Enhanced vulnerability to oxidative stress by α-synuclein mutations and C-terminal truncation
- 1 April 2000
- journal article
- Published by Elsevier in Neuroscience
- Vol. 97 (2) , 279-284
- https://doi.org/10.1016/s0306-4522(00)00077-4
Abstract
No abstract availableKeywords
This publication has 24 references indexed in Scilit:
- Both Familial Parkinson's Disease Mutations Accelerate α-Synuclein AggregationJournal of Biological Chemistry, 1999
- Mutant and Wild Type Human α-Synucleins Assemble into Elongated Filaments with Distinct Morphologies in VitroJournal of Biological Chemistry, 1999
- Lewy Bodies Contain Altered α-Synuclein in Brains of Many Familial Alzheimer's Disease Patients with Mutations in Presenilin and Amyloid Precursor Protein GenesPublished by Elsevier ,1998
- Aggregates from mutant and wild‐type α‐synuclein proteins and NAC peptide induce apoptotic cell death in human neuroblastoma cells by formation of β‐sheet and amyloid‐like filamentsFEBS Letters, 1998
- Effects of the mutations Ala30 to Pro and Ala53 to Thr on the physical and morphological properties of α‐synuclein protein implicated in Parkinson's diseaseFEBS Letters, 1998
- Synthetic filaments assembled from C‐terminally truncated α‐synucleinFEBS Letters, 1998
- Ataxin-1 Nuclear Localization and AggregationCell, 1998
- α-Synuclein in filamentous inclusions of Lewy bodies from Parkinson’s disease and dementia with Lewy bodiesProceedings of the National Academy of Sciences, 1998
- AlaSOPro mutation in the gene encoding α-synuclein in Parkinson's diseaseNature Genetics, 1998
- Mutation in the α-Synuclein Gene Identified in Families with Parkinson's DiseaseScience, 1997