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      α-Synuclein Fibrillogenesis Is Nucleation-dependent : IMPLICATIONS FOR THE PATHOGENESIS OF PARKINSON′S DISEASE

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          Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease.

          Two mutations in the gene encoding alpha-synuclein have been linked to early-onset Parkinson's disease (PD). alpha-Synuclein is a component of Lewy bodies, the fibrous cytoplasmic inclusions characteristic of nigral dopaminergic neurons in the PD brain. This connection between genetics and pathology suggests that the alpha-synuclein mutations may promote PD pathogenesis by accelerating Lewy body formation. To test this, we studied alpha-synuclein folding and aggregation in vitro, in the absence of other Lewy body-associated molecules. We demonstrate here that both mutant forms of alpha-synuclein (A53T and A30P) are, like wild-type alpha-synuclein (WT), disordered in dilute solution. However, at higher concentrations, Lewy body-like fibrils and discrete spherical assemblies are formed; most rapidly by A53T. Thus, mutation-induced acceleration of alpha-synuclein fibril formation may contribute to the early onset of familial PD.
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            The carboxy terminus of the .beta. amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease

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              Neuropathology of Parkinsonʼs Disease

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                Author and article information

                Journal
                Journal of Biological Chemistry
                J. Biol. Chem.
                American Society for Biochemistry & Molecular Biology (ASBMB)
                0021-9258
                1083-351X
                July 09 1999
                July 09 1999
                : 274
                : 28
                : 19509-19512
                Article
                10.1074/jbc.274.28.19509
                5272e728-6077-4711-80b5-02ab0f4feb16
                © 1999
                History

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