Evidence map›Paper›PMID 29735682›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Laboratory evolution of virus-like nucleocapsids from nonviral protein cages.

Naohiro Terasaka, Yusuke Azuma, Donald Hilvert

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing 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

36 citing papers in PubMed.

  1. Review
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  3. Chemical reviews · 2026
    Review
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  7. Journal of the American Chemical Society · 2025
    Article
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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

3 authors.

Naohiro TerasakaLaboratory of Organic Chemistry, Eidgenössische Technische Hochschule Zürich, 8093 Zürich, Switzerland.ORCID 0000-0002-4988-6899
Yusuke AzumaLaboratory of Organic Chemistry, Eidgenössische Technische Hochschule Zürich, 8093 Zürich, Switzerland.ORCID 0000-0003-3543-3159
Donald HilvertLaboratory of Organic Chemistry, Eidgenössische Technische Hochschule Zürich, 8093 Zürich, Switzerland hilvert@org.chem.ethz.ch.ORCID 0000-0002-3941-621X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Viruses are remarkable nanomachines that efficiently hijack cellular functions to replicate and self-assemble their components within a complex biological environment. As all steps of the viral life cycle depend on formation of a protective proteinaceous shell that packages the DNA or RNA genome, bottom-up construction of virus-like nucleocapsids from nonviral materials could provide valuable insights into virion assembly and evolution. Such constructs could also serve as safe alternatives to natural viruses for diverse nano- and biotechnological applications. Here we show that artificial virus-like nucleocapsids can be generated-rapidly and surprisingly easily-by engineering and laboratory evolution of a nonviral protein cage formed by

Indexed as

BioengineeringDirected Molecular EvolutionBacteriaCapsid ProteinsModels, MolecularMultienzyme ComplexesNucleocapsidPeptide FragmentsVirus Assembly6,7-dimethyl-8-ribityllumazine synthaseCapsid ProteinsMultienzyme ComplexesPeptide Fragmentsdirected evolutionnucleocapsidprotein cagesynthetic biology

Identifiers

PMID29735682
PMCPMC6003473

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.