α-synuclein interacts with SOD1 and promotes its oligomerization
Parkinson’s disease (PD) and amyotrophic lateral sclerosis (ALS) are both neurodegenerative diseases leading to impaired execution of movement. α-Synuclein plays a central role in the pathogenesis of PD whereas Cu, Zn superoxide dismutase (SOD1) is a key player in a subset of familial ALS cases. Und...
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| Main Authors: | , , , , , , , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
08 December 2015
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| In: |
Molecular neurodegeneration
Year: 2015, Volume: 10, Pages: 1-16 |
| ISSN: | 1750-1326 |
| DOI: | 10.1186/s13024-015-0062-3 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1186/s13024-015-0062-3 |
| Author Notes: | Anika M. Helferich, Wolfgang P. Ruf, Veselin Grozdanov, Axel Freischmidt, Marisa S. Feiler, Lisa Zondler, Albert C. Ludolph, Pamela J. McLean, Jochen H. Weishaupt and Karin M. Danzer |
| Summary: | Parkinson’s disease (PD) and amyotrophic lateral sclerosis (ALS) are both neurodegenerative diseases leading to impaired execution of movement. α-Synuclein plays a central role in the pathogenesis of PD whereas Cu, Zn superoxide dismutase (SOD1) is a key player in a subset of familial ALS cases. Under pathological conditions both α-synuclein and SOD1 form oligomers and fibrils. In this study we investigated the possible molecular interaction of α-synuclein and SOD1 and its functional and pathological relevance. |
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| Item Description: | Gesehen am 29.07.2021 |
| Physical Description: | Online Resource |
| ISSN: | 1750-1326 |
| DOI: | 10.1186/s13024-015-0062-3 |