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Article

E46K Parkinson's-linked mutation enhances C-terminal-to-N-terminal contacts in alpha-synuclein.

Journal of molecular biology - 22 May 2009

Rospigliosi Carla C, McClendon Sebastian, Schmid Adrian W, Ramlall Trudy F, Barré Patrick, Lashuel Hilal A, Eliezer David

Abstract excerpt

Parkinson's disease (PD) is associated with the deposition of fibrillar aggregates of the protein alpha-synuclein (alphaS) in neurons. Intramolecular contacts between the acidic C-terminal tail of alphaS and its N-terminal region have been proposed to regulate alphaS aggregation, and two originally described PD mutations, A30P and A53T, reportedly reduce such contacts. We find that the most recently discovered...

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Identifiers

PMID: 19345692
DOI: 10.1016/j.jmb.2009.03.065
PMCID: PMC2719283

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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