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Article

Ubiquitin is associated with early truncation of tau protein at aspartic acid(421) during the maturation of neurofibrillary tangles in Alzheimer's disease.

Brain pathology (Zurich, Switzerland) - 1 Mar 2012

García-Sierra Francisco, Jarero-Basulto Jose J, Kristofikova Zdena, Majer Emerich, Binder Lester I, Ripova Daniela

Abstract excerpt

Pathological processing of tau protein during the formation and maturation of neurofibrillary tangles (NFTs) includes abnormal phosphorylation, conformational changes and truncation of the C-terminus at aspartic-acid(421) (apoptotic product) and glutamic-acid(391) residues. Abnormal phosphorylation and misfolding may serve as recognition signals for ubiquitin-targeting and proteosomal processing. For this...

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Identifiers

PMID: 21919991
DOI: 10.1111/j.1750-3639.2011.00525.x
PMCID: PMC8029281

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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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