Evidence map›Paper›PMID 24082135›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

In vitro evolution of α-hemolysin using a liposome display.

Satoshi Fujii, Tomoaki Matsuura, Takeshi Sunami, Yasuaki Kazuta, Tetsuya Yomo

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. 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
11.2field-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, 143 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Journal of the American Chemical Society · 2026
    Article
  5. Article
  6. Article
  7. Applications of cell free protein synthesis in protein design.Protein science : a publication of the Protein Society · 2024
    Review
  8. Article
  9. Progresses in Cell-Free In Vitro Evolution.Advances in biochemical engineering/biotechnology · 2023
    Review
  10. Methods to mechanically perturb and characterize GUV-based minimal cell models.Computational and structural biotechnology journal · 2023
    Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  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

5 authors at 2 institutions in 1 country.

Satoshi FujiiDynamical Microscale Reaction Environment Project, Exploratory Research for Advanced Technology, Japan Science and Technology Agency, 1-5 Yamadaoka, Suita, Osaka 565-0871, Japan.
Tomoaki Matsuura
Takeshi Sunami
Yasuaki Kazuta
Tetsuya Yomo
Japan Science and Technology Agency · JPOsaka University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In vitro methods have enabled the rapid and efficient evolution of proteins and successful generation of novel and highly functional proteins. However, the available methods consider only globular proteins (e.g., antibodies, enzymes) and not membrane proteins despite the biological and pharmaceutical importance of the latter. In this study, we report the development of a method called liposome display that can evolve the properties of membrane proteins entirely in vitro. This method, which involves in vitro protein synthesis inside liposomes, which are cell-sized phospholipid vesicles, was applied to the pore-forming activity of α-hemolysin, a membrane protein derived from Staphylococcus aureus. The obtained α-hemolysin mutant possessed only two point mutations but exhibited a 30-fold increase in its pore-forming activity compared with the WT. Given the ability to synthesize various membrane proteins and modify protein synthesis and functional screening conditions, this method will allow for the rapid and efficient evolution of a wide range of membrane proteins.

Indexed as

Point MutationBacterial ToxinsDirected Molecular EvolutionHemolysin ProteinsLiposomesPhospholipidsStaphylococcus aureusBacterial ToxinsHemolysin ProteinsLiposomesPhospholipidsstaphylococcal alpha-toxindirected evolutionFACSGiant unilamellar vesiclesin vitro synthetic biologyPURE system

Identifiers

PMID24082135
PMCPMC3801045
OpenAlexW2034070577

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.