ReviewJournal of molecular neuroscience : MN2012
SNARE requirements en route to exocytosis: from many to few.
Review in Journal of molecular neuroscience : MN, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- SNAP-25 disease variants affect synaptic transmission by destabilizing SNARE complexes within a multimeric SNARE ring.Cell reports · 2026Article
- Article
- SNARE Proteins in Synaptic Vesicle Fusion.Advances in neurobiology · 2023Article
- Overcoming presynaptic effects of VAMP2 mutations with 4-aminopyridine treatment.Human mutation · 2020Article
- Article
- The high-affinity calcium sensor synaptotagmin-7 serves multiple roles in regulated exocytosis.The Journal of general physiology · 2018Review
- v-SNARE function in chromaffin cells.Pflugers Archiv : European journal of physiology · 2018Review
- t-SNARE Transmembrane Domain Clustering Modulates Lipid Organization and Membrane Curvature.Journal of the American Chemical Society · 2017Article
- REEP6 mediates trafficking of a subset of Clathrin-coated vesicles and is critical for rod photoreceptor function and survival.Human molecular genetics · 2017Article
- A stochastic model of active zone material mediated synaptic vesicle docking and priming at resting active zones.Scientific reports · 2017Article
- The Structure of the Synaptic Vesicle-Plasma Membrane Interface Constrains SNARE Models of Rapid, Synchronous Exocytosis at Nerve Terminals.Frontiers in molecular neuroscience · 2017Review
- Variable priming of a docked synaptic vesicle.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- The mystery of the fusion pore.Nature structural & molecular biology · 2016Article
- Synaptobrevin Transmembrane Domain Dimerization Studied by Multiscale Molecular Dynamics Simulations.Biophysical journal · 2015Article
- Article
- The synaptotagmin juxtamembrane domain is involved in neuroexocytosis.FEBS open bio · 2015Article
- Microsecond dissection of neurotransmitter release: SNARE-complex assembly dictates speed and Ca²⁺ sensitivity.Neuron · 2014Article
- The blockade of the neurotransmitter release apparatus by botulinum neurotoxins.Cellular and molecular life sciences : CMLS · 2014Review
- Function suggests nano-structure: towards a unified theory for secretion rate, a statistical mechanics approach.Journal of the Royal Society, Interface · 2013Article
- Review
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Although it has been known for almost two decades that the ternary complex of N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) constitutes the functional unit driving membrane fusion, our knowledge about the dynamical arrangement and organization of SNARE proteins and their complexes before and during vesicle exocytosis is still limited. Here, we review recent progress in this expanding field with emphasis on the question of fusion complex stoichiometry, i.e., how many SNARE proteins and complexes are needed for the fusion of a vesicle with the plasma membrane.
Indexed as
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22427188What 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.