Residual Structure and Dynamics in Parkinson's Disease-associated Mutants of α-Synuclein
Open Access
- 1 December 2001
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 276 (49) , 45996-46003
- https://doi.org/10.1074/jbc.m106777200
Abstract
No abstract availableKeywords
This publication has 53 references indexed in Scilit:
- Conformational properties of α-synuclein in its free and lipid-associated states 1 1Edited by P. E. WrightJournal of Molecular Biology, 2001
- 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
- Mutation in the α-Synuclein Gene Identified in Families with Parkinson's DiseaseScience, 1997
- NACP, A Protein Implicated in Alzheimer's Disease and Learning, Is Natively UnfoldedBiochemistry, 1996
- NMRPipe: A multidimensional spectral processing system based on UNIX pipesJournal of Biomolecular NMR, 1995