Structure/function of α‐synuclein in health and disease: rational development of animal models for Parkinson's and related diseases
Open Access
- 24 July 2002
- journal article
- review article
- Published by Wiley in Journal of Neurochemistry
- Vol. 82 (3), 449-457
- https://doi.org/10.1046/j.1471-4159.2002.01020.x
Abstract
No abstract availableKeywords
This publication has 98 references indexed in Scilit:
- Vesicle Permeabilization by Protofibrillar α-Synuclein: Implications for the Pathogenesis and Treatment of Parkinson's DiseaseBiochemistry, 2001
- Conformational properties of α-synuclein in its free and lipid-associated states 1 1Edited by P. E. WrightJournal of Molecular Biology, 2001
- α-Synuclein Membrane Interactions and Lipid SpecificityJournal of Biological Chemistry, 2000
- Fiber diffraction of synthetic α-synuclein filaments shows amyloid-like cross-β conformationProceedings of the National Academy of Sciences, 2000
- Mice Lacking α-Synuclein Display Functional Deficits in the Nigrostriatal Dopamine SystemNeuron, 2000
- Binding of α-Synuclein to Brain Vesicles Is Abolished by Familial Parkinson's Disease MutationJournal of Biological Chemistry, 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
- Stabilization of α-Synuclein Secondary Structure upon Binding to Synthetic MembranesJournal of Biological Chemistry, 1998
- AlaSOPro mutation in the gene encoding α-synuclein in Parkinson's diseaseNature Genetics, 1998
- NACP, A Protein Implicated in Alzheimer's Disease and Learning, Is Natively UnfoldedBiochemistry, 1996