SERBP1 is associate with protein complexes regulating splicing, cell division, and ribosomal biogenesis that likely depend on G quadruplex (G4) binding and polyADP-ribosylation (PARylation) for their assembly and function.

Further evidence in support of a new amyloid-independent hypothesis for the pathogenesis of Alzheimer's disease is provided, with an expanded set of Alzheimer-causing mutations in the protease that produces amyloid.

Membrane lipids are involved in the maturation and cytotoxicity of Parkinson's synphilin-1 inclusion bodies.

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.

Genome-wide CRISPRi screens and proteome profiling of lysosomes link lipid dysregulation to ESCRT disruption and proteostasis defect.