ArticleNature protocols2012
A single vesicle-vesicle fusion assay for in vitro studies of SNAREs and accessory proteins.
Article in Nature protocols, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 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
65 citing papers in PubMed, 125 citations in OpenAlex.
- Single-molecule DNA flow-stretch assays for high-throughput DNA-protein interaction studies.FEBS open bio · 2026Article
- Munc18 modulates syntaxin phase separation to promote exocytosis.Nature neuroscience · 2026Article
- Using multiscale molecular dynamics simulations to explore the fusion machinery underlying neurotransmitter release.Quarterly reviews of biophysics · 2025Review
- Fusogenic Nanoreactor-Based Detection of Extracellular Vesicle-derived miRNAs for Diagnosing Atherosclerosis.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- Mechanistic Insights into Synaptotagmin-1 Mediated Membrane Fusion and Interactions.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Exocyst stimulates multiple steps of exocytic SNARE complex assembly and vesicle fusion.Nature structural & molecular biology · 2025Article
- Article
- N-acetylation of α-synuclein enhances synaptic vesicle clustering mediated by α-synuclein and lysophosphatidylcholine.bioRxiv : the preprint server for biology · 2024Article
- VAMP2 chaperones α-synuclein in synaptic vesicle co-condensates.Nature cell biology · 2024Article
- A practical guide for fast implementation of SNARE-mediated liposome fusion.Biophysics reports · 2024Article
- Neutral lysophosphatidylcholine mediates α-synuclein-induced synaptic vesicle clustering.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Dynamic Fusion of Nucleic Acid Functionalized Nano-/Micro-Cell-Like Containments: From Basic Concepts to Applications.ACS nano · 2023Review
- Double-Transmembrane Domain of SNAREs Decelerates the Fusion by Increasing the Protein-Lipid Mismatch.Journal of molecular biology · 2023Article
- Measuring single-virus fusion kinetics using an assay for nucleic acid exposure.Biophysical journal · 2022Article
- The function of VAMP2 in mediating membrane fusion: An overview.Frontiers in molecular neuroscience · 2022Review
- Single-vesicle intensity and colocalization fluorescence microscopy to study lipid vesicle fusion, fission, and lipid exchange.Frontiers in molecular neuroscience · 2022Article
- Crowding-induced morphological changes in synthetic lipid vesicles determined using smFRET.Frontiers in bioengineering and biotechnology · 2022Article
- Lipid Species Dependent Vesicles Clustering Caused by alpha-Synuclein as Revealed by Single-Vesicle Imaging with Total Internal Reflection Fluorescence Microscopy.Biophysics reports · 2021Article
- Lipids and membrane-associated proteins in autophagy.Protein & cell · 2021Review
- The shape of pleomorphic virions determines resistance to cell-entry pressure.Nature microbiology · 2021Article
5 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 5 institutions in 3 countries.
Funding
Abstract
SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins are a highly regulated class of membrane proteins that drive the efficient merger of two distinct lipid bilayers into one interconnected structure. This protocol describes our fluorescence resonance energy transfer (FRET)-based single vesicle-vesicle fusion assays for SNAREs and accessory proteins. Both lipid-mixing (with FRET pairs acting as lipophilic dyes in the membranes) and content-mixing assays (with FRET pairs present on a DNA hairpin that becomes linear via hybridization to a complementary DNA) are described. These assays can be used to detect substages such as docking, hemifusion, and pore expansion and full fusion. The details of flow cell preparation, protein-reconstituted vesicle preparation, data acquisition and analysis are described. These assays can be used to study the roles of various SNARE proteins, accessory proteins and effects of different lipid compositions on specific fusion steps. The total time required to finish one round of this protocol is 3–6 d.
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.