Evidence map›Paper›PMID 40533551›Full record

ArticleNature2025

Complete computational design of high-efficiency Kemp elimination enzymes.

Dina Listov, Eva Vos, Gyula Hoffka, Shlomo Yakir Hoch, Andrej Berg, Shelly Hamer-Rogotner, Orly Dym, Shina Caroline Lynn Kamerlin, Sarel J Fleishman

Abstract read
In one paragraph

Article in Nature, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing 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

29 citing papers in PubMed.

  1. Article
  2. High-throughput physics-based enzyme engineering.bioRxiv : the preprint server for biology · 2026
    Article
  3. Predicting Activation Barriers With Ring and Bond Critical Points in the Kemp Elimination Reaction.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026
    Article
  4. Article
  5. Review
  6. Applications and limitations of AI tools in enzyme design.Protein science : a publication of the Protein Society · 2026
    Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  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

9 authors.

Dina ListovDepartment of Biomolecular Sciences, Weizmann Institute of Science, Rehovot, Israel.ORCID 0000-0002-7378-1771
Eva VosSchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA, USA.
Gyula HoffkaDepartment of Chemistry, Lund University, Lund, Sweden.
Shlomo Yakir HochDepartment of Biomolecular Sciences, Weizmann Institute of Science, Rehovot, Israel.
Andrej BergDepartment of Chemistry - BMC, Uppsala University, Uppsala, Sweden.ORCID 0000-0002-5232-1995
Shelly Hamer-RogotnerStructural Proteomics Unit, Weizmann Institute of Science, Rehovot, Israel.
Orly DymStructural Proteomics Unit, Weizmann Institute of Science, Rehovot, Israel.
Shina Caroline Lynn KamerlinSchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA, USA.ORCID 0000-0002-3190-1173
Sarel J FleishmanDepartment of Biomolecular Sciences, Weizmann Institute of Science, Rehovot, Israel. sarel@weizmann.ac.il.ORCID 0000-0003-3177-7560

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Until now, computationally designed enzymes exhibited low catalytic rates

Indexed as

EnzymesProtein EngineeringBiocatalysisCatalytic DomainEnzyme StabilityKineticsModels, MolecularMutationEnzymes

Identifiers

PMID40533551
PMCPMC12310539

What OpenQuestion holds

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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.