| pubmed-article:16831301 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16831301 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:16831301 | lifeskim:mentions | umls-concept:C0026377 | lld:lifeskim |
| pubmed-article:16831301 | lifeskim:mentions | umls-concept:C0851827 | lld:lifeskim |
| pubmed-article:16831301 | lifeskim:mentions | umls-concept:C1701901 | lld:lifeskim |
| pubmed-article:16831301 | lifeskim:mentions | umls-concept:C1743872 | lld:lifeskim |
| pubmed-article:16831301 | lifeskim:mentions | umls-concept:C1335533 | lld:lifeskim |
| pubmed-article:16831301 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:16831301 | pubmed:dateCreated | 2006-7-11 | lld:pubmed |
| pubmed-article:16831301 | pubmed:abstractText | The transition of prion protein from a mainly alpha-structured isoform (PrPC) to a beta sheet-containing protein (PrPSc) represents a major pathogenetic mechanism in prion diseases. To study the role of PrP structural conformation in prion-dependent neurodegeneration, we analysed the neurotoxicity of PrP in alpha and beta conformations, using a recombinant protein encompassing amino acids 90-231 of the human PrP (hPrP90-231). Using controlled thermal denaturation (53 degrees C, 1h) we converted hPrP90-231 in a structural isoform displaying PrPSc-related characteristics: high beta sheet content, increased aggregability and a slight increase in the resistance to protease K. In virtue of these structural changes, hPrP90-231 powerfully affected the survival of SH-SY5Y cells, inducing a caspase-3 and p38- dependent apoptosis. Conversely, in the native alpha-helix-rich conformation, hPrP90-231 did not show significant cell toxicity. The relationship between the structural state of hPrP90-231 and its neurotoxicity was demonstrated, inducing the thermal denaturation of the peptide in the presence of Congo red that prevented both the transition of hPrP90-231 into a beta-rich isoform and the acquisition of toxic properties. In conclusion, we report that the toxicity of hPrP90-231 is dependent on its three-dimensional structure, as is supposed to occur for the pathogen PrP during TSE. | lld:pubmed |
| pubmed-article:16831301 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16831301 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16831301 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16831301 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16831301 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16831301 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16831301 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16831301 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16831301 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16831301 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16831301 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16831301 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16831301 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16831301 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16831301 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16831301 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16831301 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16831301 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16831301 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16831301 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16831301 | pubmed:issn | 0394-6320 | lld:pubmed |
| pubmed-article:16831301 | pubmed:author | pubmed-author:Di ColaDD | lld:pubmed |
| pubmed-article:16831301 | pubmed:author | pubmed-author:SchettiniGG | lld:pubmed |
| pubmed-article:16831301 | pubmed:author | pubmed-author:AcetiGG | lld:pubmed |
| pubmed-article:16831301 | pubmed:author | pubmed-author:RussoCC | lld:pubmed |
| pubmed-article:16831301 | pubmed:author | pubmed-author:PatroneEE | lld:pubmed |
| pubmed-article:16831301 | pubmed:author | pubmed-author:BalleriniPP | lld:pubmed |
| pubmed-article:16831301 | pubmed:author | pubmed-author:FlorinUU | lld:pubmed |
| pubmed-article:16831301 | pubmed:author | pubmed-author:D'ArrigoCC | lld:pubmed |
| pubmed-article:16831301 | pubmed:author | pubmed-author:CorsaroAA | lld:pubmed |
| pubmed-article:16831301 | pubmed:author | pubmed-author:VillaVV | lld:pubmed |
| pubmed-article:16831301 | pubmed:author | pubmed-author:ThellungSS | lld:pubmed |
| pubmed-article:16831301 | pubmed:author | pubmed-author:PaludiDD | lld:pubmed |
| pubmed-article:16831301 | pubmed:author | pubmed-author:ChiovittiKK | lld:pubmed |
| pubmed-article:16831301 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16831301 | pubmed:volume | 19 | lld:pubmed |
| pubmed-article:16831301 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16831301 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16831301 | pubmed:pagination | 339-56 | lld:pubmed |
| pubmed-article:16831301 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:16831301 | pubmed:articleTitle | Conformation dependent pro-apoptotic activity of the recombinant human prion protein fragment 90-231. | lld:pubmed |
| pubmed-article:16831301 | pubmed:affiliation | Section of Pharmacology, Dept. Oncology Biology and Genetics, University of Genoa, Viale Benedetto XV 2, 16132 Genoa, Italy. | lld:pubmed |
| pubmed-article:16831301 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16831301 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16831301 | lld:pubmed |
