Evidence map›Paper›PMID 28631927›Full record

ArticleBiomacromolecules2017

Stabilization of a Virus-Like Particle and Its Application as a Nanoreactor at Physiological Conditions.

Lise Schoonen, Sjors Maassen, Roeland J M Nolte, Jan C M van Hest

Open access · hybridAbstract read
In one paragraph

Article in Biomacromolecules, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
4.9field-weighted citation impact, top 5% of its field
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

12 citing papers in PubMed, 43 citations in OpenAlex.

  1. Review
  2. Article
  3. Anticancer Activity of Reconstituted Ribonuclease S-Decorated Artificial Viral Capsid.Chembiochem : a European journal of chemical biology · 2022
    Article
  4. Review
  5. Review
  6. Protein scaffolds: A tool for multi-enzyme assembly.Biotechnology reports (Amsterdam, Netherlands) · 2021
    Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Physical, chemical, and synthetic virology: Reprogramming viruses as controllable nanodevices.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2019
    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

4 authors at 1 institution in 1 country.

Lise SchoonenRadboud University, Institute for Molecules and Materials , Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands.
Sjors MaassenRadboud University, Institute for Molecules and Materials , Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands.
Roeland J M NolteRadboud University, Institute for Molecules and Materials , Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands.
Jan C M van HestEindhoven University of Technology , P.O. Box 513 (STO 3.31), 5600 MB Eindhoven, The Netherlands.ORCID http://orcid.org/0000-0001-7973-2404
Radboud University Nijmegen · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Virus-like particles are very interesting tools for application in bionanotechnology, due to their monodisperse features and biocompatibility. In particular, the cowpea chlorotic mottle virus (CCMV) capsid has been studied extensively as it can be assembled and disassembled reversibly, facilitating cargo encapsulation. CCMV is, however, only stable at physiological conditions when its endogenous nucleic acid cargo is present. To gain more flexibility in the type of cargo encapsulated and to broaden the window of operation, it is interesting to improve the stability of the empty virus-like particles. Here, a method is described to utilize the CCMV capsid at close to physiological conditions as a stable, enzyme-filled nanoreactor. As a proof-of-principle, the encapsulation of T4 lysozyme (T4L) was chosen; this enzyme is a promising antibiotic, but its clinical application is hampered by, for example, its cationic character. It was shown that four T4L molecules can successfully be encapsulated inside CCMV capsids, while remaining catalytically active, which could thus improve the enzyme's application potential.

Indexed as

NanotechnologyAnti-Bacterial AgentsBioreactorsBromovirusCapsid ProteinsHumansModels, MolecularMuramidaseNucleic AcidsAnti-Bacterial AgentsCapsid ProteinsMuramidaseNucleic Acids

Identifiers

PMID28631927
PMCPMC5686562
OpenAlexW2643596984

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.