| pubmed-article:1671174 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1671174 | lifeskim:mentions | umls-concept:C0039065 | lld:lifeskim |
| pubmed-article:1671174 | lifeskim:mentions | umls-concept:C1622186 | lld:lifeskim |
| pubmed-article:1671174 | lifeskim:mentions | umls-concept:C0087044 | lld:lifeskim |
| pubmed-article:1671174 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:1671174 | lifeskim:mentions | umls-concept:C0009609 | lld:lifeskim |
| pubmed-article:1671174 | lifeskim:mentions | umls-concept:C0598964 | lld:lifeskim |
| pubmed-article:1671174 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:1671174 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:1671174 | pubmed:dateCreated | 1991-2-28 | lld:pubmed |
| pubmed-article:1671174 | pubmed:abstractText | Synapsin I is a neuron-specific phosphoprotein that binds to small synaptic vesicles and actin filaments in a phosphorylation-dependent fashion. It has been hypothesized that dephosphorylated synapsin I inhibits neurotransmitter release either by forming a cage around synaptic vesicles (cage model) or by anchoring them to the F-actin cytoskeleton of the nerve terminal (crosslinking model). Computer modeling was performed with the aim of testing the impact of phosphorylation on the molecular interactions of synapsin I within the nerve terminal. The results of the simulation experiments demonstrate that in the crosslinking model the phosphorylation of synapsin I causes a severalfold increase in the number of vesicles released from the cytoskeleton and that in the cage model the phosphorylation induces a 2-fold increase in the number of vesicles bearing one or more unsaturated synapsin I binding sites. These data are compatible with the view that the function of synapsin I in the short-term regulation of neurotransmitter release is to induce a phosphorylation-dependent transition of synaptic vesicles from a "reserve pool" to a readily "releasable pool" of vesicles. | lld:pubmed |
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| pubmed-article:1671174 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1671174 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1671174 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1671174 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1671174 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:1671174 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:1671174 | pubmed:author | pubmed-author:GreengardPP | lld:pubmed |
| pubmed-article:1671174 | pubmed:author | pubmed-author:BenfenatiFF | lld:pubmed |
| pubmed-article:1671174 | pubmed:author | pubmed-author:ValtortaFF | lld:pubmed |
| pubmed-article:1671174 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1671174 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:1671174 | pubmed:volume | 88 | lld:pubmed |
| pubmed-article:1671174 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1671174 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1671174 | pubmed:pagination | 575-9 | lld:pubmed |
| pubmed-article:1671174 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:1671174 | pubmed:meshHeading | pubmed-meshheading:1671174-... | lld:pubmed |
| pubmed-article:1671174 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1671174 | pubmed:articleTitle | Computer modeling of synapsin I binding to synaptic vesicles and F-actin: implications for regulation of neurotransmitter release. | lld:pubmed |
| pubmed-article:1671174 | pubmed:affiliation | Institute of Human Physiology, University of Modena, Italy. | lld:pubmed |
| pubmed-article:1671174 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1671174 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1671174 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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