Evidence map›Paper›PMID 25150720›Full record

ArticleNature nanotechnology2014

Design and self-assembly of simple coat proteins for artificial viruses.

Armando Hernandez-Garcia, Daniela J Kraft, Anne F J Janssen, Paul H H Bomans, Nico A J M Sommerdijk, Dominique M E Thies-Weesie, Marco E Favretto, Roland Brock, Frits A de Wolf, Marc W T Werten and 3 more

Abstract read
PubMed Publisher
In one paragraph

Article in Nature nanotechnology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
17.9field-weighted citation impact, top 1% 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

46 citing papers in PubMed, 157 citations in OpenAlex.

  1. Article
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  6. Review
  7. Article
  8. Article
  9. Article
  10. Virus-inspired strategies for cancer therapy.Seminars in cancer biology · 2022
    Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Strategies to Build Hybrid Protein-DNA Nanostructures.Nanomaterials (Basel, Switzerland) · 2021
    Review
  18. Article
  19. Review
  20. 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

13 authors at 7 institutions in 1 country.

Armando Hernandez-Garcia1] Laboratory of Physical Chemistry and Colloid Science, Wageningen University, Dreijenplein 6, 6703 HB Wageningen, The Netherlands [2] Dutch Polymer Institute, John F. Kennedylaan 2, 5612 AB Eindhoven, The Netherlands [3].
Daniela J Kraft1] Soft Matter Physics, Huygens-Kamerlingh Onnes Laboratory, Leiden University, PO Box 9504, 2300 RA Leiden, The Netherlands [2] Center for Soft Matter Research, Department of Physics, New York University, 4 Washington Place, New York, New York 10003, USA.
Anne F J JanssenLaboratory of Physical Chemistry and Colloid Science, Wageningen University, Dreijenplein 6, 6703 HB Wageningen, The Netherlands.
Paul H H BomansLaboratory of Materials and Interface Chemistry &Soft Matter CryoTEM Research Unit, Department of Chemical Engineering and Chemistry, and Institute for Complex Molecular Systems, Eindhoven University of Technology, PO Box 513, 5600 MB Eindhoven, The Netherlands.
Nico A J M SommerdijkLaboratory of Materials and Interface Chemistry &Soft Matter CryoTEM Research Unit, Department of Chemical Engineering and Chemistry, and Institute for Complex Molecular Systems, Eindhoven University of Technology, PO Box 513, 5600 MB Eindhoven, The Netherlands.
Dominique M E Thies-WeesieUtrecht University, Van't Hoff Laboratory for Physical and Colloid Chemistry, Debye Institute of Nanomaterials Science, PO Box 80.051, 3508 TB Utrecht, The Netherlands.
Marco E Favretto1] Department of Biochemistry, Radboud Institute of Molecular Life Sciences, Radboud University Medical Centre, Geert Grooteplein 28, 6525 GA Nijmegen, The Netherlands [2] Dutch Polymer Institute, John F. Kennedylaan 2, 5612 AB Eindhoven, The Netherlands.
Roland BrockDepartment of Biochemistry, Radboud Institute of Molecular Life Sciences, Radboud University Medical Centre, Geert Grooteplein 28, 6525 GA Nijmegen, The Netherlands.
Frits A de WolfWageningen UR Food &Biobased Research, Bornse Weilanden 9, 6708 WG Wageningen, The Netherlands.ORCID 0000000254161171
Marc W T WertenWageningen UR Food &Biobased Research, Bornse Weilanden 9, 6708 WG Wageningen, The Netherlands.
Paul van der Schoot1] Theory of Polymers and Soft Matter, Department of Applied Physics, Eindhoven University of Technology, PO Box 513, 5600 MB Eindhoven, The Netherlands [2] Institute for Theoretical Physics, Utrecht University, Leuvenlaan 4, 3584 CE Utrecht, The Netherlands.
Martien Cohen StuartLaboratory of Physical Chemistry and Colloid Science, Wageningen University, Dreijenplein 6, 6703 HB Wageningen, The Netherlands.
Renko de Vries1] Laboratory of Physical Chemistry and Colloid Science, Wageningen University, Dreijenplein 6, 6703 HB Wageningen, The Netherlands [2] Department of Biomedical Engineering, University Medical Center Groningen, University of Groningen, PO Box 196, 9700 AD Groningen, The Netherlands.
Wageningen University & Research · NLEindhoven University of Technology · NLRadboud University Nijmegen · NLUtrecht University · NLDutch Polymer Institute · NLLeiden University · NLUniversity Medical Center Groningen · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Viruses are among the simplest biological systems and are highly effective vehicles for the delivery of genetic material into susceptible host cells. Artificial viruses can be used as model systems for providing insights into natural viruses and can be considered a testing ground for developing artificial life. Moreover, they are used in biomedical and biotechnological applications, such as targeted delivery of nucleic acids for gene therapy and as scaffolds in material science. In a natural setting, survival of viruses requires that a significant fraction of the replicated genomes be completely protected by coat proteins. Complete protection of the genome is ensured by a highly cooperative supramolecular process between the coat proteins and the nucleic acids, which is based on reversible, weak and allosteric interactions only. However, incorporating this type of supramolecular cooperativity into artificial viruses remains challenging. Here, we report a rational design for a self-assembling minimal viral coat protein based on simple polypeptide domains. Our coat protein features precise control over the cooperativity of its self-assembly with single DNA molecules to finally form rod-shaped virus-like particles. We confirm the validity of our design principles by showing that the kinetics of self-assembly of our virus-like particles follows a previous model developed for tobacco mosaic virus. We show that our virus-like particles protect DNA against enzymatic degradation and transfect cells with considerable efficiency, making them promising delivery vehicles.

Indexed as

Capsid ProteinsDNAHeLa CellsHumansModels, MolecularPichiaRecombinant ProteinsTransfectionVirusesCapsid ProteinsDNARecombinant Proteins

Identifiers

PMID25150720
OpenAlexW2149102927

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.