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Updated: May 21, 2026

Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
Published on: December 27, 2016
Tau Phosphorylation by GSK3 in Different Conditions
Jesús Avila1, Gonzalo León-Espinosa, Esther García
1Centro de Biologia Molecular "Severo Ochoa" (CSIC-UAM), Nicolás Cabrera 1, Campus Cantoblanco UAM, 28049 Madrid, Spain.
Abstract:
Almost a 20% of the residues of tau protein are phosphorylatable amino acids: serine, threonine, and tyrosine. In this paper we comment on the consequences for tau of being a phosphoprotein. We will focus on serine/threonine phosphorylation. It will be discussed that, depending on the modified residue in tau molecule, phosphorylation could be protective, in processes like hibernation, or toxic like in development of those diseases known as tauopathies, which are characterized by an hyperphosphorylation and aggregation of tau.
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