Evidence map›Paper›PMID 40179182›Full record

ArticleScience (New York, N.Y.)2025

Protein editing using a coordinated transposition reaction.

Yi Hua, Nicholas E S Tay, Xuanjia Ye, Jeremy A Owen, Hengyuan Liu, Robert E Thompson, Tom W Muir

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. Chemical Biology 2025: Highlights From the Ch/Bi145 Course at Caltech.Chembiochem : a European journal of chemical biology · 2026
    Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Co-Translational Incorporation of (Journal of the American Chemical Society · 2026
    Article
  8. Article
  9. Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026
    Review
  10. Article
  11. Article
  12. A transposon-like strategy for proteins.Nature chemical biology · 2025
    Article
  13. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Yi Hua *Department of Chemistry, Princeton University, Princeton, NJ, USA.ORCID 0009-0006-3662-5581
Nicholas E S Tay *Department of Chemistry, Princeton University, Princeton, NJ, USA.ORCID 0000-0002-4063-8880
Xuanjia YeDepartment of Chemistry, Princeton University, Princeton, NJ, USA.ORCID 0000-0002-6277-6045
Jeremy A OwenDepartment of Chemistry, Princeton University, Princeton, NJ, USA.
Hengyuan LiuDepartment of Chemistry, Princeton University, Princeton, NJ, USA.ORCID 0000-0003-1540-7295
Robert E ThompsonDepartment of Chemistry, Princeton University, Princeton, NJ, USA.
Tom W MuirDepartment of Chemistry, Princeton University, Princeton, NJ, USA.ORCID 0000-0001-9635-0344

Funding

Structure, Function and Applications of InteinsR01GM086868 · NIGMS · ROCKEFELLER UNIVERSITY · PI MUIR, TOM · 2008 to 2025
$4.4M
New Proximity Labeling Tools for Studying 3D Chromatin Structure and FunctionF32GM149123 · NIGMS · PRINCETON UNIVERSITY · PI TAY, NICHOLAS ENG SOON · 2023 to 2025
$233k
NCI NIH HHS R01 CA240768NIGMS NIH HHS F32 GM149123NIGMS NIH HHS R01 GM086868
6 · The paper itself

Abstract

Protein engineering through the ligation of polypeptide fragments has proven enormously powerful for studying biochemical processes. In general, this strategy necessitates a final protein-folding step, constraining the types of systems amenable to the approach. Here, we report a method that allows internal regions of target proteins to be replaced in a single operation. Conceptually, our system is analogous to a DNA transposition reaction but uses orthogonal pairs of engineered split inteins to mediate the editing process. This "protein transposition" reaction is applied to several systems, including folded protein complexes, allowing the efficient introduction of a variety of noncoded elements. By carrying out a molecular "cut and paste" under native protein-folding conditions, our approach substantially expands the scope of protein semisynthesis.

Indexed as

InteinsProtein EngineeringProtein Folding

Identifiers

PMID40179182
PMCPMC12128185

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.