Evidence map›Paper›PMID 39075293›Full record

ArticleNature nanotechnology2024

A modular DNA origami nanocompartment for engineering a cell-free, protein unfolding and degradation pathway.

J Huang, A Jaekel, J van den Boom, D Podlesainski, M Elnaggar, A Heuer-Jungemann, M Kaiser, H Meyer, B Saccà

Abstract read
In one paragraph

Article in Nature nanotechnology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Programmable DNA Assemblies Reconstitute Supramolecular Protein Function.bioRxiv : the preprint server for biology · 2026
    Article
  2. Review
  3. Article
  4. Review
  5. DNA Origami and Its Applications in Synthetic Biology.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
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.

J Huang *Bionanotechnology, CENIDE and ZMB, University of Duisburg-Essen, Essen, Germany.ORCID http://orcid.org/0000-0002-8590-5591
A Jaekel *Bionanotechnology, CENIDE and ZMB, University of Duisburg-Essen, Essen, Germany.
J van den BoomMolecular Biology, ZMB, University of Duisburg-Essen, Essen, Germany.ORCID http://orcid.org/0000-0002-2075-9351
D PodlesainskiChemical Biology, ZMB, University of Duisburg-Essen, Essen, Germany.ORCID http://orcid.org/0000-0002-1111-8042
M ElnaggarMax Planck Institute of Biochemistry, Martinsried, Germany.ORCID http://orcid.org/0000-0001-5319-146X
A Heuer-JungemannMax Planck Institute of Biochemistry, Martinsried, Germany.ORCID http://orcid.org/0000-0003-3630-6389
M KaiserChemical Biology, ZMB, University of Duisburg-Essen, Essen, Germany.ORCID http://orcid.org/0000-0002-6540-8520
H MeyerMolecular Biology, ZMB, University of Duisburg-Essen, Essen, Germany. hemmo.meyer@uni-due.de.ORCID http://orcid.org/0000-0003-1883-1796
B SaccàBionanotechnology, CENIDE and ZMB, University of Duisburg-Essen, Essen, Germany. barbara.sacca@uni-due.de.ORCID http://orcid.org/0000-0003-2708-2272

Funding

Deutsche Forschungsgemeinschaft (German Research Foundation) 427981116Deutsche Forschungsgemeinschaft (German Research Foundation) CRC 1096, project A6Deutsche Forschungsgemeinschaft (German Research Foundation) CRC 1430 (424228829)
6 · The paper itself

Abstract

Within the cell, chemical reactions are often confined and organized through a modular architecture. This facilitates the targeted localization of molecular species and their efficient translocation to subsequent sites. Here we present a cell-free nanoscale model that exploits compartmentalization strategies to carry out regulated protein unfolding and degradation. Our synthetic model comprises two connected DNA origami nanocompartments (each measuring 25 nm × 41 nm × 53 nm): one containing the protein unfolding machine, p97, and the other housing the protease chymotrypsin. We achieve the unidirectional immobilization of p97 within the first compartment, establishing a gateway mechanism that controls substrate recruitment, translocation and processing within the second compartment. Our data show that, whereas spatial confinement increases the rate of the individual reactions by up to tenfold, the physical connection of the compartmentalized enzymes into a chimera efficiently couples the two reactions and reduces off-target proteolysis by almost sixfold. Hence, our modular approach may serve as a blueprint for engineering artificial nanofactories with reshaped catalytic performance and functionalities beyond those observed in natural systems.

Indexed as

Cell-Free SystemDNANanostructuresProtein UnfoldingProteolysisChymotrypsinNanotechnologyProtein EngineeringChymotrypsinDNA

Identifiers

PMID39075293
PMCPMC11486656

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Registered trials

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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.