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Article

Impact of Lysine Acetylation Mutations on the Structure of Full-Length Tau Fibrils.

ACS chemical neuroscience - 16 Jul 2025

Dregni Aurelio J, Hong Mei

Abstract excerpt

The tau protein aggregates into amyloid fibrils in Alzheimer's disease and other neurodegenerative diseases. In these tauopathies, tau is decorated with posttranslational modifications, including phosphorylation and acetylation, suggesting that these modifications may cause tau to aggregate into specific pathological structures. Here, we investigate how pseudoacetylation of three lysine residues, K311Q, K321Q,...

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Identifiers

PMID: 40599054
DOI: 10.1021/acschemneuro.5c00149
PMCID: PMC12917877

Genes

PHF1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

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