Evidence map›Paper›PMID 24552121›Full record

ArticleBiochemistry2014

The SNARE motif of synaptobrevin exhibits an aqueous-interfacial partitioning that is modulated by membrane curvature.

Binyong Liang, Damian Dawidowski, Jeffrey F Ellena, Lukas K Tamm, David S Cafiso

Open access · bronzeAbstract read
In one paragraph

Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.4field-weighted citation impact, top 18% 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

16 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. Mechanisms of SNARE proteins in membrane fusion.Nature reviews. Molecular cell biology · 2024
    Review
  4. Article
  5. Article
  6. Structural dynamics and transient lipid binding of synaptobrevin-2 tune SNARE assembly and membrane fusion.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. The role of cholesterol in membrane fusion.Chemistry and physics of lipids · 2016
    Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. 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

5 authors at 3 institutions in 1 country.

Binyong LiangBiomolecular Magnetic Resonance Research Core, University of Virginia , P.O. Box 800741, Charlottesville, Virginia 22908, United States.
Damian Dawidowski
Jeffrey F Ellena
Lukas K Tamm
David S Cafiso
McCormick (United States) · USUniversity of Virginia · USResonance Research (United States) · US

Funding

Structural Dynamics of the Exocytotic Fusion Machine in Neurons.P01GM072694 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI TAMM, LUKAS K · 2005 to 2021
$17.4M
NIGMS NIH HHS GM072694NIGMS NIH HHS P01 GM072694
6 · The paper itself

Abstract

The structure and interfacial association of the full-length vesicle SNARE, synaptobrevin, were compared in four different lipid environments using nuclear magnetic resonance and electron paramagnetic resonance spectroscopy. In micelles, segments of the SNARE motif are helical and associated with the interface. However, the fraction of helix and interfacial association decreases as synaptobrevin is moved from micelle to bicelle to bilayer environments, indicating that the tendency toward interfacial association is sensitive to membrane curvature. In bilayers, the SNARE motif of synaptobrevin transiently associates with the lipid interface, and regions that are helical in micelles are in conformational and environmental exchange in bicelles and bilayers. This work demonstrates that the SNARE motif of synaptobrevin has a significant propensity to form a helix and exchange with the membrane interface prior to SNARE assembly. This transient interfacial association and its sensitivity to membrane curvature are likely to play a role in SNARE recognition events that regulate membrane fusion.

Indexed as

Magnetic Resonance SpectroscopyMicellesModels, BiologicalProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryR-SNARE ProteinsMicellesR-SNARE Proteins

Identifiers

PMID24552121
PMCPMC3985803
OpenAlexW2317897607

What OpenQuestion holds

Textmetadata
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.