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 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.

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

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.

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.

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

Loss of a developmentally essential gene in adulthood is tolerated in mice, thus offering potential therapeutic options for Alzheimer's and Parkinson's disease.

Production of an amyloid protein by bacteria within the gut microbiome can influence the pathophysiology of a mouse model of synucleinopathy.

One α-synuclein strain inhibited proteasome activity and induced apparent pathologies, while the other did not, indicating a strain-dependent toxicity of α-synuclein aggregates, which support a prion-like behavior of α-synuclein.

Inhibitors of seeded propagation of alpha-synuclein may be developed into diagnostics and therapeutics for Parkinson's disease.