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Article

α-Synucleins from Animal Species Show Low Fibrillation Propensities and Weak Oligomer Membrane Disruption.

Biochemistry - 28 Aug 2018

Sahin Cagla, Kjær Lars, Christensen Mette Solvang, N Pedersen Jannik, Christiansen Gunna, Pérez Adriana-Michelle Wolf, Møller Ian Max, Enghild Jan J, Pedersen Jan S, Larsen Knud, Otzen Daniel E

Abstract excerpt

The intrinsically disordered protein α-synuclein (aSN) forms insoluble aggregates in the brains of Parkinson's disease (PD) patients. Cytotoxicity is attributed to a soluble aSN oligomeric species that permeabilizes membranes significantly more than monomers and fibrils. In humans, the A53T mutation induces early onset PD and increases the level of aSN oligomerization and fibrillation propensity, but Thr53 occurs...

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PMID: 30067901
DOI: 10.1021/acs.biochem.8b00627

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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