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

SNARE function analyzed in synaptobrevin/VAMP knockout mice.

Science (New York, N.Y.) - 2 Nov 2001

Schoch S, Deák F, Königstorfer A, Mozhayeva M, Sara Y, Südhof T C, Kavalali E T

Abstract excerpt

SNAREs (soluble NSF-attachment protein receptors) are generally acknowledged as central components of membrane fusion reactions, but their precise function has remained enigmatic. Competing hypotheses suggest roles for SNAREs in mediating the specificity of fusion, catalyzing fusion, or actually executing fusion. We generated knockout mice lacking synaptobrevin/VAMP 2, the vesicular SNARE protein responsible for...

Read the complete abstract on PubMed

Topics

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

Share to Potassium
Share to Membrane Fusion
Share to Presynaptic Terminals

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

Share to Prosencephalon

Share to R-SNARE Proteins

Share to SNARE Proteins

Share to Sucrose

Share to Synaptic Vesicles

Source

Identifiers

PMID: 11691998
DOI: 10.1126/science.1064335

Genes

NSF

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

SNARE function analyzed in synaptobrevin/VAMP knockout mice.PMID 11691998Read ↗

Structural determinants of synaptobrevin 2 function in synaptic vesicle fusion.Semantic proximity Read ↗

VAMP4 directs synaptic vesicles to a pool that selectively maintains asynchronous neurotransmission.Semantic proximity Read ↗

SNARE interactions in membrane trafficking: a perspective from mammalian central synapses.Semantic proximity Read ↗

Reconstitution of Ca2+-regulated membrane fusion by synaptotagmin and SNAREs.Semantic proximity Read ↗

Synaptotagmin C2A loop 2 mediates Ca2+-dependent SNARE interactions essential for Ca2+-triggered vesicle exocytosis.Semantic proximity Read ↗

synaptotagmin mutants reveal essential functions for the C2B domain in Ca2+-triggered fusion and recycling of synaptic vesicles in vivo.Semantic proximity Read ↗

Genetic and molecular analysis of the synaptotagmin family.Semantic proximity Read ↗

Binding of the complexin N terminus to the SNARE complex potentiates synaptic-vesicle fusogenicity.Semantic proximity Read ↗

Synaptotagmin-1 utilizes membrane bending and SNARE binding to drive fusion pore expansion.Semantic proximity Read ↗

Molecular origins of synaptotagmin 1 activities on vesicle docking and fusion pore opening.Semantic proximity Read ↗

How does synaptotagmin trigger neurotransmitter release?Semantic proximity Read ↗

Synaptotagmin I functions as a calcium sensor to synchronize neurotransmitter release.Semantic proximity Read ↗

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