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

SNAP-25 functional domains in SNARE core complex assembly and glutamate release of cerebellar granule cells.

The Journal of biological chemistry - 22 Sept 2000

Yang Y, Xia Z, Liu Y

Abstract excerpt

Synaptosomal associated protein of 25 kDa (SNAP-25) is a member of the SNARE protein complex that has been implicated in synaptic vesicle docking and fusion. In this report, we have generated SNAP-25 mutants and assayed their functions in SNARE complex formation and glutamate release from cultured rat cerebellar granule cells. In vitro binding studies show that a deletion mutant lacking the C-terminal 181-206...

Read the complete abstract on PubMed

Topics

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

Share to Cerebellum
Share to Glutamic Acid
Share to Nerve Tissue Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Neurons

Share to SNARE Proteins

Share to Synaptic Membranes

Share to Synaptosomal-Associated Protein 25

Share to Vesicular Transport Proteins

Source

Identifiers

PMID: 10882724
DOI: 10.1074/jbc.M003237200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

SNAP-25 functional domains in SNARE core complex assembly and glutamate release of cerebellar granule cells.PMID 10882724Read ↗

Developmentally regulated switch in alternatively spliced SNAP-25 isoforms alters facilitation of synaptic transmission.Semantic proximity Read ↗

SNAP-25 and gene-targeted mouse mutants.Semantic proximity Read ↗

SNAP-25 disease variants affect synaptic transmission by destabilizing SNARE complexes within a multimeric SNARE ring.Semantic proximity Read ↗

A dominant mutation in <i>Snap25</i> causes impaired vesicle trafficking, sensorimotor gating, and ataxia in the blind-drunk mouseSemantic proximity Read ↗

Regional and developmental brain expression patterns of SNAP25 splice variantsSemantic proximity Read ↗

SNAP25 disease mutations change the energy landscape for synaptic exocytosis due to aberrant SNARE interactions.Semantic proximity Read ↗

Differential control of the releasable vesicle pools by SNAP-25 splice variants and SNAP-23.Semantic proximity Read ↗

Structure of the chicken gene for SNAP-25 reveals duplicated exon encoding distinct isoforms of the protein.Semantic proximity Read ↗

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

SNAP-25: a novel candidate gene in psychiatric genetics.Semantic proximity Read ↗

Opposing functions of two sub-domains of the SNARE-complex in neurotransmission.Semantic proximity Read ↗

Two distinct effects on neurotransmission in a temperature-sensitive SNAP-25 mutant.Semantic proximity Read ↗

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