Evidence map›Paper›PMID 36372831›Full record

ArticleExtremophiles : life under extreme conditions2022

Self-assembly of Aeropyrum pernix bacilliform virus 1 (APBV1) major capsid protein and its application as building blocks for nanomaterials.

Yuka Sumikama, Atsushi Takashima, Tomohiro Mochizuki, Haruhiko Sakuraba, Toshihisa Ohshima, Shinji Sugihara, Shin-Ichiro Suye, Takenori Satomura

Abstract read
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In one paragraph

Article in Extremophiles : life under extreme conditions, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.8field-weighted citation impact, top 25% 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

1 citing paper in PubMed, 5 citations in OpenAlex.

  1. 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

8 authors at 4 institutions in 1 country.

Yuka SumikamaIndustrial Innovation Engineering, Graduate School of Engineering, University of Fukui, 3-9-1 Bunkyo, Fukui, 910-8507, Japan.
Atsushi TakashimaIndustrial Innovation Engineering, Graduate School of Engineering, University of Fukui, 3-9-1 Bunkyo, Fukui, 910-8507, Japan.
Tomohiro MochizukiEarth-Life Science Institute, Tokyo Institute of Technology, 2-12-1 Ookayama, Meguro-Ku, Tokyo, 152-8550, Japan.
Haruhiko SakurabaFaculty of Agriculture, Department of Applied Biological Science, Kagawa University, 2393 Ikenobe, Miki-Cho, Kita-Gun, Kagawa, 761-0795, Japan.
Toshihisa OhshimaFaculty of Engineering, Department of Biomedical Engineering, Osaka Institute of Technology, Omiya, 5-16-1 Asahi-Ku, Osaka, 535-8585, Japan.
Shinji SugiharaDivision of Engineering, Faculty of Engineering, University of Fukui, Fukui, 910-8507, Japan.
Shin-Ichiro SuyeDivision of Engineering, Faculty of Engineering, University of Fukui, Fukui, 910-8507, Japan.
Takenori SatomuraDivision of Engineering, Faculty of Engineering, University of Fukui, Fukui, 910-8507, Japan. satomura@u-fukui.ac.jp.
University of Fukui · JPKagawa University · JPLife Science Institute · JPOsaka Institute of Technology · JP

Funding

Japan Society for the Promotion of Science KAKENHI Grant No. 15H04490
6 · The paper itself

Abstract

Virus capsid proteins have various applications in diverse fields such as biotechnology, electronics, and medicine. In this study, the major capsid protein of bacilliform clavavitus APBV1, which infects the hyperthermophilic archaeon Aeropyrum pernix, was successfully expressed in Escherichia coli. The gene product was expressed as a histidine-tagged protein in E. coli and purified to homogeneity using single-step nickel affinity chromatography. The purified recombinant protein self-assembled to form bacilliform virus-like particles at room temperature. The particles exhibited tolerance against high concentrations of organic solvents and protein denaturants. In addition, we succeeded in fabricating functional nanoparticles with amine functional groups on the surface of ORF6-81 nanoparticles. These robust protein nanoparticles can potentially be used as a scaffold in nanotechnological applications.

Indexed as

AeropyrumNanostructuresArchaeaCapsid ProteinsEscherichia coliRecombinant ProteinsCapsid ProteinsRecombinant ProteinsHyperthermophilic archaeaNanoparticle surface modificationProtein expression in E. coliSelf-assembled nanoparticleVirus capsid protein

Identifiers

PMID36372831
OpenAlexW4309048305

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.