ArticleNature2015
Mechanistic insights into the recycling machine of the SNARE complex.
Article in Nature, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 180 papers.
What it found
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Who cites it
180 citing papers in PubMed, 261 citations in OpenAlex.
- PETIMOT: a novel framework for inferring protein motions from sparse data using SE(3)-equivariant graph neural networks.Acta crystallographica. Section D, Structural biology · 2026Article
- Synaptic aging and neurodegeneration: the role of synaptic vesicle dynamics and neurotransmitter imbalance.Biogerontology · 2026Review
- A pathogenic mutation in α-SNAP impairs membrane lipid binding by concealing a critical hydrophobic loop.Communications biology · 2026Article
- A PIP2-stabilized syntaxin-1a structure mapped with transition metal ion FRET and unnatural fluorescent amino acids at the plasma membrane.Structure (London, England : 1993) · 2026Article
- Functional assembly of the Qc-SNARE with Sec18 and Sec17 on membranes.Molecular biology of the cell · 2026Article
- Recent Structural Insights into the Molecular Architecture of Synapses.Advances in neurobiology · 2026Review
- Structural remodeling of target-SNARE protein complexes by NSF enables synaptic transmission.Nature communications · 2025Article
- SNARE disassembly requires Sec18/NSF side loading.Nature structural & molecular biology · 2025Article
- Kinetic Modeling of Covalent Inhibition: Effects of Rapidly Fluctuating Intermediate States.Journal of chemical information and modeling · 2025Article
- Structural remodeling of target-SNARE protein complexes by NSF enables synaptic transmission.bioRxiv : the preprint server for biology · 2025Article
- Sec18 ATP hydrolysis selectively releases Sec17 fromMolecular biology of the cell · 2025Article
- SNARE disassembly requires Sec18/NSF side-loading.bioRxiv : the preprint server for biology · 2025Article
- Dynamic regulation of vesicle pools in a detailed spatial model of the complete synaptic vesicle cycle.Science advances · 2025Article
- Evolutionary duplication of the leishmanial adaptor protein α-SNAP plays a role in its pathogenicity.The Journal of biological chemistry · 2025Article
- Single-molecule two- and three-colour FRET studies reveal a transition state in SNARE disassembly by NSF.Nature communications · 2025Article
- Spectroscopic Methods for Detecting Conformational Changes During Sec18-Lipid 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
- After their membrane assembly, Sec18 (NSF) and Sec17 (SNAP) promote membrane fusion.Molecular biology of the cell · 2024Article
- Membrane fusion reactions limited by defective SNARE zippering or stiff lipid fatty acyl composition have distinct requirements for Sec17, Sec18, and adenine nucleotide.bioRxiv : the preprint server for biology · 2024Article
- Histamine synthesis and transport are coupled in axon terminals via a dual quality control system.The EMBO journal · 2024Article
120 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
7 authors at 3 institutions in 1 country.
Funding
Abstract
Evolutionarily conserved SNARE (soluble N-ethylmaleimide sensitive factor attachment protein receptors) proteins form a complex that drives membrane fusion in eukaryotes. The ATPase NSF (N-ethylmaleimide sensitive factor), together with SNAPs (soluble NSF attachment protein), disassembles the SNARE complex into its protein components, making individual SNAREs available for subsequent rounds of fusion. Here we report structures of ATP- and ADP-bound NSF, and the NSF/SNAP/SNARE (20S) supercomplex determined by single-particle electron cryomicroscopy at near-atomic to sub-nanometre resolution without imposing symmetry. Large, potentially force-generating, conformational differences exist between ATP- and ADP-bound NSF. The 20S supercomplex exhibits broken symmetry, transitioning from six-fold symmetry of the NSF ATPase domains to pseudo four-fold symmetry of the SNARE complex. SNAPs interact with the SNARE complex with an opposite structural twist, suggesting an unwinding mechanism. The interfaces between NSF, SNAPs, and SNAREs exhibit characteristic electrostatic patterns, suggesting how one NSF/SNAP species can act on many different SNARE complexes.
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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 OpenQuestion graph.