Source:http://linkedlifedata.com/resource/pubmed/id/16793273
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
2006-7-19
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pubmed:abstractText |
Chemical synapses are asymmetric cell junctions that mediate communication between neurons. Multidomain scaffolding proteins of the Shank family act as major organizing elements of the "postsynaptic density"--that is, the cytoskeletal protein matrix associated with the postsynaptic membrane. A recent study has shown that the C-terminal sterile alpha-motif or "SAM domain" of Shank3 (also known as ProSAP2) can form two-dimensional sheets of helical fibers. Assembly and packaging of these fibers are markedly enhanced by the presence of Zn2+ ions. Zn2+ can be released together with glutamate from synaptic vesicles and can enter the postsynaptic cell through specific ionotropic receptors. Based on these observations, we propose a new model of synaptic plasticity in which Zn2+ influx directly and instantly modulates the structure and function of the postsynaptic density.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0968-0004
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
31
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
366-73
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pubmed:dateRevised |
2009-8-18
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pubmed:meshHeading |
pubmed-meshheading:16793273-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:16793273-Animals,
pubmed-meshheading:16793273-Models, Neurological,
pubmed-meshheading:16793273-Neuronal Plasticity,
pubmed-meshheading:16793273-Protein Structure, Secondary,
pubmed-meshheading:16793273-Protein Structure, Tertiary,
pubmed-meshheading:16793273-Rats,
pubmed-meshheading:16793273-Signal Transduction,
pubmed-meshheading:16793273-Synapses,
pubmed-meshheading:16793273-Synaptic Transmission,
pubmed-meshheading:16793273-Zinc
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pubmed:year |
2006
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pubmed:articleTitle |
A role for zinc in postsynaptic density asSAMbly and plasticity?
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pubmed:affiliation |
Department of Neurochemistry and Molecular Biology, Leibniz Institute for Neurobiology, Brenneckestrasse 6, 39118 Magdeburg, Germany. gundelfinger@ifn-magdeburg.de
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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