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.

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

Convergent screens targeting the levels of alpha-synuclein and tau identify TRIM28 as a driver of their stability, nuclear accumulation and subsequent toxicity.

Two new polymorphic structures of recombinant human alpha-synuclein fibrils show striking differences to previous structures, while familial PD mutation sites remain crucial for protofilament interaction and fibril stability.

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

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

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.

The cryo-EM structure of the human N-terminal acetyltransferase NatB bound to a cognate N-terminal alpha-synuclein peptide reveals the molecular determinants of NatB-specific protein acetylation.

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.

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