Evidence map›Paper›PMID 39915241›Full record

ArticleChembiochem : a European journal of chemical biology2025

A Practical Approach for Polarity and Quantity Controlled Assembly of Membrane Proteins into Nanoliposomes.

Shiwei Zhang, Peng Lin, Futa Komatsubara, Eiji Nakata, Takashi Morii

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

5 authors.

Shiwei ZhangInstitute of Advanced Energy, Kyoto University, Uji, Kyoto, 6110011, Japan.
Peng LinInstitute of Advanced Energy, Kyoto University, Uji, Kyoto, 6110011, Japan.ORCID https://orcid.org/0000-0003-2601-0787
Futa KomatsubaraDepartment of Fundamental Energy Science, Graduate School of Energy Science, Kyoto University, Yoshida, Sakyo-ku, Kyoto, 6068501, Japan.ORCID https://orcid.org/0000-0003-0719-6635
Eiji NakataInstitute of Advanced Energy, Kyoto University, Uji, Kyoto, 6110011, Japan.ORCID https://orcid.org/0000-0001-9564-6805
Takashi MoriiInstitute of Advanced Energy, Kyoto University, Uji, Kyoto, 6110011, Japan.ORCID https://orcid.org/0000-0003-3663-3267

Funding

JSPS KAKENHI 23H02083JSPS KAKENHI 23K26776JSPS KAKENHI 24H01129JSPS KAKENHI 24K01629JSPS KAKENHI 24K17787
6 · The paper itself

Abstract

Biological membranes achieve selectivity and permeability through protein transporters and channels. The design of artificial compartments with permeable membranes is essential to facilitate substrate and product transfer in enzymatic reactions. In this study, an E. coli outer membrane protein OmpF fused to a modular adaptor was integrated onto a DNA origami skeleton to control the number and polarity of the OmpF trimer. DNA origami skeleton-guided nanoliposomes reconstituted with functional OmpF exhibit pH-responsiveness and size-selective permeability. This approach highlights the potential to construct artificial compartments that incorporate membrane proteins of defined number and polarity, allowing tunable substrate fluxes.

Indexed as

LiposomesMembrane ProteinsPorinsDNAEscherichia coliEscherichia coli ProteinsHydrogen-Ion ConcentrationDNAEscherichia coli ProteinsLiposomesMembrane ProteinsOmpF proteinPorinsDNA origamiliposomesmembrane transportermodular adaptorsize exclusion transport

Identifiers

PMID39915241
PMCPMC11907387

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.