Benedikt Frieg

Stochastic Misfolding Drives the Emergence of Distinct α-Synuclein Strains

This study shows that stochastic misfolding leads to the formation of distinct α-synuclein strains both in vitro and in vivo, resulting in different disease phenotypes.

The clinical drug candidate anle138b binds predominantly to the central cavity in lipidic Aβ fibrils and modulates fibril formation.

This paper shows that anle138b binds to a cavity in lipidic Aβ fibrils and reduces fibril formation by 75%, suggesting a potential therapeutic mechanism for Alzheimer's disease.

Structural insight into binding of novel PET tracer MODAG-005 to lipidic ????-Synuclein fibrils

This study identifies two binding sites of the PET tracer MODAG-005 on lipidic α-synuclein fibrils, with the cavity site being more stable and selectively occupied under certain conditions.

Cryo-EM structures of lipidic fibrils of amyloid-β (1-40)

The paper determines the structure of amyloid-β (Aβ40) fibrils bound to lipids using cryo-EM, showing lipid binding and potential relevance to Alzheimer's disease pathogenesis.

Cryo-EM Structures of Amyloid-β Fibrils from Alzheimer's Disease Mouse Models

The paper presents cryo-EM structures of Aβ fibrils from Alzheimer's disease mouse models and compares them to human fibrils.

The 3D structure of lipidic fibrils of α-synuclein

The paper presents six atomic structures of α-synuclein fibrils in the presence of phospholipids, revealing how phospholipids influence fibril morphology and lipid interactions.

α-Synuclein polymorphism determines oligodendroglial dysfunction

This study compares α-synuclein fibril structures from Parkinson's disease and Multiple System Atrophy patients, showing differences in their quaternary arrangement and effects on oligodendroglial cells.