| pubmed-article:21150333 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21150333 | lifeskim:mentions | umls-concept:C0033164 | lld:lifeskim |
| pubmed-article:21150333 | lifeskim:mentions | umls-concept:C0002716 | lld:lifeskim |
| pubmed-article:21150333 | lifeskim:mentions | umls-concept:C1302234 | lld:lifeskim |
| pubmed-article:21150333 | lifeskim:mentions | umls-concept:C0599219 | lld:lifeskim |
| pubmed-article:21150333 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:21150333 | pubmed:dateCreated | 2011-1-19 | lld:pubmed |
| pubmed-article:21150333 | pubmed:abstractText | The relationship between Alzheimer disease (AD) and prion-related encephalopathies (TSE) has been proposed by different points of view. Recently, the scientific attention has been attracted by the results proposing the possibility that PrPc, the protein whose pathologic form is responsible of TSE, can mediated the toxic effect of ? amyloid (A?) oligomers. The oligomers are considered the culprit of the neurodegenerative process associated to AD, although the pathogenic mechanism activated by these small aggregates remain to be elucidated. In the initial study based on the binding screening PrPc was identified as ligand /receptor of A? oligomers, while long term potentiation (LTP) analysis in vitro and behavioural studies in vivo, demonstrated that the absence of PrPc abolished the damage induced by A? oligomers. The high affinity binding A? oligomers-PrPc has been confirmed, whereas a functional role of this association has been excluded by three different studies. We approached this issue by the direct application of A? oligomers in the brain followed by the behavioural examination of memory deficits. Our data using PrP knock-out mice suggest that A? 1-42 oligomers are responsible for cognitive impairment in AD but PrPc is not required for their effect. Similarly, in two other studies the LTP alterations induced by A? 1-42 oligomers was not influenced by the absence of PrP. Possible explanations of these contradictory results are discussed. | lld:pubmed |
| pubmed-article:21150333 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21150333 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21150333 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:21150333 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21150333 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21150333 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21150333 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21150333 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21150333 | pubmed:issn | 1933-690X | lld:pubmed |
| pubmed-article:21150333 | pubmed:author | pubmed-author:ForloniGianlu... | lld:pubmed |
| pubmed-article:21150333 | pubmed:author | pubmed-author:BalducciClaud... | lld:pubmed |
| pubmed-article:21150333 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21150333 | pubmed:volume | 5 | lld:pubmed |
| pubmed-article:21150333 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21150333 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21150333 | pubmed:pagination | 10-5 | lld:pubmed |
| pubmed-article:21150333 | pubmed:meshHeading | pubmed-meshheading:21150333... | lld:pubmed |
| pubmed-article:21150333 | pubmed:meshHeading | pubmed-meshheading:21150333... | lld:pubmed |
| pubmed-article:21150333 | pubmed:meshHeading | pubmed-meshheading:21150333... | lld:pubmed |
| pubmed-article:21150333 | pubmed:meshHeading | pubmed-meshheading:21150333... | lld:pubmed |
| pubmed-article:21150333 | pubmed:meshHeading | pubmed-meshheading:21150333... | lld:pubmed |
| pubmed-article:21150333 | pubmed:meshHeading | pubmed-meshheading:21150333... | lld:pubmed |
| pubmed-article:21150333 | pubmed:meshHeading | pubmed-meshheading:21150333... | lld:pubmed |
| pubmed-article:21150333 | pubmed:meshHeading | pubmed-meshheading:21150333... | lld:pubmed |
| pubmed-article:21150333 | pubmed:meshHeading | pubmed-meshheading:21150333... | lld:pubmed |
| pubmed-article:21150333 | pubmed:articleTitle | ?-amyloid oligomers and prion protein: Fatal attraction? | lld:pubmed |
| pubmed-article:21150333 | pubmed:affiliation | Biology of Neurodegenerative Diseases Lab, Department of Neuroscience, Mario Negri Institute for Pharmacological Research, Milano, Italy. | lld:pubmed |
| pubmed-article:21150333 | pubmed:publicationType | Journal Article | lld:pubmed |
