Evidence map›Paper›PMID 18829435›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

The role of the C terminus of the SNARE protein SNAP-25 in fusion pore opening and a model for fusion pore mechanics.

Qinghua Fang, Khajak Berberian, Liang-Wei Gong, Ismail Hafez, Jakob B Sørensen, Manfred Lindau

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
–field-weighted citation impact
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

70 citing papers in PubMed.

  1. Fusion Pores as Regulators of Quantal Size and Cellular Physiology.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Energetics, kinetics, and pathways of SNARE assembly in membrane fusion.Critical reviews in biochemistry and molecular biology · 2022
    Review
  8. Article
  9. Article
  10. The function of VAMP2 in mediating membrane fusion: An overview.Frontiers in molecular neuroscience · 2022
    Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

10 more citing papers are in PubMed but not listed here.

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.

Qinghua FangSchool of Applied and Engineering Physics, 212 Clark Hall, Cornell University, Ithaca, NY 14853, USA.
Khajak Berberian
Liang-Wei Gong
Ismail Hafez
Jakob B Sørensen
Manfred Lindau

Funding

Mechanisms of Fusion &Transmitter releaseR01NS038200 · NINDS · CORNELL UNIVERSITY ITHACA · PI LINDAU, MANFRED · 2000 to 2007
$2.3M
Mechanisms of fusion and transmitter release in neurosecretionR01GM085808 · NIGMS · CORNELL UNIVERSITY · PI LINDAU, MANFRED · 2008 to 2012
$1.7M
NIGMS NIH HHS R01 GM085808NINDS NIH HHS R01 NS038200NINDS NIH HHS R01-NS38200
6 · The paper itself

Abstract

Formation of a fusion pore between a vesicle and its target membrane is thought to involve the so-called SNARE protein complex. However, there is no mechanistic model explaining how the fusion pore is opened by conformational changes in the SNARE complex. It has been suggested that C-terminal zipping triggers fusion pore opening. A SNAP-25 mutant named SNAP-25Delta9 (lacking the last nine C-terminal residues) should lead to a less-tight C-terminal zipping. Single exocytotic events in chromaffin cells expressing this mutant were characterized by carbon fiber amperometry and cell-attached patch capacitance measurements. Cells expressing SNAP-25Delta9 displayed smaller amperometric "foot-current" currents, reduced fusion pore conductances, and lower fusion pore expansion rates. We propose that SNARE/lipid complexes form proteolipid fusion pores. Fusion pores involving the SNAP-25Delta9 mutant will be less tightly zipped and may lead to a longer fusion pore structure, consistent with the observed decrease of fusion pore conductance.

Indexed as

Membrane FusionAnimalsCalcium SignalingCattleChromaffin CellsExocytosisKineticsSynaptosomal-Associated Protein 25Synaptosomal-Associated Protein 25

Identifiers

PMID18829435
PMCPMC2563113

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.