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Article

High-Pressure-Driven Reversible Dissociation of α-Synuclein Fibrils Reveals Structural Hierarchy.

Biophysical journal - 17 Oct 2017

Piccirilli Federica, Plotegher Nicoletta, Ortore Maria Grazia, Tessari Isabella, Brucale Marco, Spinozzi Francesco, Beltramini Mariano, Mariani Paolo, Militello Valeria, Lupi Stefano, Perucchi Andrea, Bubacco Luigi

Abstract excerpt

The analysis of the α-synuclein (aS) aggregation process, which is involved in Parkinson's disease etiopathogenesis, and of the structural feature of the resulting amyloid fibrils may shed light on the relationship between the structure of aS aggregates and their toxicity. This may be considered a paradigm of the ground work needed to tackle the molecular basis of all the protein-aggregation-related diseases....

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 29045863
DOI: 10.1016/j.bpj.2017.08.042
PMCID: PMC5647593

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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