Birgit Habenstein

TL;DR: It is shown that the two strains of α-synuclein have different structures, levels of toxicity, and in vitro and in vivo seeding and propagation properties, which may account for differences in disease progression in different individuals/cell types and/or types of synucleinopathies.

TL;DR: In this paper, the authors review what computer, in vitro, in vivo, and pharmacological experiments tell us about the accumulation and deposition of the oligomers of the (Aβ, tau), α-synuclein, IAPP, and superoxide dismutase 1 proteins, which have been the mainstream concept underlying Alzheimer's disease, Parkinson's disease (PD), type II diabetes (T2D), and amyotrophic lateral sclerosis (ALS) research.

TL;DR: Solid-state nuclear magnetic resonance spectroscopy is applied to investigate in vitro assembled PHFs from a truncated three-repeat tau isoform (K19) that represents the core of PHFs and finds that the rigid core of the fibrils is formed by amino acids V306 to S324, only 18 out of 99 residues, and comprises three β-strands connected by two short kinks.

TL;DR: A protocol for the sequential 13C and 15N resonance assignment of uniformly [15N,13C]‐labeled proteins, based on a suite of complementary three‐dimensional solid‐state NMR spectroscopy experiments, directed towards the application to proteins with more than about 100 amino acid residues is presented.

TL;DR: The HeLo-like domain of HELLP is homologous to the pore-forming domain of MLKL, the cell death-execution protein in necroptosis, revealing a transkingdom evolutionary relationship between amyloid-controlled fungal programmed cell death and mammalian necroPTosis.