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Article

The Two Cysteines of Tau Protein Are Functionally Distinct and Contribute Differentially to Its Pathogenicity in Vivo.

The Journal of neuroscience : the official journal of the Society for Neuroscience - 27 Jan 2021

Prifti Engie, Tsakiri Eleni N, Vourkou Ergina, Stamatakis George, Samiotaki Martina, Papanikolopoulou Katerina

Abstract excerpt

Although Tau accumulation is clearly linked to pathogenesis in Alzheimer's disease and other Tauopathies, the mechanism that initiates the aggregation of this highly soluble protein in vivo remains largely unanswered. Interestingly, in vitro Tau can be induced to form fibrillar filaments by oxidation of its two cysteine residues, generating an intermolecular disulfide bond that promotes dimerization and...

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Identifiers

PMID: 33334867
DOI: 10.1523/JNEUROSCI.1920-20.2020
PMCID: PMC7842753

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