Senthil T. Kumar

The paper determines the cryo-EM structure of alpha-synuclein fibrils with the E83Q mutation, revealing structural changes linked to enhanced aggregation and pathogenicity.

This study determines the cryo-EM structures of Aβ40 and medin fibrils in vitro, revealing polymorphic remodeling and mixed amyloid interactions.

The paper develops and validates an expanded antibody panel to capture diverse alpha-synuclein conformations and modifications in Lewy body diseases.

This study shows that nitration of alpha-synuclein after fibrillization reduces its seeding activity and pathology formation in neurons and in vivo.

The paper investigates the effects of the E83Q mutation on alpha-synuclein aggregation and toxicity, finding it accelerates fibrillization and enhances pathological features in neuronal models.

The paper characterizes 16 α-synuclein conformation-specific antibodies using defined preparations of α-synuclein species, finding none are specific to a single species and many recognize fibrils as well as oligomers.

This paper introduces gold nanoparticles labeled with 11-mercapto-1-undecanesulfonate to visualize and characterize amyloid polymorphism using cryo-EM, revealing structural differences between in vivo and in vitro amyloid fibrils.

This paper introduces a centrifugation-based filtration protocol to isolate and quantify α-synuclein monomers, oligomers, and fibrils to improve experimental reproducibility in Parkinson's research.