N. Yan

The paper determines cryo-EM structures of low-twist α-synuclein filaments from Lewy bodies and shows they share a structural core with high-twist forms.

This study identifies small molecules that stabilize diverse amyloidogenic immunoglobulin light chains by reducing conformational dynamics and proteolysis.

The paper investigates how phosphorylation at specific sites affects tau self-assembly, finding that S396 and S400 phosphorylation promotes aggregation while T403 and S404 phosphorylation suppresses it, with pS400 forming a CTE protofilament structure.

This study identifies a conserved leucine in the C-terminus of proteasome activators as essential for gate opening of the human 20S proteasome, with structural and functional evidence supporting its role.

This study uses cryo-EM to reveal the conformational landscape of human transthyretin, uncovering asymmetries and new states relevant to ligand binding and amyloid formation.

The paper determines the structure of a novel α-synuclein filament fold in multiple system atrophy using cryo-EM, identifying a new filament type distinct from other synucleinopathies.