Release and aggregation of cytochrome c and α-synuclein are inhibited by the antiparkinsonian drugs, talipexole and pramipexole
- 1 April 2001
- journal article
- Published by Elsevier in European Journal of Pharmacology
- Vol. 417 (1-2) , 59-67
- https://doi.org/10.1016/s0014-2999(01)00902-5
Abstract
No abstract availableKeywords
Funding Information
- Ministry of Education, Culture, Sports, Science and Technology
This publication has 36 references indexed in Scilit:
- Fiber diffraction of synthetic α-synuclein filaments shows amyloid-like cross-β conformationProceedings of the National Academy of Sciences, 2000
- A Drosophila model of Parkinson's diseaseNature, 2000
- Membrane Association and Protein Conformation of α-Synuclein in Intact NeuronsJournal of Biological Chemistry, 2000
- Dopaminergic Loss and Inclusion Body Formation in α-Synuclein Mice: Implications for Neurodegenerative DisordersScience, 2000
- Synucleins in synaptic plasticity and neurodegenerative disordersJournal of Neuroscience Research, 1999
- α-Synuclein in filamentous inclusions of Lewy bodies from Parkinson’s disease and dementia with Lewy bodiesProceedings of the National Academy of Sciences, 1998
- Stabilization of α-Synuclein Secondary Structure upon Binding to Synthetic MembranesJournal of Biological Chemistry, 1998
- Self‐oligomerization of NACP, the precursor protein of the non‐amyloid β/A4 protein (Aβ) component of Alzheimer's disease amyloid, observed in the presence of a C‐terminal Aβ fragment (residues 25–35)FEBS Letters, 1998
- Protective Effect of Talipexole on MPTP-Treated Planarian, a Unique Parkinsonian Worm ModelThe Japanese Journal of Pharmacology, 1998
- Deficiencies in Complex I subunits of the respiratory chain in Parkinson's diseaseBiochemical and Biophysical Research Communications, 1989