Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Disassembly of the reconstituted synaptic vesicle membrane fusion complex in vitro.

The EMBO journal - 15 May 1995

Hayashi T, Yamasaki S, Nauenburg S, Binz T, Niemann H

Abstract excerpt

The interaction of the presynaptic membrane proteins SNAP-25 and syntaxin with the synaptic vesicle protein synaptobrevin (VAMP) plays a key role in the regulated exocytosis of neurotransmitters. Clostridial neurotoxins, which proteolyze these polypeptides, are potent inhibitors of neurotransmission. The cytoplasmic domains of the three membrane proteins join into a tight SDS-resistant complex (Hayashi et al.,...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Base Sequence
Share to Carrier Proteins
Share to Membrane Proteins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Molecular Sequence Data

Share to Mutation

Share to Protein Binding

Share to Protein Conformation

Share to Recombinant Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 7774590
DOI: 10.1002/j.1460-2075.1995.tb07226.x
PMCID: PMC398339

Genes

NSF
SDS

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Disassembly of the reconstituted synaptic vesicle membrane fusion complex in vitro.PMID 7774590Read ↗

Rapid and selective binding to the synaptic SNARE complex suggests a modulatory role of complexins in neuroexocytosis.Semantic proximity Read ↗

A conserved membrane attachment site in alpha-SNAP facilitates N-ethylmaleimide-sensitive factor (NSF)-driven SNARE complex disassembly.Semantic proximity Read ↗

NSF-mediated disassembly of on- and off-pathway SNARE complexes and inhibition by complexin.Semantic proximity Read ↗

Temperature-sensitive paralytic mutations demonstrate that synaptic exocytosis requires SNARE complex assembly and disassembly.Semantic proximity Read ↗

A discontinuous SNAP-25 C-terminal coil supports exocytosis.Semantic proximity Read ↗

Gβγ inhibits exocytosis via interaction with critical residues on soluble N-ethylmaleimide-sensitive factor attachment protein-25.Semantic proximity Read ↗

Regulation of neuronal SNARE assembly by the membrane.Semantic proximity Read ↗

SNARE-complex disassembly by NSF follows synaptic-vesicle fusion.Semantic proximity Read ↗

SNARE complex formation is triggered by Ca2+ and drives membrane fusion.Semantic proximity Read ↗

SNARE function analyzed in synaptobrevin/VAMP knockout mice.Semantic proximity Read ↗

Synaptobrevin/vesicle-associated membrane protein (VAMP) of Aplysia californica: structure and proteolysis by tetanus toxin and botulinal neurotoxins type D and F.Semantic proximity Read ↗

Complexin is able to bind to SNARE core complexes in different assembled states with distinct affinity.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.