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| Description: | Silvia Lisa Ferrer, PhD Instituto de Quimica-Fisica Rocasolano Madrid Spain « Molecular switches in the genesis of pathogenic PrP: methionilsulfoxides and their models » Friday, March 14 2014 13.00-14.00 Room 7A 02 Graduate Studies Building School of Medicine University of Crete (for info contact K. Thermos x4533) Abstract Molecular switches in the genesis of pathogenic PrP: methionilsulfoxides and their models Prion disorders are dominant gain-of-function neurodegenerations whose pathogenesis is linked to misfolded forms of the cellular prion protein (PrPC), including the prion PrPSc and the neurotoxic CtmPrP (1-4). PrPSc is an aggregated and protease resistant β-sheet-enriched conformer of PrPC, which self-perpetuates by the templating the conversion of cell surface PrPC (1,4). In contrast, CtmPrP is an intracellular transmembrane form generated at the ER with neurotoxic properties (1,5,6). The long-standing hypothesis of prion biology is that the distinct biological and physicochemical properties separating PrPC and PrPSc relate only to the conformational differences of the C-terminal domain, which adopts a major globular α-fold in PrPC and displays a high content of β-sheet structure in PrPSc (7,8). However, the populations of PrPC and PrPSc also differ in the redox state the methionines of Helix-3, suggesting a possible role for these residues in facilitating the structural change ADDIN EN.CITE |
| Status: | Waiting for approval |
| Date: | Friday, March 14, 2014 |
| Time: | 13:00-14:00 EET |
| Duration: | 1 hour |
| Priority: | 5-Medium |
| Access: | Public |
| Created by: | Lila Kalogeraki |
| Updated: | Monday, March 10, 2014 09:30 GMT |