Evidence map›Paper›PMID 41339546›Full record

ArticleNature2026

Computational enzyme design by catalytic motif scaffolding.

Markus Braun, Adrian Tripp, Morakot Chakatok, Sigrid Kaltenbrunner, Celina Fischer, David Stoll, Aleksandar Bijelic, Wael Elaily, Massimo G Totaro, Melanie Moser and 6 more

Abstract read
In one paragraph

Article in Nature, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed.

  1. High-throughput physics-based enzyme engineering.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Article
  4. Applications and limitations of AI tools in enzyme design.Protein science : a publication of the Protein Society · 2026
    Review
  5. Article
  6. Review
  7. Review
  8. Review
  9. Review
  10. Zero-shot design of abioRxiv : the preprint server for biology · 2026
    Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Review
  16. Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026
    Review
  17. Review
  18. Review
  19. Article
  20. 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

16 authors.

Markus Braun *Institute of Biochemistry, Graz University of Technology, Graz, Austria.
Adrian Tripp *Institute of Biochemistry, Graz University of Technology, Graz, Austria.
Morakot ChakatokInstitute of Biochemistry, Graz University of Technology, Graz, Austria.ORCID 0009-0002-7346-0350
Sigrid KaltenbrunnerInstitute of Biochemistry, Graz University of Technology, Graz, Austria.ORCID 0009-0002-1155-1425
Celina FischerInstitute of Biochemistry, Graz University of Technology, Graz, Austria.ORCID 0009-0009-3106-6962
David StollInstitute of Biochemistry, Graz University of Technology, Graz, Austria.ORCID 0009-0007-9431-915X
Aleksandar BijelicInstitute of Biochemistry, Graz University of Technology, Graz, Austria.
Wael ElailyInstitute of Biochemistry, Graz University of Technology, Graz, Austria.ORCID 0000-0003-4169-9199
Massimo G TotaroInstitute of Biochemistry, Graz University of Technology, Graz, Austria.ORCID 0000-0002-0277-1410
Melanie MoserInstitute of Biochemistry, Graz University of Technology, Graz, Austria.
Shlomo Y HochInstitute of Biochemistry, Graz University of Technology, Graz, Austria.ORCID 0000-0003-3991-1533
Horst LechnerInstitute of Biochemistry, Graz University of Technology, Graz, Austria.ORCID 0000-0002-2177-2611
Federico RossiInstitute of Chemistry, University of Graz, Graz, Austria.ORCID 0009-0005-2957-2082
Matteo AleottiInstitute of Chemistry, University of Graz, Graz, Austria.ORCID 0000-0002-6016-0175
Mélanie HallInstitute of Chemistry, University of Graz, Graz, Austria.ORCID 0000-0003-4539-1992
Gustav OberdorferInstitute of Biochemistry, Graz University of Technology, Graz, Austria. gustav.oberdorfer@tugraz.at.ORCID 0000-0002-6144-9114

Funding

Graz University of Technology
6 · The paper itself

Abstract

Enzymes find broad use as biocatalysts in industry and medicine owing to their exquisite selectivity, efficiency and mild reaction conditions. Custom-designed enzymes can produce tailor-made biocatalysts with potential applications that extend beyond natural reactions. However, current design methods require testing a large number of designs and mostly produce de novo enzymes with low catalytic activities

Indexed as

BiocatalysisEnzymesProtein EngineeringAmino Acid MotifsCatalytic DomainMachine LearningModels, MolecularStereoisomerismEnzymes

Identifiers

PMID41339546
PMCPMC12727513

What OpenQuestion 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 OpenQuestion graph.