Mechanisms of tau self-aggregation and neurotoxicity

G. Farías, A. Cornejo, J. Jiménez, L. Guzmán, R. B. Maccioni

Resultado de la investigación: Contribución a una revistaArtículo

35 Citas (Scopus)


Pathological tau protein aggregates can be found in brain of patients with some of the neurodegenerative diseases collectively known as tauopathies, which include Alzheimer's disease (AD). Since tau post-translational modifications including phosphorylations, glycosylations, truncation and the subsequent aggregation in oligomers, paired helical filaments (PHFs) and neurofibrillary tangles (NFTs), correlate with cognitive impairment and neurodegeneration in AD, a pathogenic role for tau and its modifications has been raised. Here we summarize the current status of knowledge about tau modifications under pathologic conditions and the evidence supporting neurotoxic - or neuroprotective - roles of the diverse forms of modified and aggregated tau. Finally, we analyze the structural and functional tau alterations found in different tauopathies and how these modifications are related to the pathophysiologic mechanisms of neurodegeneration.

Idioma originalInglés
Páginas (desde-hasta)608-614
Número de páginas7
PublicaciónCurrent Alzheimer Research
EstadoPublicada - 1 sep 2011

Áreas temáticas de ASJC Scopus

  • Neurología
  • Neurología clínica

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