Evidence map›Paper›PMID 12414686›Full record

ArticleBiophysical journal2002

SNAREs in opposing bilayers interact in a circular array to form conducting pores.

Sang-Joon Cho, Marie Kelly, Katherine T Rognlien, Jin Ah Cho, J K Heinrich Hörber, Bhanu P Jena

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

43 citing papers in PubMed, 111 citations in OpenAlex.

  1. Article
  2. Nanoscale imaging using differential expansion microscopy.Histochemistry and cell biology · 2020
    Article
  3. Review
  4. Article
  5. Fusion Pore: A Curious Case of Rediscovering Science.Discoveries (Craiova, Romania) · 2017
    Article
  6. Article
  7. The neuronal porosome complex in health and disease.Experimental biology and medicine (Maywood, N.J.) · 2016
    Review
  8. Review
  9. Review
  10. Article
  11. Review
  12. Article
  13. NeuronalJournal of molecular structure · 2014
    Article
  14. Article
  15. Article
  16. Article
  17. Membrane-directed molecular assembly of the neuronal SNARE complex.Journal of cellular and molecular medicine · 2011
    Article
  18. Membrane lipids influence protein complex assembly-disassembly.Journal of the American Chemical Society · 2010
    Article
  19. Article
  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

6 authors at 1 institution in 1 country.

Sang-Joon ChoDepartments of Physiology and Pharmacology, Wayne State University School of Medicine, 540E Canfield Avenue, Detroit, MI 48201, USA.
Marie Kelly
Katherine T Rognlien
Jin Ah Cho
J K Heinrich Hörber
Bhanu P Jena
Wayne State University · US

Funding

EXOCYTOSIS: USING NANOSURGERY AND BIOENGINEERINGR01DK056212 · NIDDK · YALE UNIVERSITY · PI JENA, BHANU P · 1999 to 2003
$1.1M
UNDERSTANDING MEMBRANE FUSION A BIOENGINEERING APPROACHR01NS039918 · NINDS · YALE UNIVERSITY · PI JENA, BHANU P · 2000 to 2001
$791k
Bioengineering Approach to Study SecretionF32DK060368 · NIDDK · WAYNE STATE UNIVERSITY · PI CHO, SANG-JOON · 2001 to 2002
$90k
NIDDK NIH HHS DK 56212NIDDK NIH HHS DK 60368NINDS NIH HHS NS 39918
6 · The paper itself

Abstract

The process of fusion at the nerve terminal is mediated via a specialized set of proteins in the synaptic vesicles and the presynaptic membrane. Three soluble N-ethylmaleimide-sensitive factor (NSF)-attachment protein receptors (SNAREs) have been implicated in membrane fusion. The structure and arrangement of these SNAREs associated with lipid bilayers were examined using atomic force microscopy. A bilayer electrophysiological setup allowed for measurements of membrane conductance and capacitance. Here we demonstrate that the interaction of these proteins to form a fusion pore is dependent on the presence of t-SNAREs and v-SNARE in opposing bilayers. Addition of purified recombinant v-SNARE to a t-SNARE-reconstituted lipid membrane increased only the size of the globular t-SNARE oligomer without influencing the electrical properties of the membrane. However when t-SNARE vesicles were added to a v-SNARE membrane, SNAREs assembles in a ring pattern and a stepwise increase in capacitance, and increase in conductance were observed. Thus, t- and v-SNAREs are required to reside in opposing bilayers to allow appropriate t-/v-SNARE interactions leading to membrane fusion.

Indexed as

Vesicular Transport ProteinsAluminum SilicatesBiophysical PhenomenaBiophysicsCell MembraneElectrophysiologyLipid BilayersMembrane ProteinsMembranes, ArtificialMicroscopy, Atomic ForceProtein BindingRecombinant ProteinsSNARE ProteinsTime FactorsAluminum SilicatesLipid BilayersMembrane ProteinsMembranes, ArtificialmicaRecombinant ProteinsSNARE ProteinsVesicular Transport Proteins

Identifiers

PMID12414686
PMCPMC1302338
OpenAlexW2050563985

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.