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Article

Serine phosphorylation suppresses huntingtin amyloid accumulation by altering protein aggregation properties.

Journal of molecular biology - 23 Nov 2012

Mishra Rakesh, Hoop Cody L, Kodali Ravindra, Sahoo Bankanidhi, van der Wel Patrick C A, Wetzel Ronald

Abstract excerpt

Aggregation of expanded polyglutamine repeat-containing fragments of the huntingtin (htt) protein may play a key role in Huntington's disease. Consistent with this hypothesis, two Ser-to-Asp mutations in the 17-amino-acid N-terminal htt(NT) segment abrogate both visible brain aggregates and disease symptoms in a full-length Q(97) htt mouse model while compromising aggregation kinetics and aggregate morphology in...

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Identifiers

PMID: 22999956
DOI: 10.1016/j.jmb.2012.09.011
PMCID: PMC3488119

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Serine phosphorylation suppresses huntingtin amyloid accumulation by altering protein aggregation properties.PMID 22999956Read ↗

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