Evidence map›Paper›PMID 23836889›Full record

ArticleThe Journal of biological chemistry2013

Disassembly of all SNARE complexes by N-ethylmaleimide-sensitive factor (NSF) is initiated by a conserved 1:1 interaction between α-soluble NSF attachment protein (SNAP) and SNARE complex.

Sandro Vivona, Daniel J Cipriano, Seán O'Leary, Ye Henry Li, Timothy D Fenn, Axel T Brunger

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

32 citing papers in PubMed, 44 citations in OpenAlex.

  1. Munc18 reprograms the intrinsic neuronal SNARE complex assembly pathway.bioRxiv : the preprint server for biology · 2026
    Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Mechanisms of SNARE proteins in membrane fusion.Nature reviews. Molecular cell biology · 2024
    Review
  8. Article
  9. Review
  10. Mitochondrial Surveillance by Cdc48/p97: MAD vs. Membrane Fusion.International journal of molecular sciences · 2020
    Review
  11. Article
  12. The pre-synaptic fusion machinery.Current opinion in structural biology · 2019
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Disease resistance through impairment of α-SNAP-NSF interaction and vesicular trafficking by soybean Rhg1.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  18. Article
  19. 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

6 authors at 2 institutions in 3 countries.

Sandro VivonaDepartment of Molecular and Cellular Physiology, Stanford University Medical School, Stanford, California 94305, USA.
Daniel J Cipriano
Seán O'Leary
Ye Henry Li
Timothy D Fenn
Axel T Brunger
Institute of Neurological Sciences · ITStanford University · US

Funding

Single molecule studies of SNARE-induced vesicle fusionR37MH063105 · NIMH · STANFORD UNIVERSITY · PI BRUNGER, AXEL T · 2011 to 2020
$4.7M
Howard Hughes Medical InstituteNIMH NIH HHS R37 MH063105NIMH NIH HHS R37-MH63105
6 · The paper itself

Abstract

Vesicle trafficking in eukaryotic cells is facilitated by SNARE-mediated membrane fusion. The ATPase NSF (N-ethylmaleimide-sensitive factor) and the adaptor protein α-SNAP (soluble NSF attachment protein) disassemble all SNARE complexes formed throughout different pathways, but the effect of SNARE sequence and domain variation on the poorly understood disassembly mechanism is unknown. By measuring SNARE-stimulated ATP hydrolysis rates, Michaelis-Menten constants for disassembly, and SNAP-SNARE binding constants for four different ternary SNARE complexes and one binary complex, we found a conserved mechanism, not influenced by N-terminal SNARE domains. α-SNAP and the ternary SNARE complex form a 1:1 complex as revealed by multiangle light scattering. We propose a model of NSF-mediated disassembly in which the reaction is initiated by a 1:1 interaction between α-SNAP and the ternary SNARE complex, followed by NSF binding. Subsequent additional α-SNAP binding events may occur as part of a processive disassembly mechanism.

Indexed as

Models, ChemicalAdenosine TriphosphateAnimalsCricetinaeCricetulusMultiprotein ComplexesN-Ethylmaleimide-Sensitive ProteinsProtein BindingRatsSNARE ProteinsSoluble N-Ethylmaleimide-Sensitive Factor Attachment ProteinsAdenosine TriphosphateMultiprotein ComplexesN-Ethylmaleimide-Sensitive ProteinsNsf protein, ratSNARE ProteinsSoluble N-Ethylmaleimide-Sensitive Factor Attachment ProteinsATPasesBiophysicsBiosensorsCircular Dichroism (CD)Enzyme KineticsFluorescenceMembrane FusionProtein-Protein InteractionsSNARE ProteinsStructural Biology

Identifiers

PMID23836889
PMCPMC3750193
OpenAlexW1983127525

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.