W. Hoyer

Phase Separation and Aggregation of α-Synuclein Diverge at Different Salt Conditions

This study investigates how salt concentration affects the phase separation and aggregation of alpha-synuclein, revealing distinct salt dependencies and dynamic transitions between assembly states.

Structural Basis for the Inhibition of IAPP Fibril Formation by the Hsp60 Co-Chaperonin Prefoldin

This study shows how prefoldin inhibits IAPP fibril formation by binding to the N-terminal segment of IAPP on fibril surfaces and ends, reducing aggregate size and number.

Endo-lysosomal Aβ concentration and pH enable formation of Aβ oligomers that potently induce Tau missorting

This study shows that endo-lysosomal pH and Aβ concentration drive Aβ oligomer formation, which induces Tau mislocalization and neuronal dysfunction in Alzheimer's disease.

Amyloid fibril structure of islet amyloid polypeptide by cryo-electron microscopy reveals similarities with amyloid beta

This study uses cryo-EM to reveal the structure of IAPP fibrils, showing similarities with Aβ polymorphs and linking genetic mutations to amyloid formation.

An engineered monomer binding-protein for α-synucleinefficiently inhibits the proliferation of amyloid fibrils

The paper engineers a monomer-binding protein that inhibits α-synuclein fibril proliferation in vitro and in vivo, showing it reduces aggregates and related pathologies.

A structural and kinetic link between membrane association and amyloid fibril formation of α-Synuclein

This study investigates how α-Synuclein interacts with membrane surfaces and how these interactions influence its aggregation into amyloid fibrils.