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| Content Provider | PubMed Central |
|---|---|
| Author | Winner, Beate Jappelli, Roberto Maji, Samir K. Desplats, Paula A. Boyer, Leah Aigner, Stefan Hetzer, Claudia Loher, Thomas Vilar, Marçal Campioni, Silvia Christos, Tzitzilonis Alice, Soragni Sebastian, Jessberger Mira, Helena Consiglio, Antonella Pham, Emiley Masliah, Eliezer Gage, Fred H. Riek, Roland |
| Abstract | The aggregation of proteins into oligomers and amyloid fibrils is characteristic of several neurodegenerative diseases, including Parkinson disease (PD). In PD, the process of aggregation of α-synuclein (α-syn) from monomers, via oligomeric intermediates, into amyloid fibrils is considered the disease-causative toxic mechanism. We developed α-syn mutants that promote oligomer or fibril formation and tested the toxicity of these mutants by using a rat lentivirus system to investigate loss of dopaminergic neurons in the substantia nigra. The most severe dopaminergic loss in the substantia nigra is observed in animals with the α-syn variants that form oligomers (i.e., E57K and E35K), whereas the α-syn variants that form fibrils very quickly are less toxic. We show that α-syn oligomers are toxic in vivo and that α-syn oligomers might interact with and potentially disrupt membranes. |
| Related Links | http://dx.doi.org/10.1073/pnas.1100976108 |
| Starting Page | 4194 |
| File Format | |
| ISSN | 10916490 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 10 |
| Volume Number | 108 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2011-03-08 |
| Access Restriction | Open |
| Rights Holder | National Academy of Sciences |
| Subject Keyword | Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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