Evidence map›Paper›PMID 18596819›Full record

ReviewNature structural & molecular biology2008

The fusion pores of Ca2+ -triggered exocytosis.

Meyer B Jackson, Edwin R Chapman

Open access · greenAbstract readReview
In one paragraph

Review in Nature structural & molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

76 citing papers in PubMed, 124 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Review
  8. Energetics, kinetics, and pathways of SNARE assembly in membrane fusion.Critical reviews in biochemistry and molecular biology · 2022
    Review
  9. Article
  10. Article
  11. The Phosphoprotein Synapsin Ia Regulates the Kinetics of Dense-Core Vesicle Release.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
    Article
  12. Article
  13. Article
  14. Bacterial dynamin-like protein DynA mediates lipid and content mixing.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Phosphatidylcholine Membrane Fusion Is pH-Dependent.International journal of molecular sciences · 2018
    Article
  20. Review

16 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

2 authors at 2 institutions in 1 country.

Meyer B JacksonDepartment of Physiology, University of Wisconsin School of Medicine and Public Health, 1300 University Avenue, Madison,WI 53706, USA. mjackson@physiology.wisc.edu
Edwin R Chapman
Howard Hughes Medical Institute · USUniversity of Wisconsin–Madison · US

Funding

Synaptotagmin C2B Domain as a Ca2+ Sensing ModuleR01MH061876 · NIMH · UNIVERSITY OF WISCONSIN-MADISON · PI Edwin R Chapman · 2002 to 2026
$7.7M
Single-Channel Studies of the Fusion PoreR01NS044057 · NINDS · UNIVERSITY OF WISCONSIN-MADISON · PI JACKSON, MEYER B. · 2002 to 2022
$5.7M
MEMBRANE EXCITABILITY AND SECRETION FROM NERVE ENDINGSR37NS030016 · NINDS · UNIVERSITY OF WISCONSIN-MADISON · PI JACKSON, MEYER B. · 2001 to 2007
$2.2M
SYNAPTOTAGMIN IN EXCITATION/SECRETION COUPLINGR01GM056827 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI CHAPMAN, EDWIN R · 1998 to 2006
$1.8M
MEMBRANE EXCITABILITY AND SECRETION FROM NERVE ENDINGSR01NS030016 · NINDS · UNIVERSITY OF WISCONSIN MADISON · PI JACKSON, MEYER B. · 1992 to 2000
$159k
Howard Hughes Medical InstituteNIGMS NIH HHS GM56827NIGMS NIH HHS R01 GM056827NIMH NIH HHS MH61876NIMH NIH HHS R01 MH061876NINDS NIH HHS NS30016NINDS NIH HHS NS44057NINDS NIH HHS R01 NS030016NINDS NIH HHS R01 NS044057NINDS NIH HHS R37 NS030016
6 · The paper itself

Abstract

The aqueous compartment inside a vesicle makes its first connection with the extracellular fluid through an intermediate structure termed the exocytotic fusion pore. Progress in exocytosis can be measured in terms of the formation and growth of the fusion pore. The fusion pore has become a major focus of research in exocytosis; sensitive biophysical measurements have provided various glimpses of what it looks like and how it behaves. Some of the principal questions about the molecular mechanism of exocytosis can be cast explicitly in terms of properties and transitions of fusion pores. This Review will present current knowledge about fusion pores in Ca(2+)-triggered exocytosis, highlight recent advances and relate questions about fusion pores to broader issues concerning how cells regulate exocytosis and how nerve terminals release neurotransmitter.

Indexed as

ExocytosisCalciumCell MembraneElectric CapacitanceMembrane FusionMembrane Fusion ProteinsModels, BiologicalMutagenesisSynaptic TransmissionTransport VesiclesCalciumMembrane Fusion Proteins

Identifiers

PMID18596819
PMCPMC2914174
OpenAlexW2068323391

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.