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Article

Modelling Ser129 phosphorylation inhibits membrane binding of pore-forming alpha-synuclein oligomers.

PloS one - 1 Jan 2014

Nübling Georg Sebastian, Levin Johannes, Bader Benedikt, Lorenzl Stefan, Hillmer Andreas, Högen Tobias, Kamp Frits, Giese Armin

Abstract excerpt

BACKGROUND: In several neurodegenerative diseases, hyperphosphorylation at position Ser129 is found in fibrillar deposits of alpha-synuclein (asyn), implying a pathophysiological role of asyn phosphorylation in neurodegeneration. However, recent animal models applying asyn phosphorylation mimics demonstrated a protective effect of phosphorylation. Since metal-ion induced asyn oligomers were identified as a...

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Identifiers

PMID: 24911099
DOI: 10.1371/journal.pone.0098906
PMCID: PMC4049638

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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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