Evidence map›Paper›PMID 24867324›Full record

ArticleNature communications2014

The full-length cell-cell fusogen EFF-1 is monomeric and upright on the membrane.

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

Open access · hybridAbstract read
In one paragraph

Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

28 citing papers in PubMed, 48 citations in OpenAlex.

  1. Visualization of membrane-stabilized SorCS2Journal of structural biology: X · 2026
    Article
  2. Article
  3. Extracellular vesicles.Genetics · 2024
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Evolutionarily related small viral fusogens hijack distinct but modular actin nucleation pathways to drive cell-cell fusion.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  9. Review
  10. Fusexins, HAP2/GCS1 and Evolution of Gamete Fusion.Frontiers in cell and developmental biology · 2021
    Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
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  19. Time to make the doughnuts: Building and shaping seamless tubes.Seminars in cell & developmental biology · 2017
    Review
  20. 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 at 2 institutions in 1 country.

Tzviya Zeev-Ben-MordehaiOxford Particle Imaging Centre, Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, UK.
Daven VasishtanOxford Particle Imaging Centre, Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, UK.
C Alistair SiebertOxford Particle Imaging Centre, Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, UK.
Kay GrünewaldOxford Particle Imaging Centre, Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, 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

Fusogens are membrane proteins that remodel lipid bilayers to facilitate membrane merging. Although several fusogen ectodomain structures have been solved, structural information on full-length, natively membrane-anchored fusogens is scarce. Here we present the electron cryo microscopy three-dimensional reconstruction of the Caenorhabditis elegans epithelial fusion failure 1 (EFF-1) protein natively anchored in cell-derived membrane vesicles. This reveals a membrane protruding, asymmetric, elongated monomer. Flexible fitting of a protomer of the EFF-1 crystal structure, which is homologous to viral class-II fusion proteins, shows that EFF-1 has a hairpin monomeric conformation before fusion. These structural insights, when combined with our observations of membrane-merging intermediates between vesicles, enable us to propose a model for EFF-1 mediated fusion. This process, involving identical proteins on both membranes to be fused, follows a mechanism that shares features of SNARE-mediated fusion while using the structural building blocks of the unilaterally acting class-II viral fusion proteins.

Indexed as

AnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsCell FusionCell LineCell MembraneCricetinaeMass SpectrometryMembrane GlycoproteinsModels, BiologicalAFF-1 protein, C elegansCaenorhabditis elegans ProteinsEFF-1 protein, C elegansMembrane Glycoproteins

Identifiers

PMID24867324
PMCPMC4050280
OpenAlexW2049552177

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.