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Article

Formation of morphologically similar globular aggregates from diverse aggregation-prone proteins in mammalian cells.

Proceedings of the National Academy of Sciences of the United States of America - 2 Aug 2005

Mukai Hideyuki, Isagawa Takayuki, Goyama Emiko, Tanaka Shuhei, Bence Neil F, Tamura Atsuo, Ono Yoshitaka, Kopito Ron R

Abstract excerpt

Huntington's disease is a progressive neurodegenerative disorder caused by a polyglutamine repeat expansion in the first exon of the huntingtin (Htt) protein. N-terminal Htt peptides with polyglutamine tracts in the pathological range (51-122 glutamines) form high-molecular-weight protein aggregates with fibrillar morphology in vitro, and they form discrete inclusion bodies in a cell-culture model. However, in...

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PMID: 16040812
DOI: 10.1073/pnas.0409283102
PMCID: PMC1182404

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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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Formation of morphologically similar globular aggregates from diverse aggregation-prone proteins in mammalian cells.PMID 16040812Read ↗

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