Arthur Alves de Melo

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.

The paper elucidates the structural mechanism of nuclear membrane sealing by LEM2-ESCRT-III through a combination of biochemical and structural methods.

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 reports atomic resolution cryo-EM structures of α-synuclein fibrils from an MSA patient before and after transmission to a transgenic mouse model, showing structural adaptations while maintaining key features.

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 identifies distinct tau filament structures in FTLD-tau caused by the MAPT S305I mutation, revealing a unique 4-layer architecture and potential RNA-like polyanion binding.

This paper designs de novo proteins to modify nanopore complexes, creating customized structural and functional properties for enhanced sequencing applications.

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.