Evidence map›Paper›PMID 28055188›Full record

ArticleJournal of the American Chemical Society2017

Assembling Enzymatic Cascade Pathways inside Virus-Based Nanocages Using Dual-Tasking Nucleic Acid Tags.

Melanie Brasch, Rindia M Putri, Mark V de Ruiter, Daniel Luque, Melissa S T Koay, José R Castón, Jeroen J L M Cornelissen

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing 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

37 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Protein scaffolds: A tool for multi-enzyme assembly.Biotechnology reports (Amsterdam, Netherlands) · 2021
    Review
  18. Review
  19. Artificial Organelles: Towards Adding or Restoring Intracellular Activity.Chembiochem : a European journal of chemical biology · 2021
    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

7 authors.

Melanie BraschDepartment of Biomolecular Nanotechnology, MESA+ Institute for Nanotechnology, University of Twente , 7500 AE Enschede, The Netherlands.
Rindia M PutriDepartment of Biomolecular Nanotechnology, MESA+ Institute for Nanotechnology, University of Twente , 7500 AE Enschede, The Netherlands.
Mark V de RuiterDepartment of Biomolecular Nanotechnology, MESA+ Institute for Nanotechnology, University of Twente , 7500 AE Enschede, The Netherlands.
Daniel LuqueDepartment of Structure of Macromolecules, Centro Nacional de Biotecnología/CSIC , Cantoblanco, 28049 Madrid, Spain.
Melissa S T KoayDepartment of Biomolecular Nanotechnology, MESA+ Institute for Nanotechnology, University of Twente , 7500 AE Enschede, The Netherlands.
José R CastónDepartment of Structure of Macromolecules, Centro Nacional de Biotecnología/CSIC , Cantoblanco, 28049 Madrid, Spain.
Jeroen J L M CornelissenDepartment of Biomolecular Nanotechnology, MESA+ Institute for Nanotechnology, University of Twente , 7500 AE Enschede, The Netherlands.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The packaging of proteins into discrete compartments is an essential feature for cellular efficiency. Inspired by Nature, we harness virus-like assemblies as artificial nanocompartments for enzyme-catalyzed cascade reactions. Using the negative charges of nucleic acid tags, we develop a versatile strategy to promote an efficient noncovalent co-encapsulation of enzymes within a single protein cage of cowpea chlorotic mottle virus (CCMV) at neutral pH. The encapsulation results in stable 21-22 nm sized CCMV-like particles, which is characteristic of an icosahedral T = 1 symmetry. Cryo-EM reconstruction was used to demonstrate the structure of T = 1 assemblies templated by biological soft materials as well as the extra-swelling capacity of these T = 1 capsids. Furthermore, the specific sequence of the DNA tag is capable of operating as a secondary biocatalyst as well as bridging two enzymes for co-encapsulation in a single capsid while maintaining their enzymatic activity. Using CCMV-like particles to mimic nanocompartments can provide valuable insight on the role of biological compartments in enhancing metabolic efficiency.

Indexed as

BiocatalysisBromovirusGlucose OxidaseNucleic AcidsParticle SizePhosphogluconate DehydrogenasePhosphotransferases (Alcohol Group Acceptor)Surface PropertiesgluconokinaseGlucose OxidaseNucleic AcidsPhosphogluconate DehydrogenasePhosphotransferases (Alcohol Group Acceptor)

Identifiers

PMID28055188
PMCPMC5330652

What OpenQuestion holds

Textmetadata
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.