| pubmed-article:15044754 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15044754 | lifeskim:mentions | umls-concept:C0025246 | lld:lifeskim |
| pubmed-article:15044754 | lifeskim:mentions | umls-concept:C0084697 | lld:lifeskim |
| pubmed-article:15044754 | lifeskim:mentions | umls-concept:C0300824 | lld:lifeskim |
| pubmed-article:15044754 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:15044754 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:15044754 | lifeskim:mentions | umls-concept:C0183362 | lld:lifeskim |
| pubmed-article:15044754 | pubmed:issue | 5669 | lld:pubmed |
| pubmed-article:15044754 | pubmed:dateCreated | 2004-4-16 | lld:pubmed |
| pubmed-article:15044754 | pubmed:abstractText | We investigated the effect of synaptotagmin I on membrane fusion mediated by neuronal SNARE proteins, SNAP-25, syntaxin, and synaptobrevin, which were reconstituted into vesicles. In the presence of Ca2+, the cytoplasmic domain of synaptotagmin I (syt) strongly stimulated membrane fusion when synaptobrevin densities were similar to those found in native synaptic vesicles. The Ca2+ dependence of syt-stimulated fusion was modulated by changes in lipid composition of the vesicles and by a truncation that mimics cleavage of SNAP-25 by botulinum neurotoxin A. Stimulation of fusion was abolished by disrupting the Ca2+-binding activity, or by severing the tandem C2 domains, of syt. Thus, syt and SNAREs are likely to represent the minimal protein complement for Ca2+-triggered exocytosis. | lld:pubmed |
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| pubmed-article:15044754 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:15044754 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15044754 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15044754 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:15044754 | pubmed:issn | 1095-9203 | lld:pubmed |
| pubmed-article:15044754 | pubmed:author | pubmed-author:ChapmanEdwin... | lld:pubmed |
| pubmed-article:15044754 | pubmed:author | pubmed-author:WeberThomasT | lld:pubmed |
| pubmed-article:15044754 | pubmed:author | pubmed-author:TuckerWard... | lld:pubmed |
| pubmed-article:15044754 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:15044754 | pubmed:day | 16 | lld:pubmed |
| pubmed-article:15044754 | pubmed:volume | 304 | lld:pubmed |
| pubmed-article:15044754 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15044754 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15044754 | pubmed:pagination | 435-8 | lld:pubmed |
| pubmed-article:15044754 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:15044754 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15044754 | pubmed:articleTitle | Reconstitution of Ca2+-regulated membrane fusion by synaptotagmin and SNAREs. | lld:pubmed |
| pubmed-article:15044754 | pubmed:affiliation | Department of Physiology, University of Wisconsin, Madison, WI 53706, USA. | lld:pubmed |
| pubmed-article:15044754 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15044754 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:15044754 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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