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Aggregated tau and alpha-synuclein refer to distinct but often co-occurring protein aggregates found in the brains of patients with neurodegenerative diseases. Tau is normally a soluble microtubule-associated protein, and alpha-synuclein is a presynaptic neuronal protein; under pathological conditions, both undergo misfolding and form insoluble fibrils that propagate in a prion-like manner, drive neurotoxicity, and define tauopathies and synucleinopathies. These aggregates are central to the formation of neurofibrillary tangles (tau) and Lewy bodies (alpha-synuclein), which disrupt cellular proteostasis, mitochondrial function, and synaptic transmission. Therapeutic strategies focus on inhibiting aggregation, cross-seeding, and propagation to slow disease progression[1][2][4][5].
Inhibition of aggregation or fibril formation; Promotion of aggregate clearance via autophagy or proteasome pathways; Blocking cross-seeding between tau and alpha-synuclein aggregates; Immunotherapy targeting extracellular aggregates
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