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Article

Dissociation of amyloid fibrils of alpha-synuclein and transthyretin by pressure reveals their reversible nature and the formation of water-excluded cavities.

Proceedings of the National Academy of Sciences of the United States of America - 19 Aug 2003

Foguel Débora, Suarez Marisa C, Ferrão-Gonzales Astria D, Porto Thais C R, Palmieri Leonardo, Einsiedler Carla M, Andrade Leonardo R, Lashuel Hilal A, Lansbury Peter T, Kelly Jeffery W, Silva Jerson L

Abstract excerpt

Protein misfolding and aggregation have been linked to several human diseases, including Alzheimer's disease, Parkinson's disease, and systemic amyloidosis, by mechanisms that are not yet completely understood. The hallmark of most of these diseases is the formation of highly ordered and beta-sheet-rich aggregates referred to as amyloid fibrils. Fibril formation by WT transthyretin (TTR) or TTR variants has been...

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Identifiers

PMID: 12900507
DOI: 10.1073/pnas.1734009100
PMCID: PMC187855

Genes

TTR

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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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