J. Bieschke

Alanine replacements in the structured C-terminal domain of the prion protein reveal conformationally variable regions as major determinants for prion propagation

This study uses alanine mutagenesis to identify conformationally variable regions in PrPC that are critical for prion propagation.

Loss of the first β-strand of human prion protein generates an aggregation-competent partially "open" form

This study examines the structural and functional changes in a truncated form of human prion protein lacking a conserved membrane region, showing it forms fibrils more readily than the native form.

Syntaxin 6 delays prion protein fibril formation and prolongs presence of toxic aggregation intermediates

This study shows syntaxin-6 inhibits PrP fibril formation but prolongs toxic intermediate aggregates, suggesting it acts as an anti-chaperone in prion disease.

Direct Observation of Competing Prion Protein Fibril Populations with Distinct Structures and Kinetics

This study uses super-resolution microscopy to observe competing prion protein fibril populations with distinct structures and kinetics, revealing their quasi-species behavior.

Brazilin Removes Toxic alpha-Synuclein and Seeding Competent Assemblies from Parkinson Brain by Altering Conformational Equilibrium

This paper shows Brazilin inhibits alpha-synuclein fibril formation and reduces toxicity in Parkinson's disease by altering conformational equilibrium.

Megadalton-sized dityrosine aggregates of α-synuclein retain high degrees of structural disorder and internal dynamics.

This study examines megadalton-sized dityrosine aggregates of α-synuclein, revealing their structural disorder and dynamics, and their role in inhibiting classical amyloid formation.

TDP-43 oligomers detected as initial intermediate species during aggregate formation

This study identifies TDP-43 oligomers as early intermediates in aggregation, showing ALS-linked mutations accelerate this process and enhance aggregate propagation.