USA.
Faruck MorcosDepartment of Bioengineering, The University of Texas at Dallas, Richardson, TX, USA. faruckm@utdallas.edu.ORCID http://orcid.org/0000-0001-6208-1561
P C Dave P DingalDepartment of Bioengineering, The University of Texas at Dallas, Richardson, TX, USA. davedingal@utdallas.edu.ORCID http://orcid.org/0000-0002-1052-2537

Funding

Computational Tools to Characterize the Effects of Protein and RNA Variability in Function and InteractionsR35GM133631 · NIGMS · UNIVERSITY OF TEXAS DALLAS · PI Alonso Faruck Morcos · 2019 to 2026
$3.0M
Natural and synthetic mechanisms of ligand formationR35GM150967 · NIGMS · UNIVERSITY OF TEXAS DALLAS · PI Polimyr Caesar Dave Pelisco Dingal · 2023 to 2026
$1.5M
NIGMS NIH HHS R35 GM150967U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) R35GM133631U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) R35GM150967
6 · The paper itself

Abstract

Efficiency and substrate specificity of proteases in the Potyviridae family have not been comprehensively profiled. Here we develop a model that learns co-evolutionary features to accurately predict and experimentally validate protease performance at single amino-acid resolution. We identify and engineer several proteases that perform better than the commercially available tobacco etch virus protease. To demonstrate the resolving power of our methods, we engineer protease crosstalk to selectively trigger a synthetic cell-death program in human cells.

Indexed as

Peptide HydrolasesPotyvirusProtein EngineeringViral ProteinsEvolution, MolecularHumansSubstrate SpecificityPeptide HydrolasesViral Proteins

Identifiers

PMID41748587
PMCPMC13062108

What OpenQuestion holds

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LicenceCC BY
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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.