"SNARE Proteins" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
A superfamily of small proteins which are involved in the MEMBRANE FUSION events, intracellular protein trafficking and secretory processes. They share a homologous SNARE motif. The SNARE proteins are divided into subfamilies: QA-SNARES; QB-SNARES; QC-SNARES; and R-SNARES. The formation of a SNARE complex (composed of one each of the four different types SNARE domains (Qa, Qb, Qc, and R)) mediates MEMBRANE FUSION. Following membrane fusion SNARE complexes are dissociated by the NSFs (N-ETHYLMALEIMIDE-SENSITIVE FACTORS), in conjunction with SOLUBLE NSF ATTACHMENT PROTEIN, i.e., SNAPs (no relation to SNAP 25.)
Descriptor ID |
D050600
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MeSH Number(s) |
D12.776.543.512.249 D12.776.543.990.775
|
Concept/Terms |
SNARE Proteins- SNARE Proteins
- Receptor, SNAP
- SNAP Receptor
- SNARE
- SNAREs
- Soluble N-ethylmaleimide-Sensitive-Factor Attachment Protein Receptor
- Soluble N ethylmaleimide Sensitive Factor Attachment Protein Receptor
- NSF Attachment Protein Receptor
- SNAP Receptors
Vesicle SNARE Proteins- Vesicle SNARE Proteins
- SNARE Proteins, Vesicle
- v-SNAREs
- v SNAREs
- Vesicular SNARE Proteins
- SNARE Proteins, Vesicular
- v-SNARE
|
Below are MeSH descriptors whose meaning is more general than "SNARE Proteins".
Below are MeSH descriptors whose meaning is more specific than "SNARE Proteins".
This graph shows the total number of publications written about "SNARE Proteins" by people in this website by year, and whether "SNARE Proteins" was a major or minor topic of these publications.
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Year | Major Topic | Minor Topic | Total |
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1996 | 0 | 1 | 1 |
2000 | 0 | 1 | 1 |
2002 | 0 | 4 | 4 |
2004 | 0 | 1 | 1 |
2005 | 1 | 1 | 2 |
2006 | 1 | 0 | 1 |
2007 | 1 | 2 | 3 |
2009 | 1 | 1 | 2 |
2015 | 0 | 1 | 1 |
2016 | 2 | 1 | 3 |
2017 | 2 | 0 | 2 |
2018 | 1 | 0 | 1 |
2020 | 0 | 1 | 1 |
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Below are the most recent publications written about "SNARE Proteins" by people in Profiles.
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Neuronal BIN1 Regulates Presynaptic Neurotransmitter Release and Memory Consolidation. Cell Rep. 2020 03 10; 30(10):3520-3535.e7.
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NSF-mediated disassembly of on- and off-pathway SNARE complexes and inhibition by complexin. Elife. 2018 07 09; 7.
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The primed SNARE-complexin-synaptotagmin complex for neuronal exocytosis. Nature. 2017 08 24; 548(7668):420-425.
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Molecular Mechanisms of Synaptic Vesicle Priming by Munc13 and Munc18. Neuron. 2017 Aug 02; 95(3):591-607.e10.
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Advances in X-ray free electron laser (XFEL) diffraction data processing applied to the crystal structure of the synaptotagmin-1 / SNARE complex. Elife. 2016 10 12; 5.
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N-terminal domain of complexin independently activates calcium-triggered fusion. Proc Natl Acad Sci U S A. 2016 08 09; 113(32):E4698-707.
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Complexin induces a conformational change at the membrane-proximal C-terminal end of the SNARE complex. Elife. 2016 06 02; 5.
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Recent Advances in Deciphering the Structure and Molecular Mechanism of the AAA+ ATPase N-Ethylmaleimide-Sensitive Factor (NSF). J Mol Biol. 2016 05 08; 428(9 Pt B):1912-26.
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Synaptotagmin 1 and SNAREs form a complex that is structurally heterogeneous. J Mol Biol. 2011 Jan 21; 405(3):696-706.
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Intracellular bacteria encode inhibitory SNARE-like proteins. PLoS One. 2009 Oct 12; 4(10):e7375.