Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 139, Issue 12, Pages 4254-4257Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jacs.6b05335
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Funding
- Deutsche Forschungsgemeinschaft [SFB969, DR 746/10-1]
- Ministry of Science, Research and the Arts of Baden-Wurttemberg [AZ: 33-7532.20/723]
- Conselho Nacional de Desenvolvimento Cientifico e Tecnologico - Brazil (CNPq) [238576/2012-4]
- NWO Physics [FP127]
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The intrinsically disordered human protein alpha-Synudein (alpha S) has a prominent role in Parkinson's disease (PD) pathology. Several familial variants of aS are correlated with inherited PD. Disease mutations have been shown to have an impact on lipid membrane binding. Here, using electron paramagnetic resonance spectroscopy in combination with site-directed spin labeling, we show that familial PD-associated variants are structurally defective in membrane binding and alter the local binding properties of the protein.
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