Evidence map›Paper›PMID 39150080›Full record

ArticleProtein science : a publication of the Protein Society2024

A nondestructive membrane engineering method using an amphiphilic polymer.

Nam Hyuk Kim, Goeun Shim, Ga Hyeon Park, Yeon Gyu Yu

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2024. 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
–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

1 citing paper in PubMed.

  1. A nondestructive membrane engineering method using an amphiphilic polymer.Protein science : a publication of the Protein Society · 2024
    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

4 authors.

Nam Hyuk KimDepartment of Chemistry, Kookmin University, Seoul, Republic of Korea.ORCID 0000-0003-4544-6121
Goeun ShimDepartment of Biopharmaceutical Chemistry, Kookmin University, Seoul, Republic of Korea.
Ga Hyeon ParkDepartment of Biopharmaceutical Chemistry, Kookmin University, Seoul, Republic of Korea.
Yeon Gyu YuDepartment of Chemistry, Kookmin University, Seoul, Republic of Korea.

Funding

National Research Foundation of Korea NRF-2020R1A2C1101174
6 · The paper itself

Abstract

The cellular signaling process or ion transport is mediated by membrane proteins (MPs) located on the cell surface, and functional studies of MPs have mainly been conducted using cells endogenously or transiently expressing target proteins. Reconstitution of purified MPs in the surface of live cells would have advantages of short manipulation time and ability to target cells in which gene transfection is difficult. However, direct reconstitution of MPs in live cells has not been established. The traditional detergent-mediated reconstitution method of MPs into a lipid bilayer cannot be applied to live cells because this disrupts and reforms the lipid bilayer structure, which is detrimental to cell viability. In this study, we demonstrated that GPCRs (prostaglandin E2 receptor 4 [EP4] and glucagon-like peptide-1 receptor [GLP1R]) or serotonin receptor 3A (5HT3A), a ligand-gated ion channel, stabilized with amphiphilic poly-γ-glutamate (APG), can be reconstituted into mammalian cell plasma membranes without affecting cell viability. Furthermore, 5HT3A reconstituted in mammalian cells showed ligand-dependent Ca

Indexed as

Cell MembraneReceptors, Serotonin, 5-HT3AnimalsCalciumHEK293 CellsHumansLiposomesMembrane ProteinsCalciumLiposomesMembrane ProteinsReceptors, Serotonin, 5-HT3amphiphilic polymerengineeringGPCRion channelmembranereconstitution

Identifiers

PMID39150080
PMCPMC11328118

What OpenQuestion holds

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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.