Evidence map›Paper›PMID 27708275›Full record

ArticleNature communications2016

A modular platform for one-step assembly of multi-component membrane systems by fusion of charged proteoliposomes.

Robert R Ishmukhametov, Aidan N Russell, Richard M Berry

Abstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Membrane-Associated Biomolecules for Synthetic Cell Signalling.Chembiochem : a European journal of chemical biology · 2026
    Review
  2. Review
  3. Spatially regulated mRNA translation enables functional membrane protein integration in synthetic cells.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Review
  5. Article
  6. SecYEG-mediated translocation in a model synthetic cell.Synthetic biology (Oxford, England) · 2024
    Article
  7. Review
  8. Article
  9. Increased efficiency of charge-mediated fusion in polymer/lipid hybrid membranes.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. 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

3 authors.

Robert R IshmukhametovDepartment of Physics, University of Oxford, Clarendon Laboratory, Parks Road, Oxford OX1 3PU, UK.
Aidan N RussellDepartment of Physics, University of Oxford, Clarendon Laboratory, Parks Road, Oxford OX1 3PU, UK.
Richard M BerryDepartment of Physics, University of Oxford, Clarendon Laboratory, Parks Road, Oxford OX1 3PU, UK.

Funding

Biotechnology and Biological Sciences Research Council BB/I004831/1
6 · The paper itself

Abstract

An important goal in synthetic biology is the assembly of biomimetic cell-like structures, which combine multiple biological components in synthetic lipid vesicles. A key limiting assembly step is the incorporation of membrane proteins into the lipid bilayer of the vesicles. Here we present a simple method for delivery of membrane proteins into a lipid bilayer within 5 min. Fusogenic proteoliposomes, containing charged lipids and membrane proteins, fuse with oppositely charged bilayers, with no requirement for detergent or fusion-promoting proteins, and deliver large, fragile membrane protein complexes into the target bilayers. We demonstrate the feasibility of our method by assembling a minimal electron transport chain capable of adenosine triphosphate (ATP) synthesis, combining Escherichia coli F

Indexed as

Adenosine TriphosphateCalibrationCell MembraneCobaltElectron TransportEscherichia coliFluoresceinsGlycine maxLipid BilayersLiposomesMembrane FusionMembrane ProteinsOxidoreductasesProtein BindingProteolipidsProton PumpsAdenosine TriphosphateCobaltFluoresceinsfluorexonLipid BilayersLiposomesMembrane ProteinsOxidoreductasesProteolipidsproteoliposomesProton PumpsProton-Translocating ATPases

Identifiers

PMID27708275
PMCPMC5059690

What OpenQuestion holds

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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.