Interaction of small molecule expands the conformational ensemble of alpha synuclein.

The alpha-synuclein fibril structure reported here buries residues 50-57 at the interface between its two protofilaments, suggesting that familial Parkinson's disease associated mutations in these residues lead to a structure not compatible with the one presented here.

Alpha-synuclein binding to the synapsin E-domain is essential and sufficient for their cooperation in attenuating synaptic-vesicle trafficking and neurotransmission.

Experiments on synthetic models of synaptic vesicles have shed new light on the role of the protein α-synuclein in the central nervous system.

A combination of physiological, histological, and optical approaches reveals synapse-specific function of α-synuclein in mouse brain under both normal and pathological states.

The high affinity α-synuclein-monomer binder AS69 converts into a strong sub-stoichiometric inhibitor of nucleation processes upon formation of the AS69-α-synuclein complex, achieving reduced aggregation in vitro and in vivo.

The amyloid polymorph selection that occurs during α-synuclein aggregation is dictated by environmental conditions, in particular pH, with the largest variety of structures being observed near neutral pH.

The in-vitro seeded fibrils are unlikely to be disease-relevant and representative of the diverse alpha-synuclein polymorphs in the brain.

A pathway of unconventional secretion for alpha-synuclein, a protein which may spread in the brain as part of the pathology of Parkinson’s disease.

NMR and clustering results show that N-terminal acetylation of α-syn enhances its binding to the neutral phospholipid lysophosphatidylcholine, thereby promoting its function of clustering synaptic vesicles.