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Article

Mutational analysis of the structural organization of polyglutamine aggregates.

Proceedings of the National Academy of Sciences of the United States of America - 24 Dec 2002

Thakur Ashwani K, Wetzel Ronald

Abstract excerpt

The formation of amyloid-like aggregates by expanded polyglutamine (polyGln) sequences is suspected to play a critical role in the neuropathology of Huntington's disease and other expanded CAG-repeat diseases. To probe the folding of the polyGln sequence in the aggregate, we replaced Gln-Gln pairs at different sequence intervals with Pro-Gly pairs, elements that are compatible with beta-turn formation and...

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Identifiers

PMID: 12444250
DOI: 10.1073/pnas.252523899
PMCID: PMC139261

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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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