David Eliezer

The paper provides methods for site-specific post-translational modification of alpha-synuclein and tau using genetic code expansion and enzymatic approaches, enabling studies of their structural dynamics and aggregation.

The paper identifies amyloid fibril structures of CHCHD10 and links them to neurodegeneration, showing sequence differences between CHCHD10 and CHCHD2 allow co-aggregation.

This study investigates the structural and dynamic diversity of metabotropic glutamate receptor/beta-arrestin coupling using biophysical and structural methods, revealing new coupling stoichiometries and interaction mechanisms.

This study investigates how acetylation of specific lysine sites in α-synuclein affects aggregation and function, identifying K80 acetylation as a potential therapeutic target.

The paper identifies PGK1 as a rate-limiting enzyme in axonal metabolism and shows its protective role against Parkinson's disease-related synaptic deficits.

This study shows that beta-synuclein and gamma-synuclein modulate alpha-synuclein's membrane binding and synaptic function, but not its downstream roles in vesicle clustering and SNARE-complex assembly.

This study identifies lysine succinylation as a post-translational modification linked to amyloid and tau pathology in Alzheimer's disease through human brain and mouse model analyses.