Parkinson-causing α-synuclein missense mutations shift native tetramers to monomers as a mechanism for disease initiation

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4. Determining the Location of the α-Synuclein Dimer Interface Using Native Top-Down Fragmentation and Isotope Depletion-Mass Spectrometry
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5. Generation of G51D and 3D mice reveals decreased α-synuclein tetramer-monomer ratios promote Parkinson’s disease phenotypes
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6. Aggregation-resistant alpha-synuclein tetramers are reduced in the blood of Parkinson’s patients
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8. Keeping α-Synuclein at Bay: A More Active Role of Molecular Chaperones in Preventing Mitochondrial Interactions and Transition to Pathological States?
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12. Characterization of α-Synuclein Multimer Stoichiometry in Complex Biological Samples by Electrophoresis
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13. Similarity of the non-amyloid-β component and C-terminal tail of monomeric and tetrameric alpha-synuclein with 14-3-3 sigma
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42. Acute introduction of monomeric or multimeric α‐synuclein induces distinct impacts on synaptic vesicle trafficking at lamprey giant synapses
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48. The native form of α‐Synuclein: Monomer, tetramer, or a combination in equilibrium
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