Annular Oligomeric Amyloid Intermediates Observed by in Situ Atomic Force Microscopy
Open Access
- 1 June 2004
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 279 (23) , 24452-24459
- https://doi.org/10.1074/jbc.m400004200
Abstract
No abstract availableKeywords
This publication has 35 references indexed in Scilit:
- α-Synuclein, Especially the Parkinson's Disease-associated Mutants, Forms Pore-like Annular and Tubular ProtofibrilsJournal of Molecular Biology, 2002
- Aggregation and neurotoxicity of α-synuclein and related peptidesBiochemical Society Transactions, 2002
- Annular α-Synuclein Protofibrils Are Produced When Spherical Protofibrils Are Incubated in Solution or Bound to Brain-Derived MembranesBiochemistry, 2002
- Amyloid-Beta Peptide Is Toxic to Neurons In Vivo via Indirect MechanismsNeurobiology of Disease, 2002
- Inhibition of Fibrillization and Accumulation of Prefibrillar Oligomers in Mixtures of Human and Mouse α-SynucleinBiochemistry, 2000
- Is there a cause-and-effect relationship between α-synuclein fibrillization and Parkinson’s disease?Nature Cell Biology, 2000
- Review: History of the Amyloid FibrilJournal of Structural Biology, 2000
- Review: Immunoglobulin Light Chain Amyloidosis—The Archetype of Structural and Pathogenic VariabilityJournal of Structural Biology, 2000
- Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapyProceedings of the National Academy of Sciences, 2000
- α-Synuclein in filamentous inclusions of Lewy bodies from Parkinson’s disease and dementia with Lewy bodiesProceedings of the National Academy of Sciences, 1998