Evidence map›Paper›PMID 25438672›Full record

ArticleStructure (London, England : 1993)2014

Extracellular vesicles: a platform for the structure determination of membrane proteins by Cryo-EM.

Tzviya Zeev-Ben-Mordehai, Daven Vasishtan, C Alistair Siebert, Cathy Whittle, Kay Grünewald

Open access · hybridAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

30 citing papers in PubMed, 50 citations in OpenAlex.

  1. Visualization of membrane-stabilized SorCS2Journal of structural biology: X · 2026
    Article
  2. Cryo-EM single-particle analysis expanding towards increasingly native samples.Acta crystallographica. Section D, Structural biology · 2025
    Review
  3. Article
  4. Structure and organization of full-length epidermal growth factor receptor in extracellular vesicles by cryo-electron tomography.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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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.

Tzviya Zeev-Ben-MordehaiDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, UK.
Daven VasishtanDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, UK.
C Alistair SiebertDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, UK.
Cathy WhittleDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, UK.
Kay GrünewaldDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, UK. Electronic address: kay@strubi.ox.ac.uk.
Centre for Human Genetics · GBUniversity of Oxford · GB

Funding

Wellcome Trust 060208/Z/00/ZWellcome Trust 090532/Z/09/ZWellcome Trust 090895Wellcome Trust 093305/Z/10/Z
6 · The paper itself

Abstract

Membrane protein-enriched extracellular vesicles (MPEEVs) provide a platform for studying intact membrane proteins natively anchored with the correct topology in genuine biological membranes. This approach circumvents the need to conduct tedious detergent screens for solubilization, purification, and reconstitution required in classical membrane protein studies. We have applied this method to three integral type I membrane proteins, namely the Caenorhabditis elegans cell-cell fusion proteins AFF-1 and EFF-1 and the glycoprotein B (gB) from Herpes simplex virus type 1 (HSV1). Electron cryotomography followed by subvolume averaging allowed the 3D reconstruction of EFF-1 and HSV1 gB in the membrane as well as an analysis of the spatial distribution and interprotein interactions on the membrane. MPEEVs have many applications beyond structural/functional investigations, such as facilitating the raising of antibodies, for protein-protein interaction assays or for diagnostics use, as biomarkers, and possibly therapeutics.

Indexed as

AnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsCell LineCryoelectron MicroscopyMass SpectrometryMembrane GlycoproteinsMembrane ProteinsModels, MolecularSimplexvirusTransfectionViral Envelope ProteinsAFF-1 protein, C elegansCaenorhabditis elegans ProteinsEFF-1 protein, C elegansglycoprotein B, herpes simplex virus type 2Membrane GlycoproteinsMembrane ProteinsViral Envelope Proteins

Identifiers

PMID25438672
PMCPMC4229021
OpenAlexW1978215296

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.