Evidence map›Paper›PMID 26861509›Full record

ArticleNature communications2016

Nanocaged enzymes with enhanced catalytic activity and increased stability against protease digestion.

Zhao Zhao, Jinglin Fu, Soma Dhakal, Alexander Johnson-Buck, Minghui Liu, Ting Zhang, Neal W Woodbury, Yan Liu, Nils G Walter, Hao Yan

Abstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 126 papers.

0numbers the graph read from it
0cells of the map it votes in
126citing 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

126 citing papers in PubMed.

  1. Programmable DNA Assemblies Reconstitute Supramolecular Protein Function.bioRxiv : the preprint server for biology · 2026
    Article
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  4. Construction of a COChemistry (Weinheim an der Bergstrasse, Germany) · 2026
    Article
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  6. Article
  7. Review
  8. Review
  9. DNA Origami and Its Applications in Synthetic Biology.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

66 more citing papers are in PubMed but not listed here.

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.

Zhao ZhaoCenter for Molecular Design and Biomimetics, the Biodesign Institute at Arizona State University, Tempe, Arizona 85287, USA.
Jinglin FuDepartment of Chemistry, Center for Computational and Integrative Biology, Rutgers University-Camden, Camden, New Jersey 08102, USA.
Soma DhakalDepartment of Chemistry, Single Molecule Analysis Group, University of Michigan, Ann Arbor, Michigan 48109, USA.
Alexander Johnson-BuckDepartment of Chemistry, Single Molecule Analysis Group, University of Michigan, Ann Arbor, Michigan 48109, USA.
Minghui LiuCenter for Molecular Design and Biomimetics, the Biodesign Institute at Arizona State University, Tempe, Arizona 85287, USA.
Ting ZhangDepartment of Chemistry, Center for Computational and Integrative Biology, Rutgers University-Camden, Camden, New Jersey 08102, USA.
Neal W WoodburySchool of Molecular Sciences, Arizona State University, Tempe, Arizona 85287, USA.
Yan LiuCenter for Molecular Design and Biomimetics, the Biodesign Institute at Arizona State University, Tempe, Arizona 85287, USA.
Nils G WalterDepartment of Chemistry, Single Molecule Analysis Group, University of Michigan, Ann Arbor, Michigan 48109, USA.
Hao YanCenter for Molecular Design and Biomimetics, the Biodesign Institute at Arizona State University, Tempe, Arizona 85287, USA.

Funding

Theranostic Nano-objects: Basic Principles and Initial ApplicationsR01GM104960 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI STOJANOVIC, MILAN N, YAN, HAO · 2012 to 2016
$5.4M
NIGMS NIH HHS R01 GM104960NIGMS NIH HHS R01GM104960
6 · The paper itself

Abstract

Cells routinely compartmentalize enzymes for enhanced efficiency of their metabolic pathways. Here we report a general approach to construct DNA nanocaged enzymes for enhancing catalytic activity and stability. Nanocaged enzymes are realized by self-assembly into DNA nanocages with well-controlled stoichiometry and architecture that enabled a systematic study of the impact of both encapsulation and proximal polyanionic surfaces on a set of common metabolic enzymes. Activity assays at both bulk and single-molecule levels demonstrate increased substrate turnover numbers for DNA nanocage-encapsulated enzymes. Unexpectedly, we observe a significant inverse correlation between the size of a protein and its activity enhancement. This effect is consistent with a model wherein distal polyanionic surfaces of the nanocage enhance the stability of active enzyme conformations through the action of a strongly bound hydration layer. We further show that DNA nanocages protect encapsulated enzymes against proteases, demonstrating their practical utility in functional biomaterials and biotechnology.

Indexed as

Enzyme Stabilitybeta-GalactosidaseCatalysisDNAEnzymesGlucose OxidaseGlucosephosphate DehydrogenaseHorseradish PeroxidaseLactate DehydrogenasesMalate DehydrogenaseMicroscopy, Electron, TransmissionMicroscopy, FluorescenceNanostructuresbeta-GalactosidaseDNAEnzymesGlucose OxidaseGlucosephosphate DehydrogenaseHorseradish PeroxidaseLactate DehydrogenasesMalate Dehydrogenase

Identifiers

PMID26861509
PMCPMC4749968

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.