| pubmed-article:17169463 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17169463 | lifeskim:mentions | umls-concept:C0027882 | lld:lifeskim |
| pubmed-article:17169463 | lifeskim:mentions | umls-concept:C0019564 | lld:lifeskim |
| pubmed-article:17169463 | lifeskim:mentions | umls-concept:C0085103 | lld:lifeskim |
| pubmed-article:17169463 | lifeskim:mentions | umls-concept:C1511625 | lld:lifeskim |
| pubmed-article:17169463 | lifeskim:mentions | umls-concept:C0085151 | lld:lifeskim |
| pubmed-article:17169463 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:17169463 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:17169463 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:17169463 | pubmed:dateCreated | 2008-3-7 | lld:pubmed |
| pubmed-article:17169463 | pubmed:abstractText | The function of the amyloid precursor protein (APP), a key molecule in Alzheimer's disease (AD) remains unknown. Among the proteins that interact with the APP cytoplasmic domain in vitro and in heterologous systems is Disabled-1, a signaling molecule of the reelin pathway. The physiological consequence of this interaction is unknown. Here we used an in vitro model of hippocampal neurons grown on a reelin substrate that inhibits neurite outgrowth. Our results show that an excess of APP cytoplasmic domain internalized by a cell permeable peptide, is able to antagonize the neurite outgrowth inhibition of reelin. The APP cytoplasmic domain binds Disabled-1 and retains it in the cytoplasm, preventing it from reaching the plasma membrane and sequesters tyrosine phosphorylated Disabled-1, both of which disrupt reelin signaling. In the context of AD, increased formation of APP cytoplasmic domain in the cytosol released after cleavage of the A beta peptide, could then inhibit reelin signaling pathway in the hippocampus and thus influence synaptic plasticity. | lld:pubmed |
| pubmed-article:17169463 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17169463 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17169463 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17169463 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17169463 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17169463 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17169463 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17169463 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17169463 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17169463 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17169463 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17169463 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:17169463 | pubmed:issn | 1558-1497 | lld:pubmed |
| pubmed-article:17169463 | pubmed:author | pubmed-author:ProchiantzAA | lld:pubmed |
| pubmed-article:17169463 | pubmed:author | pubmed-author:SorianoEE | lld:pubmed |
| pubmed-article:17169463 | pubmed:author | pubmed-author:AllinquantBB | lld:pubmed |
| pubmed-article:17169463 | pubmed:author | pubmed-author:KrebsM OMO | lld:pubmed |
| pubmed-article:17169463 | pubmed:author | pubmed-author:BorrellVV | lld:pubmed |
| pubmed-article:17169463 | pubmed:author | pubmed-author:HoareauCC | lld:pubmed |
| pubmed-article:17169463 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:17169463 | pubmed:volume | 29 | lld:pubmed |
| pubmed-article:17169463 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17169463 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17169463 | pubmed:pagination | 542-53 | lld:pubmed |
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| pubmed-article:17169463 | pubmed:meshHeading | pubmed-meshheading:17169463... | lld:pubmed |
| pubmed-article:17169463 | pubmed:meshHeading | pubmed-meshheading:17169463... | lld:pubmed |
| pubmed-article:17169463 | pubmed:meshHeading | pubmed-meshheading:17169463... | lld:pubmed |
| pubmed-article:17169463 | pubmed:meshHeading | pubmed-meshheading:17169463... | lld:pubmed |
| pubmed-article:17169463 | pubmed:meshHeading | pubmed-meshheading:17169463... | lld:pubmed |
| pubmed-article:17169463 | pubmed:meshHeading | pubmed-meshheading:17169463... | lld:pubmed |
| pubmed-article:17169463 | pubmed:meshHeading | pubmed-meshheading:17169463... | lld:pubmed |
| pubmed-article:17169463 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:17169463 | pubmed:articleTitle | Amyloid precursor protein cytoplasmic domain antagonizes reelin neurite outgrowth inhibition of hippocampal neurons. | lld:pubmed |
| pubmed-article:17169463 | pubmed:affiliation | INSERM U796, Centre Paul Broca, 2 ter rue d'Alésia, 75014 Paris, France. | lld:pubmed |
| pubmed-article:17169463 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17169463 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:17169463 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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