ArticleNature communications2020
Resolving kinetic intermediates during the regulated assembly and disassembly of fusion pores.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
What it found
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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
33 citing papers in PubMed, 55 citations in OpenAlex.
- Munc18 reprograms the intrinsic neuronal SNARE complex assembly pathway.bioRxiv : the preprint server for biology · 2026Article
- NSF is required for diverse endocytic modes by promoting fusion and fission pore closure in secretory cells.iScience · 2026Article
- From Population Averaging to Single Event Resolution: Evolution of Sensing Platforms for Membrane Fusion.Sensors (Basel, Switzerland) · 2026Review
- ATPase N-ethylmaleimide-sensitive factor mediated calcium dependent fusion pore closure and endocytosis.Communications biology · 2026Article
- Formation, Organization, and Maintenance of Synaptic Vesicle Pools: From Molecules to Structure and Dynamics.Advances in neurobiology · 2026Review
- Fusion Pores as Regulators of Quantal Size and Cellular Physiology.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- Synergistic regulation of fusion pore opening and dilation by SNARE and synaptotagmin-1.Journal of molecular cell biology · 2024Article
- Differential SNARE chaperoning by Munc13-1 and Munc18-1 dictates fusion pore fate at the release site.Nature communications · 2024Article
- Synaptobrevin2 monomers and dimers differentially engage to regulate the functional trans-SNARE assembly.Life science alliance · 2024Article
- Article
- Mechanisms of SNARE proteins in membrane fusion.Nature reviews. Molecular cell biology · 2024Review
- The role of synaptic protein NSF in the development and progression of neurological diseases.Frontiers in neuroscience · 2024Review
- Synaptotagmin-7 outperforms synaptotagmin-1 to promote the formation of large, stable fusion pores via robust membrane penetration.Nature communications · 2023Article
- Three membrane fusion pore families determine the pathway to pore dilation.Biophysical journal · 2023Article
- Designer Nanodiscs to Probe and Reprogram Membrane Biology in Synapses.Journal of molecular biology · 2023Review
- High-speed imaging reveals the bimodal nature of dense core vesicle exocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- The beginning and the end of SNARE-induced membrane fusion.FEBS open bio · 2022Review
- Vesicle trafficking and vesicle fusion: mechanisms, biological functions, and their implications for potential disease therapy.Molecular biomedicine · 2022Review
- Energetics, kinetics, and pathways of SNARE assembly in membrane fusion.Critical reviews in biochemistry and molecular biology · 2022Review
- VAMP2 and synaptotagmin mobility in chromaffin granule membranes: implications for regulated exocytosis.Molecular biology of the cell · 2022Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The opening of a fusion pore during exocytosis creates the first aqueous connection between the lumen of a vesicle and the extracellular space. Soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) mediate the formation of these dynamic structures, and their kinetic transitions are tightly regulated by accessory proteins at the synapse. Here, we utilize two single molecule approaches, nanodisc-based planar bilayer electrophysiology and single-molecule FRET, to address the relationship between SNARE complex assembly and rapid (micro-millisecond) fusion pore transitions, and to define the role of accessory proteins. Synaptotagmin (syt) 1, a major Ca
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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 Socratic graph.