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Article

Sumoylation inhibits alpha-synuclein aggregation and toxicity.

The Journal of cell biology - 11 Jul 2011

Krumova Petranka, Meulmeester Erik, Garrido Manuel, Tirard Marilyn, Hsiao He-Hsuan, Bossis Guillaume, Urlaub Henning, Zweckstetter Markus, Kügler Sebastian, Melchior Frauke, Bähr Mathias, Weishaupt Jochen H

Abstract excerpt

Posttranslational modification of proteins by attachment of small ubiquitin-related modifier (SUMO) contributes to numerous cellular phenomena. Sumoylation sometimes creates and abolishes binding interfaces, but increasing evidence points to another role for sumoylation in promoting the solubility of aggregation-prone proteins. Using purified α-synuclein, an aggregation-prone protein implicated in Parkinson's...

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Identifiers

PMID: 21746851
DOI: 10.1083/jcb.201010117
PMCID: PMC3135405

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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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