pubmed-article:17466415 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17466415 | lifeskim:mentions | umls-concept:C0002395 | lld:lifeskim |
pubmed-article:17466415 | lifeskim:mentions | umls-concept:C1412481 | lld:lifeskim |
pubmed-article:17466415 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
pubmed-article:17466415 | lifeskim:mentions | umls-concept:C0002085 | lld:lifeskim |
pubmed-article:17466415 | lifeskim:mentions | umls-concept:C1538914 | lld:lifeskim |
pubmed-article:17466415 | lifeskim:mentions | umls-concept:C0752046 | lld:lifeskim |
pubmed-article:17466415 | pubmed:issue | 10 | lld:pubmed |
pubmed-article:17466415 | pubmed:dateCreated | 2008-8-18 | lld:pubmed |
pubmed-article:17466415 | pubmed:abstractText | The gamma-secretase complex is a multimeric aspartyl protease which plays a pivotal role in the production of amyloid beta-peptide, the main component of senile plaques in Alzheimer's disease (AD). APH-1a and APH-1b have been recently identified as important subunits of the gamma-secretase complex. We previously studied sequence variations in both genes and their association with AD in a small Italian population. The rare polymorphism c + 651T > G in APH-1b showed a possible interaction with the Apolipoprotein E (APOE) epsilon4 allele in the AD population sample. We extended our genetic analysis to 449 AD patients and 435 controls and, in AD cases, we found a significant interaction (P=0.001) between the allelic variants in the two genes, resulting in a marked increase of the relative risk for AD (OR=28.6). Despite the amino acid substitution does not seem to modify either the intracellular localization or the half-life of APH-1b protein, these data suggest that a cooperative mechanism involving APOE and APH-1b plays a role in the susceptibility to develop AD. | lld:pubmed |
pubmed-article:17466415 | pubmed:language | eng | lld:pubmed |
pubmed-article:17466415 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17466415 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:17466415 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17466415 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17466415 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:17466415 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17466415 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17466415 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:17466415 | pubmed:month | Oct | lld:pubmed |
pubmed-article:17466415 | pubmed:issn | 1558-1497 | lld:pubmed |
pubmed-article:17466415 | pubmed:author | pubmed-author:AlbertiniAlbe... | lld:pubmed |
pubmed-article:17466415 | pubmed:author | pubmed-author:BiunnoIdaI | lld:pubmed |
pubmed-article:17466415 | pubmed:author | pubmed-author:ScarpiniElioE | lld:pubmed |
pubmed-article:17466415 | pubmed:author | pubmed-author:GalimbertiDan... | lld:pubmed |
pubmed-article:17466415 | pubmed:author | pubmed-author:MarianiClaudi... | lld:pubmed |
pubmed-article:17466415 | pubmed:author | pubmed-author:DominiciRober... | lld:pubmed |
pubmed-article:17466415 | pubmed:author | pubmed-author:PoliMauraM | lld:pubmed |
pubmed-article:17466415 | pubmed:author | pubmed-author:GattaLuisa... | lld:pubmed |
pubmed-article:17466415 | pubmed:author | pubmed-author:FinazziDarioD | lld:pubmed |
pubmed-article:17466415 | pubmed:author | pubmed-author:MusiccoMassim... | lld:pubmed |
pubmed-article:17466415 | pubmed:author | pubmed-author:LovatiCarloC | lld:pubmed |
pubmed-article:17466415 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:17466415 | pubmed:volume | 29 | lld:pubmed |
pubmed-article:17466415 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:17466415 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:17466415 | pubmed:pagination | 1494-501 | lld:pubmed |
pubmed-article:17466415 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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pubmed-article:17466415 | pubmed:year | 2008 | lld:pubmed |
pubmed-article:17466415 | pubmed:articleTitle | Interaction between the APOE epsilon4 allele and the APH-1b c + 651T > G SNP in Alzheimer's disease. | lld:pubmed |
pubmed-article:17466415 | pubmed:affiliation | Section of Chemistry, Faculty of Medicine, University of Brescia, viale Europa 11, 25123 Brescia, Italy. | lld:pubmed |
pubmed-article:17466415 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:17466415 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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