ReviewFEBS letters2018
The fusion pore, 60 years after the first cartoon.
Review in FEBS letters, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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.
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.
Who cites it
37 citing papers in PubMed.
- Fusion Pores as Regulators of Quantal Size and Cellular Physiology.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- The adhesion plaque mediates fluid discharge and duplication of the contractile vacuole complex in Trypanosoma cruzi.Journal of cell science · 2025Article
- Membrane fusion and budding.Biophysical journal · 2025Article
- Vesicle docking and fusion pore modulation by the neuronal calcium sensor Synaptotagmin-1.Biophysical journal · 2025Article
- Unraveling the nature of physicochemical and biological processes underlying vesicular exocytotic release events through modeling of amperometric current spikes.QRB discovery · 2025Review
- Quantitative assessment of the nanoanatomy of the contractile vacuole complex inLife science alliance · 2024Article
- Vesicle docking and fusion pore modulation by the neuronal calcium sensor Synaptotagmin-1.bioRxiv : the preprint server for biology · 2024Article
- Cell Membrane Tension Gradients, Membrane Flows, and Cellular Processes.Physiology (Bethesda, Md.) · 2024Review
- Synaptobrevin2 monomers and dimers differentially engage to regulate the functional trans-SNARE assembly.Life science alliance · 2024Article
- Mechanisms of SNARE proteins in membrane fusion.Nature reviews. Molecular cell biology · 2024Review
- Membrane transformations of fusion and budding.Nature communications · 2024Review
- Fusion pore dynamics of large secretory vesicles define a distinct mechanism of exocytosis.The Journal of cell biology · 2023Article
- How micron-sized exocrine vesicles release content: A comparison with sub-micron endocrine vesicles.The Journal of cell biology · 2023Article
- Ca2+ and cAMP open differentially dilating synaptic fusion pores.Journal of cell science · 2023Article
- Patch Amperometry and Intracellular Patch Electrochemistry.Methods in molecular biology (Clifton, N.J.) · 2023Article
- α-Synuclein is required for sperm exocytosis at a post-fusion stage.Frontiers in cell and developmental biology · 2023Article
- PI(4,5)PAdvances in experimental medicine and biology · 2023Article
- The beginning and the end of SNARE-induced membrane fusion.FEBS open bio · 2022Review
- Illuminating membrane structural dynamics of fusion and endocytosis with advanced light imaging techniques.Biochemical Society transactions · 2022Review
- Stability profile of the neuronal SNARE complex reflects its potency to drive fast membrane fusion.Biophysical journal · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Neurotransmitter release occurs in the form of quantal events by fusion of secretory vesicles with the plasma membrane, and begins with the formation of a fusion pore that has a conductance similar to that of a large ion channel or gap junction. In this review, we propose mechanisms of fusion pore formation and discuss their implications for fusion pore structure and function. Accumulating evidence indicates a direct role of soluble N-ethylmaleimide-sensitive-factor attachment receptor proteins in the opening of fusion pores. Fusion pores are likely neither protein channels nor purely lipid, but are of proteolipidic composition. Future perspectives to gain better insight into the molecular structure of fusion pores are discussed.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.