SNARE Proteins
"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
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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
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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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1998 | 0 | 1 | 1 | 1999 | 0 | 4 | 4 | 2001 | 0 | 1 | 1 | 2003 | 0 | 1 | 1 | 2004 | 0 | 1 | 1 | 2006 | 0 | 1 | 1 | 2010 | 1 | 1 | 2 | 2011 | 0 | 1 | 1 | 2012 | 1 | 0 | 1 | 2013 | 2 | 1 | 3 | 2014 | 0 | 1 | 1 | 2015 | 0 | 1 | 1 | 2018 | 1 | 0 | 1 | 2019 | 3 | 1 | 4 | 2021 | 1 | 0 | 1 |
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Below are the most recent publications written about "SNARE Proteins" by people in Profiles.
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Liu Y, Wan C, Rathore SS, Stowell MHB, Yu H, Shen J. SNARE Zippering Is Suppressed by a Conformational Constraint that Is Removed by v-SNARE Splitting. Cell Rep. 2021 01 12; 34(2):108611.
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Rathore SS, Liu Y, Yu H, Wan C, Lee M, Yin Q, Stowell MHB, Shen J. Intracellular Vesicle Fusion Requires a Membrane-Destabilizing Peptide Located at the Juxtamembrane Region of the v-SNARE. Cell Rep. 2019 12 24; 29(13):4583-4592.e3.
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Aivazidis S, Jain A, Rauniyar AK, Anderson CC, Marentette JO, Orlicky DJ, Fritz KS, Harris PS, Siegel D, Maclean KN, Roede JR. SNARE proteins rescue impaired autophagic flux in Down syndrome. PLoS One. 2019; 14(11):e0223254.
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Liu Q, Sinnen BL, Boxer EE, Schneider MW, Grybko MJ, Buchta WC, Gibson ES, Wysoczynski CL, Ford CP, Gottschalk A, Aoto J, Tucker CL, Kennedy MJ. A Photoactivatable Botulinum Neurotoxin for Inducible Control of Neurotransmission. Neuron. 2019 03 06; 101(5):863-875.e6.
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Yu H, Crisman L, Stowell MHB, Shen J. Functional Reconstitution of Intracellular Vesicle Fusion Using Purified SNAREs and Sec1/Munc18 (SM) Proteins. Methods Mol Biol. 2019; 1860:237-249.
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Yu H, Shen C, Liu Y, Menasche BL, Ouyang Y, Stowell MHB, Shen J. SNARE zippering requires activation by SNARE-like peptides in Sec1/Munc18 proteins. Proc Natl Acad Sci U S A. 2018 09 04; 115(36):E8421-E8429.
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Shen C, Rathore SS, Yu H, Gulbranson DR, Hua R, Zhang C, Schoppa NE, Shen J. The trans-SNARE-regulating function of Munc18-1 is essential to synaptic exocytosis. Nat Commun. 2015 Nov 17; 6:8852.
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Yu H, Rathore SS, Gulbranson DR, Shen J. The N- and C-terminal domains of tomosyn play distinct roles in soluble N-ethylmaleimide-sensitive factor attachment protein receptor binding and fusion regulation. J Biol Chem. 2014 Sep 12; 289(37):25571-80.
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Yu H, Rathore SS, Lopez JA, Davis EM, James DE, Martin JL, Shen J. Comparative studies of Munc18c and Munc18-1 reveal conserved and divergent mechanisms of Sec1/Munc18 proteins. Proc Natl Acad Sci U S A. 2013 Aug 27; 110(35):E3271-80.
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Yu H, Rathore SS, Shen J. Synip arrests soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE)-dependent membrane fusion as a selective target membrane SNARE-binding inhibitor. J Biol Chem. 2013 Jun 28; 288(26):18885-93.
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