pubmed-article:8247129 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8247129 | lifeskim:mentions | umls-concept:C1154474 | lld:lifeskim |
pubmed-article:8247129 | lifeskim:mentions | umls-concept:C0288881 | lld:lifeskim |
pubmed-article:8247129 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:8247129 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
pubmed-article:8247129 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
pubmed-article:8247129 | lifeskim:mentions | umls-concept:C2825311 | lld:lifeskim |
pubmed-article:8247129 | lifeskim:mentions | umls-concept:C2349209 | lld:lifeskim |
pubmed-article:8247129 | lifeskim:mentions | umls-concept:C1549781 | lld:lifeskim |
pubmed-article:8247129 | lifeskim:mentions | umls-concept:C1334043 | lld:lifeskim |
pubmed-article:8247129 | pubmed:issue | 6453 | lld:pubmed |
pubmed-article:8247129 | pubmed:dateCreated | 1993-12-30 | lld:pubmed |
pubmed-article:8247129 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8247129 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8247129 | pubmed:abstractText | Three synaptic proteins, syntaxin, SNAP-25 and synaptobrevin, were recently identified as targets of clostridial neurotoxins that irreversibly inhibit synaptic vesicle fusion. Experiments searching for membrane receptors for N-ethylmaleimide-sensitive fusion protein (NSF), which has an important role in membrane fusion, revealed an ATP-dependent interaction of the same three synaptic proteins with NSF and its soluble attachment proteins. Thus, two independent approaches identify syntaxin, synaptobrevin and SNAP-25 as components of the synaptic vesicle fusion machinery, but their mode of action is unclear. We have now discovered a brain protein of relative molecular mass 67,000 (67K) which binds stably to syntaxin. Amino-acid sequencing and complementary DNA cloning revealed that the 67K protein is encoded by the mammalian homologue of the Caenorhabditis elegans gene unc-18. In C. elegans, unc-18 belongs to a group of genes defined by mutations with a paralytic phenotype and accumulations of acetylcholine, suggesting a defect in neurotransmitter release. The binding of the mammalian homologue of unc-18 (Munc-18) to syntaxin requires the N terminus of syntaxin whereas that of SNAP-25 involves a more C-terminal sequence. Our data suggest that Munc-18 is a previously unidentified essential component of the synaptic vesicle fusion protein complex. | lld:pubmed |
pubmed-article:8247129 | pubmed:language | eng | lld:pubmed |
pubmed-article:8247129 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8247129 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:8247129 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8247129 | pubmed:month | Nov | lld:pubmed |
pubmed-article:8247129 | pubmed:issn | 0028-0836 | lld:pubmed |
pubmed-article:8247129 | pubmed:author | pubmed-author:HataYY | lld:pubmed |
pubmed-article:8247129 | pubmed:author | pubmed-author:SlaughterC... | lld:pubmed |
pubmed-article:8247129 | pubmed:author | pubmed-author:SüdhofT CTC | lld:pubmed |
pubmed-article:8247129 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8247129 | pubmed:day | 25 | lld:pubmed |
pubmed-article:8247129 | pubmed:volume | 366 | lld:pubmed |
pubmed-article:8247129 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8247129 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8247129 | pubmed:pagination | 347-51 | lld:pubmed |
pubmed-article:8247129 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:8247129 | pubmed:year | 1993 | lld:pubmed |
pubmed-article:8247129 | pubmed:articleTitle | Synaptic vesicle fusion complex contains unc-18 homologue bound to syntaxin. | lld:pubmed |
pubmed-article:8247129 | pubmed:affiliation | Howard Hughes Medical Institute, University of Texas Southwestern Medical School, Dallas 75235. | lld:pubmed |
pubmed-article:8247129 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8247129 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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