Evidence map›Paper›PMID 19489736›Full record

ReviewAnnual review of biochemistry2009

Single-molecule studies of the neuronal SNARE fusion machinery.

Axel T Brunger, Keith Weninger, Mark Bowen, Steven Chu

Open access · greenAbstract readReview
In one paragraph

Review in Annual review of biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
5.5field-weighted citation impact, top 3% 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

57 citing papers in PubMed, 106 citations in OpenAlex.

  1. Article
  2. Synaptobrevin-2 disease variants reveal spatial constraints within the presynaptic active zone.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Review
  4. Review
  5. Article
  6. The function of VAMP2 in mediating membrane fusion: An overview.Frontiers in molecular neuroscience · 2022
    Review
  7. Article
  8. Selected tools to visualize membrane interactions.European biophysics journal : EBJ · 2021
    Review
  9. Article
  10. InducibleThe Journal of biological chemistry · 2019
    Article
  11. Article
  12. Review
  13. KPlant physiology · 2019
    Article
  14. Single-Molecule Optical Tweezers Study of Regulated SNARE Assembly.Methods in molecular biology (Clifton, N.J.) · 2019
    Article
  15. Review
  16. Structural characterization of the Rabphilin-3A-SNAP25 interaction.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  17. Article
  18. Review
  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

4 authors at 3 institutions in 1 country.

Axel T BrungerThe Howard Hughes Medical Institute and Departments of Molecular and Cellular Physiology, Neurology and Neurological Sciences, Structural Biology, and Photon Science, Stanford University, CA 94305, USA. brunger@stanford.edu
Keith Weninger
Mark Bowen
Steven Chu
Howard Hughes Medical Institute · USNorth Carolina State University · USStony Brook University Hospital · US

Funding

SINGLE MOLECULE ANALYSIS OF PSD-95 STRUCTURE AND LIGAND BINDINGR01MH081923 · NIMH · STATE UNIVERSITY NEW YORK STONY BROOK · PI BOWEN, MARK E · 2008 to 2022
$5.6M
STRUCTURE OF PROTEINS INVOLVED IN SYNAPTIC EXOCYTOSISR01MH063105 · NIMH · STANFORD UNIVERSITY · PI BRUNGER, AXEL T · 2000 to 2025
$4.7M
Single molecule studies of SNARE-induced vesicle fusionR37MH063105 · NIMH · STANFORD UNIVERSITY · PI BRUNGER, AXEL T · 2011 to 2020
$4.7M
Detecting Individual Protein Conformation in Live CellsR21GM076039 · NIGMS · NORTH CAROLINA STATE UNIVERSITY RALEIGH · PI WENINGER, KEITH R. · 2006 to 2007
$366k
Howard Hughes Medical InstituteNIGMS NIH HHS GM 076039NIGMS NIH HHS R21 GM076039NIMH NIH HHS 1R01 MH 63105NIMH NIH HHS MH 081923-01NIMH NIH HHS R01 MH063105NIMH NIH HHS R01 MH081923NIMH NIH HHS R37 MH063105
6 · The paper itself

Abstract

SNAREs are essential components of the machinery for Ca(2+)-triggered fusion of synaptic vesicles with the plasma membrane, resulting in neurotransmitter release into the synaptic cleft. Although much is known about their biophysical and structural properties and their interactions with accessory proteins such as the Ca(2+) sensor synaptotagmin, their precise role in membrane fusion remains an enigma. Ensemble studies of liposomes with reconstituted SNAREs have demonstrated that SNAREs and accessory proteins can trigger lipid mixing/fusion, but the inability to study individual fusion events has precluded molecular insights into the fusion process. Thus, this field is ripe for studies with single-molecule methodology. In this review, we discuss applications of single-molecule approaches to observe reconstituted SNAREs, their complexes, associated proteins, and their effect on biological membranes. Some of the findings are provocative, such as the possibility of parallel and antiparallel SNARE complexes or of vesicle docking with only syntaxin and synaptobrevin, but have been confirmed by other experiments.

Indexed as

AnimalsFluorescenceHumansMicroscopy, Atomic ForceNeuronsSNARE ProteinsSpectrum AnalysisSynaptotagminsSNARE ProteinsSynaptotagmins

Identifiers

PMID19489736
PMCPMC2854664
OpenAlexW2134371594

What OpenQuestion holds

Textmetadata
LicenceTDM
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.