Evidence map›Paper›PMID 40613217›Full record

ArticleAdvanced materials (Deerfield Beach, Fla.)2025

Flippase-Mediated Hybrid Vesicle Division.

Paula De Dios Andres, Amalie Benfeldt Purup, Grégory Beaune, Jaakko V I Timonen, Joseph A Lyons, Brigitte Städler

Abstract read
In one paragraph

Article in Advanced materials (Deerfield Beach, Fla.), 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. Review
  2. Flippase-Mediated Hybrid Vesicle Division.Advanced materials (Deerfield Beach, Fla.) · 2025
    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

6 authors.

Paula De Dios AndresInterdisciplinary Nanoscience Center (iNANO), Aarhus University, Aarhus, 8000, Denmark.ORCID https://orcid.org/0000-0003-3315-5319
Amalie Benfeldt PurupInterdisciplinary Nanoscience Center (iNANO), Aarhus University, Aarhus, 8000, Denmark.
Grégory BeauneDepartment of Applied Physics, Aalto University School of Science, Espoo, Aalto, FI-00076, Finland.
Jaakko V I TimonenDepartment of Applied Physics, Aalto University School of Science, Espoo, Aalto, FI-00076, Finland.ORCID https://orcid.org/0000-0002-5499-1482
Joseph A LyonsInterdisciplinary Nanoscience Center (iNANO), Aarhus University, Aarhus, 8000, Denmark.ORCID https://orcid.org/0000-0003-0218-4862
Brigitte StädlerInterdisciplinary Nanoscience Center (iNANO), Aarhus University, Aarhus, 8000, Denmark.ORCID https://orcid.org/0000-0002-7335-3945

Funding

Academy of Finland Center of Excellence Program 346112EMBION Danish National cryoEM facility of Aarhus University 5072-00025BH2020 European Research Council 818890Lundbeck Foundation R335-2019-2053
6 · The paper itself

Abstract

The assembly of synthetic systems with the ability for protein-mediated division remains a challenge in bottom-up synthetic biology. Here, the reconstitution of an active Drs2p-Cdc50p lipid flippase in polymer lipid hybrid vesicles (HVs) made from phospholipids and 1 or 2.5 mol% amphiphilic block copolymers, with poly(carboxyethyl acrylate) or poly(6-O-methacryloyl-d-galactopyranose) as the hydrophilic extension and either cholesteryl methacrylate or butyl methacrylate or combinations thereof as the hydrophobic blocks is demonstrated. The reconstitution of Drs2p-Cdc50p in HVs flip 2-dioleoyl-sn-glycero-3-phospho-l-serine (DOPS) lipids from the inner to the outer leaflet, leading to transmembrane asymmetry. Importantly, the chemical nature of the hydrophobic block in the amphiphilic block copolymers used to assemble the HVs is crucial to support changes in the spontaneous curvature of the bilayers due to translocation of DOPS lipids that results in HV constriction and division. Taken together, this effort is a step forward in imitating cell division in synthetic assemblies toward potentially bottom-up assembled self-replicating units.

Indexed as

Saccharomyces cerevisiae ProteinsHydrophobic and Hydrophilic InteractionsLipid BilayersPolymersLipid BilayersPolymersSaccharomyces cerevisiae Proteinshybrid vesiclelipid flippasemembrane constrictiontransmembrane asymmetryvesicle division

Identifiers

PMID40613217
PMCPMC12506619

What OpenQuestion holds

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LicenceCC BY-NC
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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.