Quantitative Morphological Analysis Reveals Ultrastructural Diversity of Amyloid Fibrils from α-Synuclein Mutants
- 1 December 2006
- journal article
- research article
- Published by Elsevier in Biophysical Journal
- Vol. 91 (11) , L96-L98
Abstract
No abstract availableKeywords
This publication has 12 references indexed in Scilit:
- Pathogenic effects of α-synuclein aggregationMolecular Brain Research, 2005
- Neurodegenerative diseases: a decade of discoveries paves the way for therapeutic breakthroughsNature Medicine, 2004
- Mutation E46K increases phospholipid binding and assembly into filaments of human α‐synucleinFEBS Letters, 2004
- Rapid Self-assembly of α-Synuclein Observed by In Situ Atomic Force MicroscopyJournal of Molecular Biology, 2004
- The new mutation, E46K, of α‐synuclein causes parkinson and Lewy body dementiaAnnals of Neurology, 2003
- Protein folding and misfoldingNature, 2003
- A General Model for Amyloid Fibril Assembly Based on Morphological Studies Using Atomic Force MicroscopyBiophysical Journal, 2003
- Unfolding the role of protein misfolding in neurodegenerative diseasesNature Reviews Neuroscience, 2003
- Dependence of α-Synuclein Aggregate Morphology on Solution ConditionsJournal of Molecular Biology, 2002
- Mutation in the α-Synuclein Gene Identified in Families with Parkinson's DiseaseScience, 1997