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Fig. 1 | Translational Neurodegeneration

Fig. 1

From: Propagation of tau and α-synuclein in the brain: therapeutic potential of the glymphatic system

Fig. 1

The formation of cytotoxic species of tau and α-synuclein leading to formation of insoluble filaments. a Monomeric forms of these proteins, which are notably soluble, are capable of recruiting and binding to similar structures, giving rise to oligomeric configurations and more complex structures—helical filaments in the case of tau and amyloid fibrils in α-synuclein protein. This process leads to the formation of insoluble aggregates (tau neurofibrillary tangles and α-synuclein Lewy bodies and neurites) which can accumulate intracellularly and lead to cell death. b As indicated by the arrows, the formation of a pathological seed is an energetically unfavourable event, and as such is rare. Once a seed has formed however, monomers of the protein in its natively folded form can change shape and join the initially formed seed in creation of a seeded aggregate. Fragmentation of this aggregate generates new seed forms, accelerating the formation of further aggregates. Recruitment of further monomers/oligomers results in its growth and formation of fibrils (Adapted from Goedert [97])

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