Abstract | BACKGROUND: RESULTS: Using a protein-fragment complementation approach and co-IP, we found that α- synuclein and SOD1 physically interact in living cells, human erythrocytes and mouse brain tissue. Additionally, our data show that disease related mutations in α- synuclein (A30P, A53T) and SOD1 (G85R, G93A) modify the binding of α- synuclein to SOD1. Notably, α- synuclein accelerates SOD1 oligomerization independent of SOD1 activity. CONCLUSION:
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Authors | Anika M Helferich, Wolfgang P Ruf, Veselin Grozdanov, Axel Freischmidt, Marisa S Feiler, Lisa Zondler, Albert C Ludolph, Pamela J McLean, Jochen H Weishaupt, Karin M Danzer |
Journal | Molecular neurodegeneration
(Mol Neurodegener)
Vol. 10
Pg. 66
(Dec 08 2015)
ISSN: 1750-1326 [Electronic] England |
PMID | 26643113
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- SNCA protein, human
- SOD1 protein, human
- Snca protein, mouse
- alpha-Synuclein
- Sod1 protein, mouse
- Superoxide Dismutase
- Superoxide Dismutase-1
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Topics |
- Amyotrophic Lateral Sclerosis
(metabolism)
- Animals
- Brain
(metabolism)
- Humans
- Mice, Transgenic
- Mutation
(genetics)
- Parkinson Disease
(metabolism)
- Protein Multimerization
- Superoxide Dismutase
(metabolism)
- Superoxide Dismutase-1
- alpha-Synuclein
(metabolism)
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