α‐synuclein oligomers and fibrils: a spectrum of species, a spectrum of toxicities

This review article provides an overview of the different species that α‐synuclein aggregates can populate. It also attempts to reconcile conflicting views regarding the cytotoxic roles of oligomers versus fibrils. α‐synuclein, while highly dynamic in the monomeric state, can access a large number o...

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Veröffentlicht in:	Journal of neurochemistry Jg. 150; H. 5; S. 522 - 534
Hauptverfasser:	Alam, Parvez, Bousset, Luc, Melki, Ronald, Otzen, Daniel E.
Format:	Journal Article
Sprache:	Englisch
Veröffentlicht:	England Blackwell Publishing Ltd 01.09.2019 Wiley
Schlagworte:	alpha-Synuclein - chemistry alpha-Synuclein - genetics Amyloid - chemistry Assembly biophysics Coalescing Collapse conformations Cytotoxicity Fibrillogenesis fibrils Heterogeneity Homeostasis Humans Kinetics Lewy Bodies - chemistry Life Sciences Lipid Peroxidation Metals - metabolism Models, Molecular Movement disorders Mutation, Missense Neurobiology Neurodegenerative diseases Neurons and Cognition Oligomers Organic chemistry Oxidation Parkinson's disease Phosphorylation Point Mutation propagation Protein Aggregation, Pathological Protein Conformation Protein Folding Protein Multimerization Protein Processing, Post-Translational Solubility Species Structure-Activity Relationship Synuclein Synucleinopathies - genetics Synucleinopathies - metabolism Thermodynamics Toxicity conformations synuclein propagation biophysics oligomers fibrils
ISSN:	0022-3042, 1471-4159, 1471-4159
Online-Zugang:	Volltext
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