Source:http://linkedlifedata.com/resource/pubmed/id/14630214
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
2003-11-21
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pubmed:abstractText |
Cell adhesion molecules of the immunoglobulin superfamily (IgCAMS) play pivotal roles during synapse development and remodeling, being required in both activity-dependent and activity independent aspects of these processes. Recent advances using the fruit fly neuromuscular junction, as well as the mollusk Aplysia californica, have provided evidence for at least three mechanisms by which levels of IgCAMs are regulated during synapse remodeling--activity-dependent regulation of IgCAM clustering by PSD-95-type molecules, IgCAM internalization by MAP kinase pathway activation, and postsynaptic IgCAM exocytosis. These studies offer convincing evidence that synaptic cell adhesion brings about both negative and positive forces that stabilize synapses, while maintaining their ability to change in an activity-dependent manner.
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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 |
Oct
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pubmed:issn |
0959-4388
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
13
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
527-34
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:14630214-Animals,
pubmed-meshheading:14630214-Cell Adhesion Molecules, Neuronal,
pubmed-meshheading:14630214-Drosophila,
pubmed-meshheading:14630214-Drosophila Proteins,
pubmed-meshheading:14630214-Humans,
pubmed-meshheading:14630214-Immunoglobulins,
pubmed-meshheading:14630214-Synapses
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pubmed:year |
2003
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pubmed:articleTitle |
FASt remodeling of synapses in Drosophila.
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pubmed:affiliation |
Department of Neurobiology, University of Massachusetts Medical School, Aaron Lazare Medical Research Building, 364 Plantation Street, Worcester, MA 01605-2324, USA. mary.packard@umassmed.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review
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